| Number |
Title |
Comments |
| ...1... |
- The role of glucosamine sulfate and chondroitin sulfates in the treatment of
degenerative joint disease.
|
|
| ...2... |
- Danaparoid. A review of its pharmacology and clinical use in the management
of heparin-induced thrombocytopenia.
|
|
| ...3... |
- College of American Pathologists Conference XXXI on laboratory monitoring of
anticoagulant therapy: the clinical use and laboratory monitoring of
low-molecular-weight heparin, danaparoid, hirudin and related compounds, and
argatroban.
|
|
| ...4... |
- Danaparoid in the prevention of thromboembolic complications.
|
|
| ...5... |
- A comparative review of the adverse effect profiles of heparins and
heparinoids.
|
|
| ...6... |
- Characterization of appican, the chondroitin sulfate proteoglycan form of
the Alzheimer amyloid precursor protein.
|
|
| ...7... |
- Immunology of chondroitin/dermatan sulfate.
|
|
| ...8... |
- Thrombomodulin as a model of molecular mechanisms that modulate protease
specificity and function at the vessel surface.
|
|
| ...9... |
- CD44 in inflammation and metastasis.
|
|
| ...10... |
- Pathogenesis and therapy of neuropathies associated with monoclonal
gammopathies.
|
|
| Menu
Position #10 |
| ...11... |
- MHC class II antigen processing: biology of invariant chain.
|
|
| ...12... |
- Effects of cryopreservation upon vein function in vivo.
|
|
| ...13... |
- Update on chemonucleolysis.
|
|
| ...14... |
- New antithrombotic agents for the prevention and treatment of deep vein
thrombosis.
|
|
| ...15... |
- Cell surface chondroitin sulfate proteoglycans in tumor cell adhesion,
motility and invasion.
|
|
| ...16... |
- Heparinoid anticoagulation and topical fibrin sealant in heparin-induced
thrombocytopenia.
|
|
| ...17... |
- Glycosaminoglycans: structure and interaction.
|
|
| ...18... |
- Mechanisms for the anticoagulant effect of heparin and related
polysaccharides.
|
|
| ...19... |
- Mucosal mast cells in the rat and in man.
|
|
| ...20... |
- Viscoelastic agents.
|
|
| Menu
Position #20 |
| ...21... |
- Keratan sulphate--a 'reserve' polysaccharide?
|
|
| ...22... |
- Structure-function relationships of the thrombin-thrombomodulin interaction.
|
|
| ...23... |
- The structure, function and turnover of aggrecan, the large aggregating
proteoglycan from cartilage.
|
|
| ...24... |
- Mapping of proteoglycans in atherosclerotic lesions.
|
|
| ...25... |
- Mesangial cell proteoglycans: synthesis and metabolism.
|
|
| ...26... |
- Advances in corneal preservation.
|
This study describes how a "mixture" based on
chondroitin is so "alive" that a eye-ball not only stays alive
in it, but grows -- while awaiting transplantation! |
| ...27... |
- Chondroitin sulfate proteoglycans as mediators of axon growth and
pathfinding.
|
|
| ...28... |
- Chondroprotection with chondroitin sulfate.
|
|
| ...29... |
- Neurocan and phosphacan: two major nervous tissue-specific chondroitin
sulfate proteoglycans.
|
|
| ...30... |
- Arterial wall proteoglycans--biological properties related to pathogenesis
of atherosclerosis.
|
|
| Menu
Position #30 |
| ...31... |
- Proteoglycans and cell adhesion. Their putative role during tumorigenesis.
|
|
| ...32... |
- Glycosaminoglycan chondroprotection: pharmacological vistas.
|
|
| ...33... |
- Angiogenesis in wound healing and tumor metastasis.
|
|
| ...34... |
- C1q inhibitor (chondroitin-4-sulfate proteoglycan): structure and function.
|
|
| ...35... |
- Molecular events that control the protein C anticoagulant pathway.
|
|
| ...36... |
- Hair follicle proteoglycans.
|
|
| ...37... |
- Altered proteoglycan gene expression and the tumor stroma.
|
|
| ...38... |
- Molecular cloning and analysis of the protein modules of aggrecans.
|
|
| ...39... |
- Roles of aggrecan, a large chondroitin sulfate proteoglycan, in cartilage
structure and function.
|
|
| ...40... |
- Hydrocephalus, lumbar canal stenosis and Maroteaux-Lamy syndrome (mucopolysaccharidosis type 6). Case report.
|
|
| Menu
Position #40 |
| ...41... |
- Overview of the corneal toxicity of surgical solutions and drugs: and
clinical concepts in corneal edema.
|
|
| ...42... |
- The chemical morphology of the vitreous.
|
|
| ...43... |
- Analysis of glycosaminoglycans and their oligosaccharide fragments by
capillary electrophoresis.
|
|
| ...44... |
- Inhibitory molecules in development and regeneration.
|
|
| ...45... |
- Proteoglycans: the "Teflon" of the airways?
|
|
| ...46... |
- Proteoglycans in male reproductive tract.
|
|
| ...47... |
- Regulation of proteoglycan expression in fibrotic liver and cultured
fat-storing cells.
|
|
| ...48... |
- Activation of proteoglycan synthesis in injured liver--a brief review of
molecular and cellular aspects.
|
|
| ...49... |
- Molecular cloning and analysis of the protein modules of aggrecans.
|
|
| ...50... |
- Altered proteoglycan gene expression and the tumor stroma.
|
|
| Menu
Position #50 |
| ...51... |
- CD44: structure, function, and association with the malignant process.
|
|
| ...52... |
- Basement membranes and pulmonary development.
|
|
| ...53... |
- Functions of brain chondroitin sulfate proteoglycans during developments:
interactions with adhesion molecules.
|
|
| ...54... |
- The NG2 chondroitin sulfate proteoglycan: a multifunctional proteoglycan
associated with immature cells.
|
|
| ...55... |
- Viscoelastic substances in ophthalmology.
|
|
| ...56... |
- Glycosaminoglycans in autoimmunity.
|
|
| ...57... |
- Adhesion molecules in neural crest development.
|
|
| ...58... |
- Functional domains of the human C1q A-chain.
|
|
| ...59... |
- The mast cell--a potential link between inflammation and cellular
cholesterol deposition in atherogenesis.
|
|
| ...60... |
- Effects of extracellular matrix components on cell locomotion.
|
|
| Menu
Position #60 |
| ...61... |
- Proteoglycans and the modulation of cell adhesion by steric exclusion.
|
|
| ...62... |
- Proteoglycans of basement membranes.
|
|
| ...63... |
- Small proteoglycans.
|
|
| ...64... |
- The link proteins.
|
|
| ...65... |
- Genetic defects in proteoglycan biosynthesis.
|
|
| ...66... |
- Association of apo B lipoproteins with arterial proteoglycans: pathological
significance and molecular basis.
|
|
| ...67... |
- The role of the invariant chain in mucosal immunity.
|
|
| ...68... |
- Biological activities and clinical application of M-CSF.
|
|
| ...69... |
- Proteoglycans in cell regulation.
|
|
| ...70... |
- Maternal malaria and parasite adhesion.
|
|
| Menu
Position #70 |
| ...71... |
- Lipoprotein (a) regulates plasmin generation and inhibition.
|
|
| ...72... |
- Proteoglycans of basement membranes.
|
|
| ...73... |
- Proteoglycans: many forms and many functions.
|
|
| ...74... |
- Neuropathies associated with monoclonal gammapathies [see comments]
|
|
| ...75... |
- The biology and action of colony stimulating factor-1.
|
|
| ...76... |
- The clinical role of immunoscintigraphy for the detection of ocular
melanoma.
|
|
| ...77... |
- Facilitatory and inhibitory effects of glial cells and extracellular matrix
in axonal regeneration.
|
|
| ...78... |
- Investigational approaches to pulmonary hypertension.
|
|
| ...79... |
- A role for glycosaminoglycans in the development of collagen fibrils.
|
|
| ...80... |
- Cartilage proteoglycans: structure and potential functions.
|
|
| Menu
Position #80 |
| ...81... |
- Mechanisms of astrocyte-directed neurite guidance.
|
|
| ...82... |
- Experimental and clinical pharmacology of glycosaminoglycans (GAGs).
|
|
| ...83... |
- The role of heparan sulfate proteoglycans in the pathogenesis of Alzheimer's
disease.
|
|
| ...84... |
- Small proteoglycans.
|
|
| ...85... |
- The link proteins.
|
|
| ...86... |
- Proteoglycans and hyaluronan in female reproductive organs.
|
|
| ...87... |
- Structure and biological functions of keratan sulfate proteoglycans.
|
|
| ...88... |
- Thrombomodulin structure and function.
|
|
| ...89... |
- x82p4and the adhesion of neoplastic cells.
|
|
| ...90... |
- Thrombin specificity.
|
|
| Menu
Position #90 |
| ...91... |
- Syndecan, a developmentally regulated cell surface proteoglycan that binds
extracellular matrix and growth factors.
|
|
| ...92... |
- Plasmalogens, phospholipases A2 and signal transduction.
|
|
| ...93... |
- Cell-extracellular matrix interactions in the ductus arteriosus and
perinatal pulmonary circulation.
|
|
| ...94... |
- Brevican: a major proteoglycan in adult brain.
|
|
| ...95... |
- Brain aggrecan.
|
|
| ...96... |
- Versican.
|
|
| ...97... |
- Biology and action of colony--stimulating factor-1.
|
|
| ...98... |
- Pheno- and genotypic characteristics of human non-Hodgkin lymphoma
xenografts.
|
|
| ...99... |
- The small proteoglycans of cartilage matrix.
|
|
| ...100... |
- Clinical implications of cartilage metabolism in arthritis.
|
|
|
|
|
| Menu
Position #100 |
NLM database Documents

Record 1 from database: MEDLINE
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- Title
- The role of glucosamine sulfate and chondroitin sulfates in the treatment of
degenerative joint disease.
- Author
- Kelly GS
- Address
-
- Source
- Altern Med Rev, 1998 Feb, 3:1, 27-39
- Abstract
- Successful treatment of osteoarthritis must effectively control pain, and
should slow down or reverse progression of the disease. Biochemical and
pharmacological data combined with animal and human studies demonstrate
glucosamine sulfate is capable of satisfying these criteria. Glucosamine
sulfate's primary biological role in halting or reversing joint degeneration
appears to be directly due to its ability to act as an essential substrate for,
and to stimulate the biosynthesis of, the glycosaminoglycans and the hyaluronic
acid backbone needed for the formation of proteoglycans found in the structural
matrix of joints. Chondroitin sulfates, whether they are absorbed intact or
broken into their constituent components, similarly provide additional
substrates for the formation of a healthy joint matrix. Evidence also supports
the oral administration of chondroitin sulfates for joint disease, both as an
agent to slowly reduce symptoms and to reduce the need for non-steroidal
anti-inflammatory drugs. The combined use of glucosamine sulfate and chondroitin
sulfates in the treatment of degenerative joint disease has become an extremely
popular supplementation protocol in arthritic conditions of the joints. Although
glucosamine sulfate and chondroitin sulfates are often administered together,
there is no information available to demonstrate the combination produces better
results than glucosamine sulfate alone.
- Language of Publication
- English
- Unique Identifier
- 98262758
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- MeSH Heading (Major)
- Chondroitin Sulfates|CH/ME/*TU; Glucosamine|ME/*TU; Osteoarthritis|*DT
- MeSH Heading
- Drug Therapy, Combination; Human

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 1089-5159
- Country of Publication
- UNITED STATES


Record 2 from database: MEDLINE
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- Title
- Danaparoid. A review of its pharmacology and clinical use in the management
of heparin-induced thrombocytopenia.
- Author
- Wilde MI; Markham A
- Address
- Adis International Limited, Auckland, New Zealand. demail@adis.co.nz
- Source
- Drugs, 1997 Dec, 54:6, 903-24
- Abstract
- Danaparoid, a low molecular weight heparinoid consisting of a mixture of
heparan, dermatan and chondroitin sulfates, has well established antithrombotic
activity. The drug has a high antifactor Xa to antifactor IIa (thrombin)
activity ratio, a low tendency to cause bleeding and minimal effects on the
fibrinolytic system. Danaparoid has a low cross-reactivity rate with
heparin-associated antiplatelet antibodies (0 to 20%; mean approximately 10%).
This represents a significant advantage over low molecular weight heparins
(LMWHs) as a potential replacement agent for unfractionated heparin (UFH) in
patients with immune-mediated (type II) heparin-induced thrombocytopenia (HIT).
In a worldwide compassionate-use programme involving a total of 667 patients
with HIT to date, 93% of danaparoid treatment courses were considered to be
successful. Thrombocytopenia resolved in 91% of episodes. In a multicentre
randomised comparative trial of danaparoid and dextran in patients with HIT plus
thrombosis (HITT), significantly more danaparoid than dextran recipients had
resolution of thromboses, and an effective clinical response was achieved in
significantly more danaparoid recipients. Results of a retrospective
case-controlled study of danaparoid and ancrod in patients with HITT showed
significantly fewer new or progressive thromboses with danaparoid. In the
compassionate-use programme, danaparoid was associated with a mortality rate of
10.4% during treatment (up to 3.5 years) and 7.8% during the follow-up period (3
months). 14 of 114 deaths during the follow-up period were considered to be
related to danaparoid therapy. A mortality rate of 23.5% was reported in
patients accepted for but not treated with, danaparoid. Mortality rates with
danaparoid, ancrod and dextran in the comparative studies were similar (7, 11
and 12%, respectively). Severe bleeding was reported in 3.1% of patients in the
compassionate-use programme, persistent or recurrent thrombocytopenia in 2.6%
and new thromboembolic events/extension of existing thrombosis in 1.7%. The
incidence of bleeding was similar with danaparoid and dextran in a comparative
trial. Although in vitro cross-reactivity does not always translate into
clinical cross-reactivity, testing is currently recommended, when possible,
before initiation of danaparoid therapy. Thus, danaparoid appears to be an
effective and well tolerated replacement agent for UFH in many patients with HIT
who require further anticoagulation. The drug has low cross-reactivity with
HIT-associated antibodies. Further comparative trials are needed to confirm
these promising findings.
- Language of Publication
- English
- Unique Identifier
- 98083474
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- MeSH Heading (Major)
- Chondroitin Sulfates|AE/*PD/PK/*TU; Dermatan Sulfate|AE/*PD/PK/*TU;
Heparitin Sulfate|AE/*PD/PK/*TU; Thrombocytopenia|CI/*DT/PP
- MeSH Heading
- Blood Coagulation|DE; Drug Combinations; Heparin|AE;
Heparinoids|AE/PD/PK/TU; Human

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0012-6667
- Country of Publication
- NEW ZEALAND


Record 3 from database: MEDLINE
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- Title
- College of American Pathologists Conference XXXI on laboratory monitoring of
anticoagulant therapy: the clinical use and laboratory monitoring of
low-molecular-weight heparin, danaparoid, hirudin and related compounds, and
argatroban.
- Author
- Laposata M; Green D; Van Cott EM; Barrowcliffe TW; Goodnight SH; Sosolik RC
- Address
- Division of Laboratory Medicine, Massachusetts General Hospital, Boston
02114, USA.
- Source
- Arch Pathol Lab Med, 1998 Sep, 122:9, 799-807
- Abstract
- OBJECTIVE: To review the role of the laboratory in monitoring therapy with
low-molecular-weight heparin, danaparoid, hirudin, and argatroban, as reflected
in the medical literature and the consensus opinion of recognized experts in the
field. DATA SOURCES: Review of the medical literature and current clinical
practice by a panel of 6 international experts in the field of anticoagulant
therapy. DATA EXTRACTION AND SYNTHESIS: The experts made an extensive review of
the published literature and prepared a draft manuscript, which included
preliminary recommendations. The draft manuscript was circulated to participants
in the College of American Pathologists Conference XXXI on Laboratory Monitoring
of Anticoagulant Therapy prior to the conference. The manuscript and
recommendations were then presented at the Conference for discussion.
Recommendations were accepted if a consensus of the 26 experts attending the
Conference was reached. The results of the discussion were used to revise the
manuscript into its final form. CONCLUSIONS: This report reviews the mechanism
of action and potential uses of these newer anticoagulant agents. General
guidelines for monitoring these agents and 9 specific recommendations for
laboratory monitoring of low-molecular-weight heparin and danaparoid are
provided, along with citation of the appropriate supporting literature. Issues
for which a consensus was not reached at the Conference are also discussed.
- Language of Publication
- English
- Unique Identifier
- 98410853
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- MeSH Heading (Major)
- Anticoagulants|AD/*TU
- MeSH Heading
- Chondroitin Sulfates|AD/TU; Dermatan Sulfate|AD/TU; Drug Combinations; Drug
Monitoring|MT; Heparin|AD/TU; Heparin, Low-Molecular-Weight|AD/TU; Heparitin
Sulfate|AD/TU; Hirudin|AA/AD/TU; Human; Pathology, Clinical|MT; Pipecolic
Acids|AD/TU; Thromboembolism|BL/DT

- Publication Type
- CONSENSUS DEVELOPMENT CONFERENCE; GUIDELINE; JOURNAL ARTICLE; PRACTICE
GUIDELINE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0003-9985
- Country of Publication
- UNITED STATES
- CAS Registry/EC Number
- 0 (danaparoid); 0 (Anticoagulants); 0 (Drug Combinations); 0 (Heparin,
Low-Molecular-Weight); 0 (Pipecolic Acids); 24967-94-0 (Dermatan Sulfate);
74863-84-6 (Argatroban); 8001-27-2 (Hirudin); 9005-49-6 (Heparin); 9007-28-7
(Chondroitin Sulfates); 9050-30-0 (Heparitin Sulfate)


Record 4 from database: MEDLINE
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- Title
- Danaparoid in the prevention of thromboembolic complications.
- Author
- Skoutakis VA
- Address
- National Pharmacotherapy Institute, Germantown, TN 38183, USA.
- Source
- Ann Pharmacother, 1997 Jul, 31:7-8, 876-87
- Abstract
- OBJECTIVE: To review the therapies used to prevent postoperative
thromboembolic complications with a focus on the role of danaparoid, a new
low-molecular-weight glycosaminoglycan. DATA SOURCES: A MEDLINE search was
performed to identify pertinent English-language literature including studies,
abstracts, and review articles. Key search terms included danaparoid,
heparinoid, lomoparin, heparin, prophylaxis, thrombosis, embolism,
thromboembolism, and thromboembolic and postoperative complications. The
manufacturer of danaparoid was contracted for additional information related to
this compound. STUDY SELECTION AND DATA EXTRACTION: All identified articles were
reviewed for possible inclusion in this review. Comparisons primarily focused on
data obtained from prospective, randomized, controlled, blind clinical trials.
Another important consideration was the use of venography to determine the
presence of deep venous thrombosis. DATA SYNTHESIS: Various therapies are
available for the prevention of postoperative thromboembolic complications.
Effective pharmacologic treatments currently available include adjusted-dose
heparin, warfarin, aspirin, dextran, and low-molecular-weight heparins (LMWHs).
Until recently, warfarin was considered the drug of choice for
thromboprophylaxis in high-risk patients, including patients undergoing
orthopedic surgical procedures. Because of their comparable efficacy and greater
ease of use, LMWHs are gaining favor over warfarin in this patient population.
In well-designed clinical trials involving patients undergoing elective total
hip replacement or fractured hip surgery, danaparoid has demonstrated greater
efficacy than other active treatments, including warfarin, dextran, aspirin, and
heparin plus dihydroergotamine. While studies comparing danaparoid with LMWHs
have not yet been published, danaparoid may be more useful in patients with
heparin-associated thrombocytopenia. CONCLUSIONS: Danaparoid is an
antithrombotic agent with characteristics that distinguish it from heparin and
LMWHs. Based on the efficacy and safety data reviewed, danaparoid should be
considered one of the drugs of choice for the prevention of thromboembolic
complications in patients undergoing orthopedic hip procedures and the drug of
choice for the management of any patient with heparin-induced thrombocytopenia
who requires anticoagulant therapy.
- Language of Publication
- English
- Unique Identifier
- 97363759
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- MeSH Heading (Major)
- Chondroitin Sulfates|CH/PD/*TU; Dermatan Sulfate|CH/PD/*TU;
Heparin|CH/PD/*TU; Heparitin Sulfate|CH/PD/*TU; Postoperative Complications|*PC;
Thromboembolism|*PC
- MeSH Heading
- Drug Combinations; Human; Randomized Controlled Trials

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 1060-0280
- Country of Publication
- UNITED STATES


Record 5 from database: MEDLINE
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- Title
- A comparative review of the adverse effect profiles of heparins and
heparinoids.
- Author
- Borris LC; Lassen MR
- Address
- Department of Orthopaedics, Aalborg Hospital, Denmark.
- Source
- Drug Saf, 1995 Jan, 12:1, 26-31
- Abstract
- On the basis of the results of the 11 studies reviewed, thromboprophylaxis
with unfractionated heparin, low molecular weight (LMW) heparin or a heparinoid
(danaparoid sodium; Org 10172) in patients undergoing total hip replacement did
not show any important clinical differences with respect to the tolerability
profiles of the different compounds. However, as a result of the great
variability in the presentation and evaluation of blood losses and bleeding
complications in these studies, it is mandatory to perform a direct comparison
of the different compounds in question in a double-blind, prospective clinical
study.
- Language of Publication
- English
- Unique Identifier
- 95260439
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- MeSH Heading (Major)
- Chondroitin Sulfates|AD/*AE/TU; Dermatan Sulfate|AD/*AE/TU; Fibrinolytic
Agents|AD/*AE/TU; Heparin|AD/*AE/TU; Heparinoids|AD/*AE/TU; Heparitin
Sulfate|AD/*AE/TU
- MeSH Heading
- Comparative Study; Hemorrhage|CI; Hip Prosthesis; Human; Molecular Weight;
Postoperative Complications|CI; Thrombocytopenia|CI; Thrombosis|PC; Wound
Infection|CI

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0114-5916
- Country of Publication
- NEW ZEALAND


Record 6 from database: MEDLINE
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- Title
- Characterization of appican, the chondroitin sulfate proteoglycan form of
the Alzheimer amyloid precursor protein.
- Author
- Pangalos MN; Shioi J; Efthimiopoulos S; Wu A; Robakis NK
- Address
- Department of Psychiatry, Mount Sinai School of Medicine, New York, NY
10029, USA.
- Source
- Neurodegeneration, 1996 Dec, 5:4, 445-51
- Abstract
- In this report we focus on the characterization of appican, the chondroitin
sulfate proteoglycan form of amyloid precursor protein (APP), and the role that
it and other proteoglycans may play in AD. Appican is expressed by certain
transformed cell lines of neural origin, namely C6 cells and N2a neuroblastomas.
It is detected in both human and rat brain and in primary cultures is expressed
by astrocytes, but not neurons. The core protein of appican has been shown to be
an alternatively spliced isoform of APP, lacking exon 15 of the APP gene,
originally identified in leukocytes (L-APP). Splicing out of exon 15 results in
the joining of exons 14 and 16, and formation of an Asp-Xaa-Ser-Gly consensus
sequence for chondroitin sulfate chain attachment to serine 619 of L-APP, which
lies 16 amino acids upstream of the A beta peptide sequence. Mutation of this
serine residue to an alanine prevented chondroitin sulfate chain addition to the
core protein. Levels of appican expression could be regulated by growth
conditions independently of APP, suggesting that these molecules may serve
distinct physiological roles within the cell. Morphological changes were also
observed in both astrocytic and transformed cell cultures, that appeared to
reflect changes in levels of appican expression. Preliminary data suggest that
appican may be a strong cell adhesion molecule. Transfected C6 glioma cells
overexpressing appican remained attached to tissue culture dishes markedly
better than either C6 cells over-expressing exon-15 containing APP or WT C6
cells. Appican-enriched extracellular matrix (ECM) was also observed to serve as
a much better substrate for attachment of N2a neuroblastomas, pheocromocytoma
PC12 cells and primary astrocytes compared to APP enriched ECM.
- Language of Publication
- English
- Unique Identifier
- 97179581
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- MeSH Heading (Major)
- Alzheimer Disease|*ME/PP; Amyloid beta-Protein Precursor|GE/ME/*PH;
Proteochondroitin Sulfates|*PH; Proteoglycans|ME/*PH
- MeSH Heading
- Amino Acid Sequence; Animal; Chondroitin Sulfates|ME; Human; Molecular
Sequence Data

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 1055-8330
- Country of Publication
- ENGLAND


Record 7 from database: MEDLINE
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- Title
- Immunology of chondroitin/dermatan sulfate.
- Author
- Hascall VC; Midura RJ; Sorrell JM; Plaas AH
- Address
- Department of Biomedical Engineering, Cleveland Clinic Foundation, Ohio,
USA.
- Source
- Adv Exp Med Biol, 1995, 376:, 205-16
- Abstract
- Variable substitutions and locations of the sulfate esters along the
backbone of chondroitin/dermatan sulfate chains, combined with their
carbohydrate structures, present topographies to immune systems which can be
recognized as antigenic. This has led to the development of a number of
monoclonal antibodies which recognize distinct epitopes in the native structures
of these glycosaminoglycan chains. In some studies, the original
chondroitin/dermatan sulfate proteoglycan was digested with chondroitinase
enzymes before being used as an immunogen. in this case, the linkage
oligosaccharides remaining bound to the core protein contain a modified
(4,5-unsaturated) hexuronic acid derivative at their non-reducing ends as a
result of the eliminase mechanism of the enzyme. This 'haptenic' structure is
highly antigenic and has led to the development of a number of monoclonal
antibodies which recognize this structure as part of their epitopes. Examples of
the use of some of these monoclonal antibodies for localization of proteoglycan
structures in tissue sections and on transblots are described. The precise
structures are known for only a few of the native epitopes recognized by these
monoclonal antibodies. Recent analytical methods have been developed for
determining structures of chondroitin sulfate oligosaccharides. An example of
the use of these methods to analyze the structures of the non-reducing termini
of chondroitin/dermatan sulfate chains is discussed. The results show their
potential value for quantifying the native epitope recognized by a monoclonal
antibody, designated 3B3, which recognizes chains terminated by glucuronic
acid-N-acetylgalactosamine-6-sulfate. Such methods should be useful for
determining the epitope structures for other monoclonal antibodies in this
class.
- Language of Publication
- English
- Unique Identifier
- 96167365
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- MeSH Heading (Major)
- Antigens|*IM; Chondroitin Sulfates|CH/*IM; Dermatan Sulfate|CH/*IM
- MeSH Heading
- Antibodies, Monoclonal|IM; Antibody Specificity; Carbohydrate Sequence;
Epitopes|AN; Human; Molecular Sequence Data; Molecular Structure

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0065-2598
- Country of Publication
- UNITED STATES


Record 8 from database: MEDLINE
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- Title
- Thrombomodulin as a model of molecular mechanisms that modulate protease
specificity and function at the vessel surface.
- Author
- Esmon CT
- Address
- Oklahoma Medical Research Foundation, Department of Pathology, University of
Oklahoma Health Sciences Center, Oklahoma City, USA.
- Source
- FASEB J, 1995 Jul, 9:10, 946-55
- Abstract
- The protein C anticoagulant system generates an "on demand"
physiologic anticoagulant response. The pathway is initiated when thrombin binds
to the endothelial cell thrombin binding protein, thrombomodulin. The complex
exhibits dramatically altered macromolecular specificity. It rapidly cleaves the
protein C zymogen to form the anticoagulant, activated protein C. Complex
formation between thrombin and thrombomodulin also prevents thrombin, the enzyme
responsible for clot formation and a potent platelet activator, from being able
to clot fibrinogen or to activate platelets. Structural, kinetic, and
competition studies suggest that thrombomodulin blocks these clotting reactions
by masking the binding sites for fibrinogen and the platelet thrombin receptor.
Stimulation of protein C activation appears to occur through conformational
changes in the extended binding pocket of thrombin. This prevents repulsive
interactions with protein C that exist when the free enzyme attempts to dock
with this substrate. In addition to protein-protein interactions, thrombomodulin
has a covalently associated chondroitin sulfate moiety. Chondroitin sulfate
binds to a basic surface on thrombin that is also involved in heparin
interaction. The chondroitin sulfate enhances the affinity of thrombin for
thrombomodulin approximately 10- to 20-fold, making thrombomodulin a more potent
inhibitor of coagulation, altering thrombin's conformation and specificity, and
accelerating thrombin inhibition by the serpin, antithrombin. These properties
make thrombomodulin a molecular switch ideally suited to trigger an
anticoagulant response when too much thrombin is generated. The importance of
the system is documented by the clinical observation that patients deficient in
protein C often die of massive thrombotic complications that can be reversed or
prevented by infusion of protein C.
- Language of Publication
- English
- Unique Identifier
- 95340068
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- MeSH Heading (Major)
- Blood Coagulation|*; Proteins|*ME; Thrombomodulin|*PH
- MeSH Heading
- Chondroitin Sulfates|ME; Comparative Study; Fibrinogen|ME; Human; Platelet
Activation; Protein C|ME; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.;
Thrombin|ME

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0892-6638
- Country of Publication
- UNITED STATES


Record 9 from database: MEDLINE
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- Title
- CD44 in inflammation and metastasis.
- Author
- Lesley J; Hyman R; English N; Catterall JB; Turner GA
- Address
- Department of Cancer Biology, The Salk Institute, San Diego, California
92186, USA.
- Source
- Glycoconj J, 1997 Aug, 14:5, 611-22
- Abstract
- CD44 is a major cell surface receptor for the glycosaminoglycan, hyaluronan
(HA). CD44 binds HA specifically, although certain chondroitin-sulfate
containing proteoglycans may also be recognized. CD44 binding of HA is regulated
by the cells in which it is expressed. Thus, CD44 expression alone does not
correlate with HA binding activity. CD44 is subject to a wide array of
post-translational carbohydrate modifications, including N-linked, O-linked and
glycosaminoglycan side chain additions. These modifications, which differ in
different cell types and cell activation states, can have profound effects on HA
binding function and are the main mechanism of regulating CD44 function that has
been described to date. Some glycosaminoglycan modifications also affect ligand
binding specificity, allowing CD44 to interact with proteins of the
extracellular matrix, such as fibronectin and collagen, and to sequester heparin
binding growth factors. It is not yet established whether the HA binding
function of CD44 is responsible for its proposed involvement in inflammation. It
has been shown, however, that CD44/HA interactions can mediate leukocyte rolling
on endothelial and tissue substrates and that CD44-mediated recognition of HA
can contribute to leukocyte activation. Changes in CD44 expression (mainly
up-regulation, occasionally down-regulation, and frequently alteration in the
pattern of isoforms expressed) are associated with a wide variety of cancers and
the degree to which they spread; however, in other cancers, the CD44 pattern
remains unchanged. Increased expression of CD44 is associated with increased
binding to HA and increased metastatic potential in some experimental tumor
systems; however, in other systems increased HA binding and metastatic potential
are not correlated. CD44 may contribute to malignancy through changes in the
regulation of HA recognition, the recognition of new ligands and/or other new
biological functions of CD44 that remain to be discovered.
- Language of Publication
- English
- Unique Identifier
- 97442145
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- MeSH Heading (Major)
- Antigens, CD44|*PH; Inflammation|*PP; Neoplasm Metastasis|*PP;
Neoplasms|PA/*PP
- MeSH Heading
- Animal; Antigens, CD|PH; Chondroitin Sulfates|ME; Human; Hyaluronic Acid|ME;
Proteoglycans|CH/ME; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.;
Variation (Genetics)

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- ISSN
- 0282-0080
- Country of Publication
- ENGLAND


Record 10 from database: MEDLINE
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- Title
- Pathogenesis and therapy of neuropathies associated with monoclonal
gammopathies.
- Author
- Latov N
- Address
- Department of Neurology, College of Physicians and Surgeons, Columbia
University, New York, NY 10032, USA.
- Source
- Ann Neurol, 1995 May, 37 Suppl 1:, S32-42
- Abstract
- Approximately 10% of patients with peripheral neuropathy of otherwise
unknown etiology have an associated monoclonal gammopathy. Both the neuropathies
and the monoclonal gammopathies in these patients are heterogeneous, but several
distinct clinical syndromes that may respond to specific therapies can be
recognized. It is important to recognize these syndromes because monoclonal
gammopathies also occur in 1% of the normal adult population, and in some cases,
monoclonal gammopathies are coincidental and unrelated to the neuropathy. In
patients with IgM monoclonal gammopathies, IgM M proteins frequently have
autoantibody activity and are implicated in the pathogenesis of the neuropathy.
IgM M proteins that bind to myelin-associated glycoprotein (MAG) have been shown
to cause demyelinating peripheral neuropathy; anti-GM1 antibody activity is
associated with predominantly motor neuropathy, and anti-sulfatide or
chondroitin sulfate antibodies are associated with sensory neuropathy. The IgM
monoclonal gammopathies may be malignant or nonmalignant, and polyclonal
antibodies with the same specificities are associated with similar clinical
presentations in the absence of monoclonal gammopathy. IgG or IgA monoclonal
gammopathies are associated with neuropathy in patients with osteosclerotic
myeloma or the POEMS syndrome (polyneuropathy, organomegaly, endocrinopathy
myeloma, and skin changes). Amyloidosis or cryoglobulinemic neuropathies can
occur with either IgM or IgG and IgA monoclonal gammopathies. Therapeutic
intervention depends on the specific clinical syndrome but is generally directed
at removing the autoantibodies, reducing the number of monoclonal B cells, and
interfering with the effector mechanisms.
- Language of Publication
- English
- Unique Identifier
- 97122966
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- MeSH Heading (Major)
- Autoimmune Diseases|*ET/IM/TH; Paraproteinemias|*CO/EP/IM/TH; Peripheral
Nervous System Diseases|EP/*ET/IM/TH
- MeSH Heading
- Adult; Aged; Amyloidosis|ET/IM/TH; Antibody Specificity; Antineoplastic
Agents|TU; Autoantibodies|IM; Autoantigens|IM; Chondroitin Sulfates|IM;
Gangliosides|IM; Human; IgA|IM; IgG|IM; IgM|IM; Immunoglobulins, Intravenous|TU;
Middle Age; Myelin-Associated Glycoprotein|IM; Paraneoplastic
Syndromes|ET/IM/TH; Paraproteins|AN/IM; Plasmapheresis; Sulfatides|IM

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- ISSN
- 0364-5134
- Country of Publication
- UNITED STATES


Record 11 from database: MEDLINE
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- Title
- MHC class II antigen processing: biology of invariant chain.
- Author
- Sant AJ; Miller J
- Address
- Department of Pathology, University of Chicago, Illinois 60637.
- Source
- Curr Opin Immunol, 1994 Feb, 6:1, 57-63
- Abstract
- The invariant chain (Ii) has been shown to play a critical role in the
assembly, intracellular transport and function of MHC class II molecules. Recent
studies suggest that these distinct activities can in many cases be attributed
to distinct isoforms of Ii or to specific regions within it. Thus, regulation of
Ii synthesis, post-transcriptional events, and post-translational modification
has the potential to dramatically modulate immune responses.
- Language of Publication
- English
- Unique Identifier
- 94226733
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- MeSH Heading (Major)
- Antigen Presentation|*IM; Histocompatibility Antigens Class II|*IM/ME
- MeSH Heading
- Animal; Chondroitin Sulfates|PH; Endocytosis|IM; Human; Peptides|IM; Protein
Binding; Protein Processing, Post-Translational

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0952-7915
- Country of Publication
- ENGLAND


Record 12 from database: MEDLINE
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- Title
- Effects of cryopreservation upon vein function in vivo.
- Author
- Brockbank KG
- Address
- CryoLife, Inc., Marietta, Georgia 30067.
- Source
- Cryobiology, 1994 Feb, 31:1, 71-81
- Abstract
- This review covers experimental and clinical experiences with
transplantation of allogeneic veins processed by slow rate cooling with 2.5%
(W/V) chondroitin sulfate and 1 M dimethylsulfoxide. These results are
contrasted with the results obtained using dimethylsulfoxide alone. The
short-term patency of experimental autologous (100%) and allogeneic (70-100%)
cryopreserved veins may be attributed to the combination of "no-touch"
procurement techniques employing the smooth muscle relaxant papaverine, the
chondroitin sulfate preservation method, and recipient therapy. Explanted
autografts retain many cell and tissue functions. In contrast, explanted
allografts demonstrate short-term loss of endothelial cells and smooth muscle
function, both of which subsequently return. Clinically there have been positive
short-term correlations between good initial runoff from the graft site and
1-year patency (68-74%) and limb salvage (94%) rates. In contrast, grafts with
poor initial runoff, composite grafts, or grafts requiring secondary
reconstruction resulted in lower 1-year patency (40-44%) and limb salvage (64%)
rates. More experience, larger study groups, and longer follow-up are necessary
to evaluate the clinical performance of chondroitin sulfate-preserved grafts. In
the meantime, chondroitin sulfate-preserved veins are reserved for coronary
artery bypass or peripheral bypass patients in the absence of suitable
autologous vessels.
- Language of Publication
- English
- Unique Identifier
- 94208279
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- MeSH Heading (Major)
- Cryopreservation|*MT; Veins|*/IM/PP/TR
- MeSH Heading
- Animal; Chondroitin Sulfates; Cryoprotective Agents; Dimethyl Sulfoxide;
Human; Immunosuppression; Platelet Aggregation Inhibitors|PD;
Thrombophlebitis|PC; Transplantation, Autologous; Transplantation, Homologous

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0011-2240
- Country of Publication
- UNITED STATES


Record 13 from database: MEDLINE
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- Title
- Update on chemonucleolysis.
- Author
- Brown MD
- Address
- Department of the Orthopaedics and Rehabilitation, University of Miami
School of Medicine, Florida, USA.
- Source
- Spine, 1996 Dec, 21:24 Suppl, 62S-68S
- Abstract
- A review of the world medical literature on chemonucleolysis with an
emphasis on recent studies, meta-analyses, and the history of the procedure in
North America from a regulatory, social, and medicolegal perspective was
performed to determine the current status of chemonucleolysis in the management
of disc displacement. The world literature supports the use of chymopapain for
chemonucleolysis as a safe and effective alternative to surgical disc excision.
The efficacy of chymopapain has been shown by prospective, randomized,
placebo-controlled, double-blind trials with a minimum 10-year follow-up period.
The safety of chymopapain injection compared with surgery has been demonstrated
in meta-analyses and in extensive post-marketing surveillance in the United
States and Europe. Clinical studies with collagenase and laboratory studies with
chondroitinase ABC have shown that chemonucleolysis can be performed with
enzymes other than chymopapain. Clinical trials have been performed with
collagenase for chemonucleolysis, but all of the results have not been
published. Preclinical research with chondroitinase ABC has demonstrated its
usefulness for chemonucleolysis in the animal model, but human trials have not
begun.
- Language of Publication
- English
- Unique Identifier
- 97266574
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- MeSH Heading (Major)
- Chymopapain|*TU; Intervertebral Disk Chemolysis|*; Intervertebral Disk
Displacement|*DT/SU
- MeSH Heading
- Animal; Chondroitin Lyases|TU; Collagenases|TU; Comparative Study; Human;
Meta-Analysis; Randomized Controlled Trials

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0362-2436
- Country of Publication
- UNITED STATES


Record 14 from database: MEDLINE
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- Title
- New antithrombotic agents for the prevention and treatment of deep vein
thrombosis.
- Author
- Boneu B
- Address
- Laboratoire de Recherche sur l'HÆemostase et la Thrombose Toulouse, France.
- Source
- Haemostasis, 1996 Oct, 26 Suppl 4:, 368-78
- Abstract
- Besides low molecular weight heparins (LMWHs) a number of new antithrombotic
agents have been evaluated mainly in the prevention of deep vein thrombosis
(DVT) and, to a lesser extent, in the treatment of established DVT. They include
the Pentasaccharide, a synthetic ultra LMWH, Dermatan Sulphate, a
glycosaminoglycan which activates heparin cofactor II, Orgaran, a mixture of
Heparan and of Dermatan Sulphate, Hirulog and Hirudin, two direct thrombin
inhibitors. The efficacy and safety of these compounds have been studied in
comparison with a placebo or with unfractionated heparin but not with LMWH which
is considered as a gold standard for these clinical indications. It is thus
difficult at present to appreciate the advantages of these new antithrombotic
agents over conventional LMWH therapy.
- Language of Publication
- English
- Unique Identifier
- 97133746
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- MeSH Heading (Major)
- Fibrinolytic Agents|*TU; Pulmonary Embolism|DT/*PC; Thrombophlebitis|DT/*PC
- MeSH Heading
- Anticoagulants|TU; Antithrombin III|CH/ME; Binding Sites; Chondroitin
Sulfates|TU; Clinical Trials; Dermatan Sulfate|TU; Drug Screening; Factor Xa|AI;
Heparin|CH/ME/TU; Heparin, Low-Molecular-Weight|TU; Heparitin Sulfate|TU; Human;
Multicenter Studies; Oligosaccharides|TU; Postoperative Complications|PC;
Recurrence; Thrombin|AI

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0301-0147
- Country of Publication
- SWITZERLAND


Record 15 from database: MEDLINE
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- Title
- Cell surface chondroitin sulfate proteoglycans in tumor cell adhesion,
motility and invasion.
- Author
- Iida J; Meijne AM; Knutson JR; Furcht LT; McCarthy JB
- Address
- University of Minnesota, Department of Laboratory Medicine and Pathology,
Minneapolis, USA.
- Source
- Semin Cancer Biol, 1996 Jun, 7:3, 155-62
- Abstract
- Tumor cell invasion and metastasis is highly dependent on dynamic changes in
the adhesion and migration of transformed and malignant cells. As with normal
cell adhesion, the adhesion of tumor cells influences their cytoskeletal
organization, activation of signal transduction pathways within the cell, and
nuclear events leading to changes in mRNA transcription and protein synthesis.
Furthermore, as tumor cells invade the circulation, they adhere to activated
endothelial cells at sites within the vasculature during arrest and
extravasation. Studies in the area of tumor cell adhesion and migration have
demonstrated that the recognition of extracellular matrix ligands, or adhesion
promoting ligands expressed on neighboring cells (i.e. counter-receptors),
involves complex molecular recognition mechanisms. The complexity arises, in
part, from the multiple recognition sites that are present within adhesion
promoting ligands. Some of these structures within ECM components act by binding
integrins, whereas others bind additional receptors such as cell surface
proteoglycans. In this sense, adhesion promoting ligands may be considered as
informational arrays, that function to modulate cell phenotype by engaging
specific combinations of adhesion receptors on the cell surface. Understanding
the mechanism(s) by which these receptor 'cluster' modify cell adhesion,
motility and growth may lead to novel therapeutic strategies to control tumor
cell invasion and metastasis formation. This review will highlight the role that
cell surface chondroitin sulfate proteoglycans may play in modulating tumor cell
adhesion, migration and invasion, with an emphasis on the relationship between
cell surface chondroitin sulfate proteoglycans and integrins.
- Language of Publication
- English
- Unique Identifier
- 96369295
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- MeSH Heading (Major)
- Cell Adhesion|*PH; Cell Movement|*PH; Chondroitin|*BI; Proteoglycans|*BI
- MeSH Heading
- Human

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 1044-579X
- Country of Publication
- UNITED STATES


Record 16 from database: MEDLINE
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- Title
- Heparinoid anticoagulation and topical fibrin sealant in heparin-induced
thrombocytopenia.
- Author
- Jackson MR; Danby CA; Alving BM
- Address
- Department of Surgery, Walter Reed Army Medical Center, Washington, DC, USA.
- Source
- Ann Thorac Surg, 1997 Dec, 64:6, 1815-7
- Abstract
- The development of heparin-induced thrombocytopenia in patients who require
systemic anticoagulation for cardiac and vascular operations poses a therapeutic
dilemma because no alternative anticoagulants are generally available.
Heparinoid (Org 10172) has been used as an alternative anticoagulant under
protocol or on a compassionate use basis, and has recently been approved by the
Food and Drug Administration. There is, however, no heparinoid antagonist to
reverse the anticoagulation. This report describes the combined use of
heparinoid anticoagulation and adjunctive fibrin sealant for topical hemostasis
in a patient with heparin-induced thrombocytopenia. Recommendations for
perioperative monitoring of heparinoid anticoagulation are provided.
- Language of Publication
- English
- Unique Identifier
- 98097082
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- MeSH Heading (Major)
- Anticoagulants|*TU; Chondroitin Sulfates|*TU; Coronary Artery Bypass|*;
Dermatan Sulfate|*TU; Fibrin Tissue Adhesive|*TU; Heparin|*AE; Heparinoids|*TU;
Heparitin Sulfate|*TU; Thrombocytopenia|*CI
- MeSH Heading
- Case Report; Human; Male; Middle Age

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW OF REPORTED CASES
- ISSN
- 0003-4975
- Country of Publication
- UNITED STATES


Record 17 from database: MEDLINE
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- Title
- Glycosaminoglycans: structure and interaction.
- Author
- Chakrabarti B; Park JW
- Address
-
- Source
- CRC Crit Rev Biochem, 1980, 8:3, 225-313
- Abstract
- In the last few years, there has been considerable progress in the studies
on glycosaminoglycans, a group of acidic polysaccharides present in the
intercellular matrix of connective tissue. X-ray diffraction studies have
indicated that these polymers can exist in the condensed phase in some helical
form. Chiroptical and hydrodynamic measurements have provided significant
information regarding the molecular conformation in solution and other
physicochemical properties of the polymers. Studies related to the interaction
properties of glycosaminoglycans with polypeptides, metal ions, and other
molecules are numerous. This review covers mainly the results and their
interpretations of both published and as yet unpublished material of the 1970s,
but certain previous data are also included. A present-day concept regarding the
structure and interaction properties of these molecules on the basis of various
physicochemical measurements is presented. The biosynthesis and metabolism of
glycosaminoglycans, and the structure of proteoglycans and glycoproteins, are
not discussed.
- Language of Publication
- English
- Unique Identifier
- 81023329
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- MeSH Heading (Major)
- Glycosaminoglycans|*
- MeSH Heading
- Animal; Cations; Chemistry; Chemistry, Physical; Chondroitin; Chondroitin
Sulfates; Circular Dichroism; Dermatan Sulfate; Heparin; Heparitin Sulfate;
Human; Hyaluronic Acid; Hydrogen-Ion Concentration; Keratan Sulfate;
Macromolecular Systems; Metals|ME; Models, Molecular; Molecular Conformation;
Spectrum Analysis; Support, U.S. Gov't, Non-P.H.S.; Support, U.S. Gov't, P.H.S.;
Tissue Distribution; X-Ray Diffraction

- Publication Type
- JOURNAL ARTICLE; REVIEW
- ISSN
- 0045-6411
- Country of Publication
- UNITED STATES
- CAS Registry/EC Number
- 0 (Cations); 0 (Glycosaminoglycans); 0 (Macromolecular Systems); 0 (Metals);
24967-94-0 (Dermatan Sulfate); 9004-61-9 (Hyaluronic Acid); 9005-49-6 (Heparin);
9007-27-6 (Chondroitin); 9007-28-7 (Chondroitin Sulfates); 9050-30-0 (Heparitin
Sulfate); 9056-36-4 (Keratan Sulfate)


Record 18 from database: MEDLINE
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- Title
- Mechanisms for the anticoagulant effect of heparin and related
polysaccharides.
- Author
- Ofosu FA
- Address
- Canadian Red Cross Society, Blood Transfusion Service, Hamilton, Ontario.
- Source
- Nouv Rev Fr Hematol, 1988, 30:3, 155-60
- Abstract
- The anticoagulant actions of heparin and related polysaccharides can best be
addressed by answering the following 2 questions: to what extent do
unfractionated heparin, low molecular weight heparins, dermatan sulfate and
heparan sulfate inhibit the activation of prothrombin in plasma depleted of
antithrombin III and heparin cofactor II? What roles do antithrombin III and
heparin cofactor II play in the expression of the overall anticoagulant effects
of heparin, low molecular weight heparins, dermatan sulfate and heparan sulfate?
Since only heparin can, but only weakly at best, inhibit the activation of
prothrombin in plasma depleted of both antithrombin III and heparin cofactor II,
it is obvious that the anticoagulant effects of heparin, low molecular weight
heparins, dermatan sulfate and heparan sulfate are mediated primarily by their
catalytic effects on the antiprotease actions of antithrombin III (heparin, low
molecular weight heparins and heparan sulfate) and heparin cofactor II (dermatan
sulfate). The catalytic efficiencies of various glycosaminoglycans (GAGs) on the
inhibition of thrombin by undiluted plasma follow in the order of the ability of
each GAG to inhibit the intrinsic pathway activation of prothrombin. The reasons
for this observation probably follow from the effects of GAGs on the 2 positive
amplification reactions of thrombin during blood coagulation. Factor VIIIa and
factor Va, which directly or indirectly contribute to the rapid formation of
prothrombinase, arise from the limited proteolysis of factor VIII and factor V
by thrombin and/or factor Xa. On depletion of thrombin by enhanced formation of
thrombin-antithrombin III or thrombin-heparin cofactor II, factor Xa provides
the only mechanism by which factor VIII and factor V activation in plasma will
proceed.(ABSTRACT TRUNCATED AT 250 WORDS)
- Language of Publication
- English
- Unique Identifier
- 88335518
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- MeSH Heading (Major)
- Anticoagulants|*; Chondroitin|*AA; Dermatan Sulfate|*PD;
Glycosaminoglycans|*PD; Heparin|*PD; Heparitin Sulfate|*PD
- MeSH Heading
- Antithrombin III|AI; Human; Support, Non-U.S. Gov't; Thrombin|AI

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0029-4810
- Country of Publication
- GERMANY, WEST
- CAS Registry/EC Number
- EC 3.4.21.5 (Thrombin); 0 (Anticoagulants); 0 (Glycosaminoglycans);
24967-94-0 (Dermatan Sulfate); 9000-94-6 (Antithrombin III); 9005-49-6
(Heparin); 9007-27-6 (Chondroitin); 9050-30-0 (Heparitin Sulfate)


Record 19 from database: MEDLINE
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- Title
- Mucosal mast cells in the rat and in man.
- Author
- Enerbäck L
- Address
-
- Source
- Int Arch Allergy Appl Immunol, 1987, 82:3-4, 249-55
- Abstract
- The proteoglycan structure of mucosal mast cells (MMC) of the two species
has been analyzed with histochemical in situ techniques. The findings indicate
that human MMC, like human mast cells of several other sites, contain a heparin
proteoglycan, unlike rat MMC which lack heparin but contain an oversulphated
chondroitin sulphate. However, the dye-binding of the human MMC proteoglycan,
like that of the rat, is highly susceptible to blocking by formaldehyde. Human
MMC also exhibit a lower critical electrolyte concentration (CEC) of dye-binding
than mast cells of other connective tissue sites, suggesting a relatively lower
charge density and/or molecular weight of the glycosaminoglycan of the MMC.
These findings thus suggest that the human MMC like those of the rat have a
distinctive proteoglycan structure. Recent findings of another group indicate
that the human MMC like those of the rat have also a distinctive proteinase
composition. Finally, the mast cell response of the nasal mucosa during birch
pollen allergy shows fundamental similarities to the nematode response of the
rat intestinal mucosa. During both conditions mast cells are redistributed from
the lamina propria into the epithelium, probably as a result of migration of
mast cells or mast cell precursors. Taken together, these findings suggest the
existence of a distinctive MMC phenotype also in man.
- Language of Publication
- English
- Unique Identifier
- 87193224
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- MeSH Heading (Major)
- Chondroitin|*AA; Chondroitin Sulfates|*AN; Heparin|*AA/AN; Mast Cells|*AN;
Mucous Membrane|*CY; Proteoglycans|*AN; Rats|*AH
- MeSH Heading
- Animal; Comparative Study; Cystitis|PA; Hay Fever|PA; Human; Intestinal
Diseases, Parasitic|PA; Organ Specificity; Peptide Hydrolases|AN; Phenotype;
Species Specificity; Staining; Support, Non-U.S. Gov't

- Publication Type
- JOURNAL ARTICLE; REVIEW
- ISSN
- 0020-5915
- Country of Publication
- SWITZERLAND
- CAS Registry/EC Number
- EC 3.4 (Peptide Hydrolases); 0 (heparin proteoglycan); 0 (Proteoglycans);
9005-49-6 (Heparin); 9007-27-6 (Chondroitin); 9007-28-7 (Chondroitin Sulfates)


Record 20 from database: MEDLINE
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- Title
- Viscoelastic agents.
- Author
- Larson RS; Lindstrom RL; Skelnik DL
- Address
- Department of Ophthalmology, University of Minnesota School of Medicine,
Minneapolis.
- Source
- CLAO J, 1989 Apr-Jun, 15:2, 151-60
- Abstract
- Viscoelastic materials possess a unique set of properties that result from
their chemical structure. These properties enable them to protect the corneal
endothelium and epithelium from mechanical trauma and to maintain an intraocular
space, such as the anterior or vitreous chambers, even in the face of an open
incision. Hence viscoelastic materials have been successfully applied to many
areas of ophthalmic surgery, most notably anterior segment surgery, with few
complications. There are currently three commercially available viscoelastic
preparations, and several new preparations are in various stages of development.
- Language of Publication
- English
- Unique Identifier
- 89249770
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- MeSH Heading (Major)
- Acrylic Resins|*TU; Chondroitin|*TU; Eye|PH/*SU; Hyaluronic Acid|*TU;
Methylcellulose|*AA/TU
- MeSH Heading
- Anterior Eye Segment|PH/SU; Chemistry; Drug Combinations|TU; Endothelium,
Corneal|PH; Human; Intraocular Pressure

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0733-8902
- Country of Publication
- UNITED STATES
- CAS Registry/EC Number
- 0 (Acrylic Resins); 0 (Drug Combinations); 123352-36-3 (Viscoat); 9003-05-8
(polyacrylamide); 9004-61-9 (Hyaluronic Acid); 9004-65-3 (hydroxypropyl
methylcellulose); 9004-67-5 (Methylcellulose); 9007-27-6 (Chondroitin)


Record 21 from database: MEDLINE
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- Title
- Keratan sulphate--a 'reserve' polysaccharide?
- Author
- Scott JE
- Address
- Manchester University, U.K.
- Source
- Eur J Clin Chem Clin Biochem, 1994 Apr, 32:4, 217-23
- Abstract
- The early history of keratan sulphate and its proteoglycans is briefly
described. Studies were overlooked that could have had a profound influence on
later work. Early methods of writing the structures of keratan and chondroitin
sulphates obscured the fundamental relationships between them. Both are now seen
to be based on the same polymer backbone poly(Gal beta 1:4 Glc beta 1-3).
Confusion over the complicated sulphation patterns in keratan sulphate was
clarified by the domain structure idea by the group of Helmut Greiling. Keratan
sulphate is characteristic of avascular tissues (cartilages, intervertebral
discs, corneal stromas) that get their oxygen supplies by diffusion. Stockwell's
early idea that the distribution of keratan sulphate in cartilages was a
response to the poor supply of oxygen has been generalised, to the hypothesis
that keratan sulphate is a functional substitute for chondroitin sulphate under
conditions of oxygen lack. The keratan:chondroitin sulphate ratios in discs,
corneas of different species, and changes therein with age can be explained on
this basis. The biochemical controlling step is probably the NAD:NADH ratio.
Keratan sulphate may thus be a 'reserve' polysaccharide, able to do the job of
chondroitin sulphate in adverse conditions of oxygen supply. Keratan and
chondroitin/dermatan sulphates have similar functions in corneal stroma, and
probably in the other connective tissues in which they are found. They swell the
collagenous matrix, keeping the fibrils apart. Even more importantly, they
probably act as tissue organisers, orienting the fibrils vis-a-vis each other
via specific interactions of their proteoglycan protein cores with the
fibrils.(ABSTRACT TRUNCATED AT 250 WORDS)
- Language of Publication
- English
- Unique Identifier
- 94312496
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- MeSH Heading (Major)
- Keratan Sulfate|*CH/*PH; Polysaccharides|*PH
- MeSH Heading
- Animal; Carbohydrate Sequence; Human; Molecular Sequence Data; Support,
Non-U.S. Gov't

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0939-4974
- Country of Publication
- GERMANY


Record 22 from database: MEDLINE
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- Title
- Structure-function relationships of the thrombin-thrombomodulin interaction.
- Author
- Sadler JE; Lentz SR; Sheehan JP; Tsiang M; Wu Q
- Address
- Howard Hughes Medical Institute, Washington University School of Medicine,
St. Louis, Mo.
- Source
- Haemostasis, 1993 Mar, 23 Suppl 1:, 183-93
- Abstract
- Thrombomodulin is an anticoagulant protein cofactor that modulates the
substrate specificity of thrombin and promotes the cleavage of protein C. The
structure-function relationships of the thrombin-thrombomodulin interaction have
been explored by recombinant DNA and protein chemistry methods. Thrombomodulin
binds to thrombin at an anion-binding exosite on the carboxyl-terminal side of
the substrate binding cleft. This interaction interferes with the recognition
and cleavage of fibrinogen, factor V, and the platelet thrombin receptor.
Binding to thrombomodulin also protects thrombin from inhibition by heparin
cofactor II. The major thrombin binding site on thrombomodulin consists of
EGF-like domains 5 and 6. In addition, EGF-like domain 4 is required for
thrombomodulin to accelerate the activation of protein C. Some thrombomodulin
molecules contain a chondroitin sulfate moiety attached to a Ser/Thr-rich domain
adjacent to the cell membrane. This modification is not required for the
cofactor activity of thrombomodulin, but appears to contribute to 'direct
anticoagulant' activity--the ability of thrombomodulin to inhibit fibrinogen
clotting, factor V activation, and platelet activation. The chondroitin sulfate
moiety of thrombomodulin also can affect the rate of thrombin inhibition by
antithrombin III, possibly by competing with heparin for the heparin binding
site on thrombin. Detailed understanding of these interactions could lead to new
strategies for the treatment of bleeding or thrombotic disorders.
- Language of Publication
- English
- Unique Identifier
- 93266145
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- MeSH Heading (Major)
- Receptors, Cell Surface|*ME; Thrombin|*ME
- MeSH Heading
- Amino Acid Sequence; Animal; Binding Sites; Blood Coagulation; Chondroitin
Sulfates|ME; Human; Ligands; Molecular Sequence Data; Peptide Fragments|CS/ME;
Protein Binding; Protein Conformation; Recombinant Fusion Proteins|ME;
Structure-Activity Relationship; Support, U.S. Gov't, P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0301-0147
- Country of Publication
- SWITZERLAND
- CAS Registry/EC Number
- EC 3.4.21.5 (Thrombin); 0 (Ligands); 0 (Peptide Fragments); 0 (Receptors,
Cell Surface); 0 (Receptors, Thrombin); 0 (Recombinant Fusion Proteins);
9007-28-7 (Chondroitin Sulfates)


Record 23 from database: MEDLINE
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- Title
- The structure, function and turnover of aggrecan, the large aggregating
proteoglycan from cartilage.
- Author
- Hardingham TE; Fosang AJ; Dudhia J
- Address
- Kennedy Institute of Rheumatology, Hammersmith, London, UK.
- Source
- Eur J Clin Chem Clin Biochem, 1994 Apr, 32:4, 249-57
- Abstract
- Aggrecan, the large aggregating proteoglycan from cartilage contains
chondroitin sulphate and keratan sulphate attached to a multidomain protein
core. It aggregates by binding to hyaluronan and this is further stabilised by a
separate globular link protein. There are two structurally related N-terminal
globular domains, G1 and G2, of which only G1 and not G2 is involved in
aggregation. The interglobular domain joining G1 and G2 contains proteinase
sensitive sequences which appear to be the key site for cleavage during aggrecan
turnover. Much of the keratan sulphate and all of the chondroitin sulphate is
attached to the long extended glycosaminoglycan attachment region. The function
of the C-terminal G3 domain is unknown. It contains a mammalian type C lectin
and complement regulatory protein motifs. These may have interactive properties
that contribute to matrix organisation. There is also an alternatively spliced
form with an epidermal growth factor-like motif. The carbohydrate composition of
aggrecan varies with cartilage source, development and age and is heterogeneous
in each sample. There is evidence of a close control of chondroitin sulphate
synthesis that determines chain length and disaccharide composition and which
change during development and in pathology. Monoclonal antibodies that recognise
specific sequences within chondroitin sulphate chains enable some of these
changes in fine structure to be detected. Progressive digestion of chains with
chondroitinase AC II has provided evidence of a pattern of sulphation, with
6-sulphated disaccharides more abundant towards the protein core, although the
disaccharide next to the linkage region is predominantly non-sulphated.
- Language of Publication
- English
- Unique Identifier
- 94312499
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- MeSH Heading (Major)
- Cartilage|CH/ME/*PH; Proteoglycans|CH/ME/*PH
- MeSH Heading
- Amino Acid Sequence; Animal; Human; Molecular Sequence Data;
Proteochondroitin Sulfates|CH/ME/PH; Structure-Activity Relationship; Support,
Non-U.S. Gov't

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0939-4974
- Country of Publication
- GERMANY


Record 24 from database: MEDLINE
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- Title
- Mapping of proteoglycans in atherosclerotic lesions.
- Author
- Völker W; Schmidt A; Oortmann W; Broszey T; Faber V; Buddecke E
- Address
- University of Münster, Federal Republic of Germany.
- Source
- Eur Heart J, 1990 Aug, 11 Suppl E:, 29-40
- Abstract
- The involvement of sulphated glycosaminoglycans in atherosclerotic changes
have been studied in human and rat arteries, and biochemical experiments have
revealed that a significant increase in the contents of chondroitin
sulphate/dermatan sulphate and cholesterol, but loss of heparan sulphate, occurs
in human atherosclerotic arterial tissues. Electron micrographs have revealed
that extracellular deposits of lipid are predominantly present in areas rich in
chondroitin sulphate proteoglycans but not in areas rich in collagen bundles and
dermatan sulphate proteoglycans. The different types of proteoglycans have been
distinguished in situ by the cuprolinic blue staining method and enzymatic
degradation experiments, and their topohistochemical distribution patterns
analysed by morphometry of proteoglycan/cuprolinic blue precipitates. The
ultracytochemical investigations indicate changes in size and pattern of
chondroitin sulphate-rich proteoglycan-cuprolinic blue precipitates in human
atherosclerosis. In plaque tissue, these precipitates are significantly
enlarged. In addition, they accumulate around smooth muscle cells in the medial
tissue. An increase in the size of proteoglycan-cuprolinic blue precipitates has
also been observed in balloon catheter-induced lesions in rat carotid arteries.
The large chondroitin sulphate as well as the small dermatan sulphate
proteoglycan-cuprolinic blue precipitates show this alteration 2 weeks after
balloon injury. We suggest that quantitative and qualitative alterations in the
arterial proteoglycans occur in the pathogenesis of atherosclerosis in addition
to the cell proliferation and lipid accumulation.
- Language of Publication
- English
- Unique Identifier
- 91031581
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- MeSH Heading (Major)
- Atherosclerosis|ME/*PA; Proteoglycans|*UL
- MeSH Heading
- Animal; Arteries|CH/PA; Cholesterol|AN; Glycosaminoglycans|AN; Human;
Support, Non-U.S. Gov't

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0195-668X
- Country of Publication
- ENGLAND
- CAS Registry/EC Number
- 0 (Glycosaminoglycans); 0 (Proteoglycans); 57-88-5 (Cholesterol)


Record 25 from database: MEDLINE
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- Title
- Mesangial cell proteoglycans: synthesis and metabolism.
- Author
- Davies M; Thomas GJ; Shewring LD; Mason RM
- Address
- Institute of Nephrology, University of Wales College of Medicine, Cardiff
Royal Infirmary, Wales.
- Source
- J Am Soc Nephrol, 1992 Apr, 2:10 Suppl, S88-94
- Abstract
- In cultures of human adult glomerular mesangial cells, large chondroitin
sulfate proteoglycans (CSPG) and small dermatan sulfate proteoglycans (DSPG) are
synthesized. The large CSPG has a core protein, M(r) of 400,000 (major) and M(r)
of 500,000 (minor), and binds to hyaluronic acid to form large aggregates. The
two small DSPGs (Mr of approximately 350,000 and M(r) of approximately 200,000)
were related to biglycan and decorin, respectively. The majority of these
proteoglycans were located in the culture medium, but a hydrophobic form of the
CSPG was extracted from the cell layer. Mesangial cells in the growing phase
synthesized and secreted all three types of proteoglycans, but in cells arrested
in G0 by serum deprivation the incorporation of (35S)sulfate in CSPG was
drastically reduced. In the same cells stimulated to proliferate by replacing
the medium with one containing serum, the synthesis of CSPG dramatically
enhanced. The synthesis of CSPG and DSPG was also elevated in cells cocultured
with cytokines but in contrast was significantly reduced when cultured in medium
containing hyperglycemic levels of glucose. Finally, preliminary experiments are
reported that indicate that CSPG and DSPG bind to low-density lipoproteins in
vitro. These observations suggest a possible specialized function for
proteoglycans in cellular processes characteristic of glomerular disease.
- Language of Publication
- English
- Unique Identifier
- 92288287
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- MeSH Heading (Major)
- Glomerular Mesangium|DE/*ME; Proteoglycans|*BI/ME
- MeSH Heading
- Animal; Cells, Cultured; Chondroitin Sulfates|BI; Cytokines|PD; Dermatan
Sulfate|BI; Glucose|PD; Growth Substances|PD; Human; Lipoproteins|BL

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 1046-6673
- Country of Publication
- UNITED STATES
- CAS Registry/EC Number
- 0 (Cytokines); 0 (Growth Substances); 0 (Lipoproteins); 0 (Proteoglycans);
24967-94-0 (Dermatan Sulfate); 50-99-7 (Glucose); 9007-28-7 (Chondroitin
Sulfates)


Record 26 from database: MEDLINE
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- Title
- Advances in corneal preservation.
- Author
- Lindstrom RL
- Address
- University of Minnesota Department of Ophthalmology, Minneapolis.
- Source
- Trans Am Ophthalmol Soc, 1990, 88:, 555-648
- Abstract
- The functional status of the endothelium and sustained corneal deturgescence
after corneal preservation are of great clinical importance and have been
primary goals in the development of corneal storage media. In our
investigational studies we have specifically addressed the improvement of the
quality of donor tissue after 4 degrees C storage, the extension of corneal
preservation time, the enhancement of corneal wound healing, and the reduction
of the normal progressive loss of endothelial cells postkeratoplasty.
Specifically we have developed in vitro HCE cell and epithelial cell culture
models that can accurately reflect the response of human corneal tissue in vivo.
These models have been utilized to study the effects of growth factors and
medium components in relation to their biocompatibility and efficacy in the
development of improved corneal preservation solutions. Our laboratory
investigated in vitro conditions that allowed human corneal endothelium to shift
from a nonproliferative state, in which they remain viable and metabolically
active, to a proliferative, mitotically active state. Isolation techniques
developed in our laboratory have enabled the establishment of primary and
subsequent subcultures of human corneal endothelium that retain the attributes
of native endothelium. These in vitro conditions maintain HCE cells in a
proliferative state, actively undergoing mitosis. A quantitative bioassay has
been developed to determine the effects of various test medium in the
stimulation or inhibition of DNA synthesis. In attempting to learn more about
the events that occur during in vitro endothelial cell isolation, cell
reattachment, extracellular matrix interaction and migrating during subculture,
SEM was done on isolated HCE cells incubated in CSM. These studies suggest that
the components of the extracellular matrix modulate the growth response of HCE
cells, and play a role in regulating proliferation and migration. These
observations are important in view of the fact that anterior chamber environment
limits cell regeneration of the endothelium, and supports wound healing via cell
migration. In vivo, it is the complex interaction of the HCE cell and the
extracellular matrix that signal the cell to respond to cell loss in this
manner. As our knowledge of human corneal endothelium has increased so has our
anticipation of developing the "optimum" medium. Thus additional
components have been added to this basic medium to address specific
complications encountered with 4 degrees C corneal preservation. Antioxidants,
additional energy sources, and other nutritive substrates have been used to
supplement and further define a chondroitin sulfate-based medium. These changes
have been a part of our new awareness that, even at 4 degrees C, the cornea is
metabolically active.(ABSTRACT TRUNCATED AT 400 WORDS)
- Language of Publication
- English
- Unique Identifier
- 91247156
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- MeSH Heading (Major)
- Cornea|*PH; Organ Preservation|*MT
- MeSH Heading
- Cells, Cultured; Chondroitin Sulfates|AN; Cryopreservation; Dextrans|PK;
Endothelium, Corneal|CH/ME/PH/UL; Human; Keratinocytes; Proteoglycans|DU;
Support, Non-U.S. Gov't

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0065-9533
- Country of Publication
- UNITED STATES
- CAS Registry/EC Number
- 0 (Proteoglycans); 9004-54-0 (Dextrans); 9007-28-7 (Chondroitin Sulfates)


Record 27 from database: MEDLINE
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- Title
- Chondroitin sulfate proteoglycans as mediators of axon growth and
pathfinding.
- Author
- Margolis RU; Margolis RK
- Address
- Department of Pharmacology, New York University Medical Center, 550 First
Avenue, New York, NY 10016, USA.
- Source
- Cell Tissue Res, 1997 Nov, 290:2, 343-8
- Abstract
- This review focuses primarily on studies concerning the potential roles of
two nervous-tissue-specific chondroitin sulfate proteoglycans, viz., neurocan
and phosphacan, in cell interactions and neurite growth in the developing
central nervous system. The multiple ligands of these proteoglycans and the
modulatory effects of various types of glycosylation are also considered. Other
chondroitin sulfate proteoglycans, such as NG2, DSD-1, Cat-301, versican, and
biglycan, are briefly discussed in relation to the functional properties that
have been ascribed to them.
- Language of Publication
- English
- Unique Identifier
- 97465863
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- MeSH Heading (Major)
- Axons|*PH; Cell Communication|*PH; Cell Movement|*PH; Nerve Tissue
Proteins|*PH; Nervous System|*EM; Neurons|*CY/*PH; Proteochondroitin
Sulfates|*PH
- MeSH Heading
- Animal; Human

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0302-766X
- Country of Publication
- GERMANY


Record 28 from database: MEDLINE
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- Title
- Chondroprotection with chondroitin sulfate.
- Author
- Pipitone VR
- Address
- Department of Rheumatology, University of Bari, Italy.
- Source
- Drugs Exp Clin Res, 1991, 17:1, 3-7
- Abstract
- The remarkable insights into the pathogenesis of osteo-arthrosis (OA) have
also affected the therapeutic field. Efforts have been made to find drugs which
would somehow block or slow down the evolution of this disease. In this
connection, a major contribution has been made by the investigations on
glycosaminoglycans (GAGs), which play a crucial role in the physiology of joint
cartilage. It was thus suggested that proper supplementation with GAGs might
enable chondrocytes to replace the proteoglycans (PG).
Galactosaminoglucuronoglycan sulfate (GAGGS) has been used for this purpose. In
preliminary clinical trials, GAGGS exhibited a remarkable tolerability and good
therapeutic efficacy. GAGs are generally able to inhibit certain enzymes present
in the synovial fluid which may damage joint cartilage (elastase,
hyaluronidase). Moreover, GAGGS has also been shown to act as an
anti-inflammatory drug since it has an inhibitory effect over the complement.
All these data supply evidence that, in theory, GAGGS may have a
chondroprotective effect in patients with OA. In addition to the positive
results of preliminary clinical trials, the use of GAGGS in OA therapy is based
on the fact that this drug is absorbed by the body, is concentrated in the
cartilages and produces no toxic or teratogenic effects. In the clinical studies
performed so far, although of the open type, GAGGS has always yielded clinical
improvement both of painful symptoms and of limited function thanks to its
proven anti-inflammatory activity. Thus once the results from other ongoing
trials (double blind) are available, hopefully GAGGS will in fact become a basic
drug for OA therapy.
- Language of Publication
- English
- Unique Identifier
- 92007098
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- MeSH Heading (Major)
- Chondroitin Sulfates|*TU
- MeSH Heading
- Cartilage|CY/DE; Glycosaminoglycans|TU; Human; Osteoarthritis|DT/PC

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0378-6501
- Country of Publication
- SWITZERLAND
- CAS Registry/EC Number
- 0 (Glycosaminoglycans); 9007-28-7 (Chondroitin Sulfates)


Record 29 from database: MEDLINE
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- Title
- Neurocan and phosphacan: two major nervous tissue-specific chondroitin
sulfate proteoglycans.
- Author
- Margolis RK; Rauch U; Maurel P; Margolis RU
- Address
- Department of Pharmacology, State University of New York, Brooklyn 11203,
USA.
- Source
- Perspect Dev Neurobiol, 1996, 3:4, 273-90
- Abstract
- Neurocan is a multidomain hyaluronan-binding chondroitin sulfate
proteoglycan that is synthesized by neurons, whereas the astroglial proteoglycan
phosphacan is an mRNA splice variant representing the entire extracellular
portion of a receptor-type protein tyrosine phosphatase. A glycoform of
phosphocan (phosphocan-KS) that contains both chondroitin sulfate and keratan
sulfate is present in the postnatal rat central nervous system (CNS). The
concentration of neurocan in brain increases during late embryonic development
but then declines steeply during the early postnatal period together with
hyaluronan, and neurocan also undergoes extensive proteolytic processing during
the course of brain development. In contrast, the concentrations of both
phosphocan and phosphocan-KS rise steadily after embryonic day 20 to reach a
plateau at about 2 weeks postnatally. In the embryonic CNS the distribution of
neurocan mRNA is more widespread than that of phosphocan, which is primarily
present in regions of active cell proliferation. Neurocan mRNA is also present
in areas where the proteoglycan is not expressed, and there is evidence that the
short open reading frame in its 5'-leader may function as a cis-acting
regulatory signal for the modulation of neurocan expression in the developing
CNS. Neurocan and phosphocan bind saturably, reversibly, and with high affinity
to neural cell adhesion molecules (Ng-CAM/L1, NCAM, TAG-1/axonin-1) and to
tenascin-C. The proteoglycans and their ligands have overlapping localizations
in the CNS, and binding of phosphocan to Ng-CAM/L1, NCAM, and tenascin-C is
mediated by complex-type N-linked oligosaccharides on the proteoglycan. Neurocan
and phosphocan also bind to neurons and are potent inhibitors of neuronal and
glial adhesion and neurite outgrowth. Through their interactions with neural
cell adhesion and extracellular matrix molecules, these proteoglycans may play a
major role in modulating cell adhesion, neurite growth, and signal transduction
across the plasma membrane during the development of the CNS.
- Language of Publication
- English
- Unique Identifier
- 97166458
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- MeSH Heading (Major)
- Nerve Tissue|*ME; Nerve Tissue Proteins|CH/*ME; Proteochondroitin
Sulfates|CH/*ME
- MeSH Heading
- Aging|ME; Animal; Fetal Development; Human; Support, Non-U.S. Gov't;
Support, U.S. Gov't, P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 1064-0517
- Country of Publication
- UNITED STATES


Record 30 from database: MEDLINE
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- Title
- Arterial wall proteoglycans--biological properties related to pathogenesis
of atherosclerosis.
- Author
- Radhakrishnamurthy B; Srinivasan SR; Vijayagopal P; Berenson GS
- Address
- Department of Medicine, Louisiana State University Medical Center, New
Orleans 70112.
- Source
- Eur Heart J, 1990 Aug, 11 Suppl E:, 148-57
- Abstract
- The arterial wall is a complex organ system with respect to
carbohydrate-protein macromolecules, particularly proteoglycans. Proteoglycans
in the arterial wall display polydispersity and heterogeneity even in the same
family. At least two major types are known: chondroitin sulphate-dermatan
sulphate type and heparan sulphate type. These proteoglycans have varied
biological properties, and some of these properties are implicated in the
development of atherosclerosis. The chondroitin sulphate-dermatan sulphate
proteoglycans are capable of forming complexes with serum low-density
lipoproteins, a process conductive to lipid accumulation in the extracellular
space of the arterial wall. Also, such reactions render low-density lipoprotein
particles electronegative aggregates. These altered low-density lipoproteins are
taken up by macrophages (and possibly by proliferative smooth muscle cells)
through a high-affinity receptor pathway devoid of feedback regulation, which
results in intracellular lipid accumulation and foam-cell formation, a hallmark
of atherosclerosis. On the other hand, heparan sulphate proteoglycan located on
the cell surface and internal elastic lamina is antithrombogenic, and
facilitates binding of the lipid-clearing enzyme, lipoprotein lipase, to
endothelium. Thus, chondroitin sulphate and heparan sulphate proteoglycans with
divergent biological properties play a crucial role in the pathogenesis of
atherosclerosis.
- Language of Publication
- English
- Unique Identifier
- 91031568
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- MeSH Heading (Major)
- Arteries|*PP; Atherosclerosis|*PP; Endothelium, Vascular|*PP;
Proteoglycans|*PH
- MeSH Heading
- Animal; Human; In Vitro; Support, U.S. Gov't, P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0195-668X
- Country of Publication
- ENGLAND
- CAS Registry/EC Number
- 0 (Proteoglycans)


Record 31 from database: MEDLINE
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- Title
- Proteoglycans and cell adhesion. Their putative role during tumorigenesis.
- Author
- Turley EA
- Address
-
- Source
- Cancer Metastasis Rev, 1984, 3:4, 325-39
- Abstract
- In this review, evidence that proteoglycans are involved in cell adhesion
and related behavior is considered, together with their putative role(s) during
tumorigenesis. Proteoglycans are large, carboxylated and/or sulfated structures
that interact with specific binding sites on cell surfaces. Their distribution
and synthesis in tissues alter with the onset of tumorigenesis so that
hyaluronic acid is generally increased and heparan sulfate decreased in the
developing tumor and surrounding tissue. However, the precise role of
proteoglycans during the tumorigenic process is far from clarified. Data suggest
any putative roles will be related to the adhesive properties that these
molecules confer to cells. Hyaluronic acid and chondroitin sulfate appear to be
weakly adhesive molecules that may promote 'transformed' characteristics when
they occur on cells in large amounts. These characteristics include reduced cell
spreading, increased cell motility, as well as reduced contact inhibition.
Consistent with such properties, neither hyaluronic acid nor chondroitin sulfate
are localized in specialized adhesion sites such as focal or close contacts. In
contrast, heparan sulfate is associated with increased cell-substratum adhesion
and is involved in the spreading of cells onto fibronectin and other substrata.
Its presence is generally associated with reduced motility and with a
well-spread morphology. Unlike hyaluronate and chondroitin sulfate, heparan
sulfate is found in specialized contacts. These adhesive properties of
proteoglycans predict an instructive role in tumor development, and recent
experiments have defined an involvement of these molecules in metastatic arrest.
Additional studies utilizing invasive and metastatic tumor variants including
tumor cells that employ different mechanisms to invade are required to clarify
the role of proteoglycans in tumor progression.
- Language of Publication
- English
- Unique Identifier
- 85099057
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- MeSH Heading (Major)
- Neoplasms|*ET/PA; Proteoglycans|AN/*PH
- MeSH Heading
- Animal; Carrier Proteins|AN; Cell Adhesion; Cell Movement|DE; Chemistry;
Chondroitin Sulfates|PH; Heparitin Sulfate|PH; Human; Hyaluronic Acid|PH;
Proteochondroitin Sulfates|PH; Receptors, Cell Surface|AN; Support, Non-U.S.
Gov't

- Publication Type
- JOURNAL ARTICLE; REVIEW
- ISSN
- 0167-7659
- Country of Publication
- NETHERLANDS
- CAS Registry/EC Number
- 0 (heparan sulfate proteoglycan); 0 (Antigens, CD44); 0 (Carrier Proteins);
0 (Proteochondroitin Sulfates); 0 (Proteoglycans); 0 (Receptors, Cell Surface);
9004-61-9 (Hyaluronic Acid); 9007-28-7 (Chondroitin Sulfates); 9050-30-0
(Heparitin Sulfate)


Record 32 from database: MEDLINE
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- Title
- Glycosaminoglycan chondroprotection: pharmacological vistas.
- Author
- Pàroli E
- Address
- Institute of Pharmacology, University of Rome La Sapienza, Italy.
- Source
- Int J Clin Pharmacol Res, 1993, 13 Suppl:, 1-9
- Abstract
- Chondroprotection is a somewhat new field in the therapy of osteoarthritis,
which is designed to improve cartilage repair as well as enhance joint
remodeling. It clearly results from both laboratory models as well as from
studies on human osteoarthritis, that cartilage contains biological resources to
meet the repair of degenerative injuries and inflammation. Interestingly,
sulfated glycosaminoglycans from matrix inhibit leukocyte protease and
complement-mediated immunological reactions. By fractioning cartilage
glycosaminoglycans from Selachus (Matrix), evidence has been obtained that a
proper chondroitinsulfate sequence, which is able to inhibit elastase, may be
released from cartilage proteoglycans by cleavage of the xyl-ser O-glycosidic
bond. Since a number of sulfated glycosaminoglycans have a regulatory function
in an array of tissues, attention is drawn to possible regulatory properties of
selected sequences of matrix chondroitinsulfate, as far as chondroprotection is
concerned.
- Language of Publication
- English
- Unique Identifier
- 95088047
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- MeSH Heading (Major)
- Cartilage|*DE/PA; Glycosaminoglycans|PD/*TU; Osteoarthritis|*DT
- MeSH Heading
- Anti-Inflammatory Agents, Non-Steroidal|PD/TU; Chondroitin Sulfates|PD/TU;
Comparative Study; Heparin|PD/TU; Human; Hyaluronidase|AI;
Pancreatopeptidase|AI; Protease Inhibitors|PD/TU

- Publication Type
- CLINICAL TRIAL; JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0251-1649
- Country of Publication
- SWITZERLAND
- CAS Registry/EC Number
- EC 3.2.1.35 (Hyaluronidase); EC 3.4.21.36 (Pancreatopeptidase); EC 3.4.21.37
(Leukocyte Elastase); 0 (Anti-Inflammatory Agents, Non-Steroidal); 0
(Glycosaminoglycans); 0 (Protease Inhibitors); 63449-40-1 (arteparon);
64082-61-7 (A73025); 9005-49-6 (Heparin); 9007-28-7 (Chondroitin Sulfates)


Record 33 from database: MEDLINE
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- Title
- Angiogenesis in wound healing and tumor metastasis.
- Author
- Ruiter DJ; Schlingemann RO; Westphal JR; Denijn M; Rietveld FJ; De Waal RM
- Address
- Department of Pathology, University Hospital Nijmegen St. Radboud, The
Netherlands.
- Source
- Behring Inst Mitt, 1993 Aug, :92, 258-72
- Abstract
- Formation of new blood vessels is essential for several physiological and
pathological events, e.g. embryogenesis, wound healing and tumor growth and
metastasis. In order to increase the insight into the mechanisms of angiogenesis
we have visualized the different components of the microvasculature in human
wounds and tumors by immunohistochemistry on the light and electronmicroscopic
level. For this purpose, antibodies recognizing distinct markers for human
endothelial cells, pericytes and basal lamina were used on freshly frozen or
paraformaldehyde-fixed tissue samples. In terms of efficacy, the PAL-E antigen
is highly specific for blood vessel endothelium. Its sensitivity is less than
other endothelial markers, such as von Willebrand factor and CD 31, as it is not
expressed in arterioles. Within the context of the microvasculature alpha-smooth
muscle actin and the HMW-MAA chondroitin sulphate proteoglycan are useful
markers for pericytes. Type IV Collagen and Laminin can be visualized
consistently in the microvascular basal lamina. During the formation of
granulation tissue in wound healing a heterogeneity of the expression of
endothelial and pericyte markers is found. In the least matured zone in
granulation tissue of decubitus lesions and experimental skin wounds
microvessels already contained both endothelial cells and pericytes, suggesting
a role for both cell types in the early steps of angiogenesis. Regarding the
tumor microvasculature, antibodies to von Willebrand factor often failed to
stain capillaries, that did show expression of the other endothelial markers
studied. Broad staining in pericytes was found for the HMW-MAA chondroitin
sulphate proteoglycan. In contrast, these cells only locally expressed
alpha-smooth muscle actin. Staining of the basal lamina components Type IV
Collagen and Laminin within tumors was not restricted to the microvasculature.
Therefore, antibodies recognizing endothelial markers, particularly PAL-E and
BMA 120, are preferable as tools to visualize the tumor microvasculature. In
accordance with the situation in granulation tissue of wound healing the broad
presence of pericytes in the microvasculature of human tumor suggests an
involvement of this cell type in tumor angiogenesis. Recent immunohistochemical
studies on human tumor lesions indicated that a high number of microvessels
adjacent to the tumor as a measure of tumor angiogenesis is an unfavorable
prognostic factor in cutaneous melanoma, mammary carcinoma and non-small cell
pulmonary carcinoma. This new application of immunohistochemistry represents a
valuable, clinically relevant adjunct to the repertoire of the surgical
pathologist.
- Language of Publication
- English
- Unique Identifier
- 94071793
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- MeSH Heading (Major)
- Endothelium, Vascular|*PH/*PP/UL; Neoplasm Metastasis|*PP; Neoplasms|*BS;
Neovascularization, Pathologic|*PP; Wound Healing|*PH
- MeSH Heading
- Animal; Biological Markers|AN; Blood Vessels|PH/PP; Human; Microscopy,
Immunoelectron; Skin|BS/PA; Support, Non-U.S. Gov't; Wounds and Injuries|PA/PP

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0301-0457
- Country of Publication
- GERMANY
- CAS Registry/EC Number
- 0 (Biological Markers)


Record 34 from database: MEDLINE
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- Title
- C1q inhibitor (chondroitin-4-sulfate proteoglycan): structure and function.
- Author
- Ghebrehiwet B; Galanakis DK
- Address
- Department of Medicine, State University of New York 11794-8161.
- Source
- Behring Inst Mitt, 1993 Dec, :93, 214-23
- Abstract
- The serum C1q inhibitor (C1q INH) is a chondroitin 4-sulfate proteoglycan
which is composed of several polyanionic components ranging in size from 21-750
kDa. Although the activity of C1q INH has been described in terms of its ability
to precipitate C1q and inhibit its hemolytic activity, not much is known about
either the mechanisms of its action or its role in health and disease. This
report provides evidence that a 30 kDa core protein component of the
proteoglycan macromolecule contains most of the C1q inhibitory activity. This
inhibitory activity occurs as a result of C1q INH binding to the C1q
"heads" (gC1q) as well as to the collagen "tail" (cC1q).
What may be more significant in terms of perpetuation of inflammatory processes
is the ability of C1q INH to moderately activate the classical pathway leading
to C2 and C4 consumption. The binding of C1q INH to C1q is enhanced at low ionic
strength, but significant binding does occur under physiologic conditions which
makes it likely for the inhibitor to participate in inflammatory processes
especially in microenvironments of high inhibitor concentration. Such elevated
concentration does occur in patients with active rheumatoid arthritis and
systemic lupus erythematosus either as a result of unregulated proteoglycan
synthesis or disturbances in connective tissue metabolism. Another important
function of serum C1q INH is its ability to prolong the clotting time of plasma
and fibrinogen solutions containing or lacking CaCl2. This potent anticoagulant
activity is again displayed by the 30 kDa putative protein core which
specifically binds to both the E and D domains of fibrinogen. However, the
epitope(s) on the 30 kDa which binds to C1q appears to be distinct from that
which binds to fibrinogen. The known presence of proteoglycans on the basement
membranes and other sites may explain at least in part the presence of
fibrinogen in atheromatous lesions. Furthermore, by binding to fibrinogen,
soluble C1q INH-and C1q-C1q INH complexes may limit fibrin gelation in
inflammatory and tissue repair microenvironments.
- Language of Publication
- English
- Unique Identifier
- 94226571
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- MeSH Heading (Major)
- Complement Activation|*; Proteochondroitin Sulfates|*CH/IP/*ME
- MeSH Heading
- Chromatography, Affinity; Fibrinogen|ME; Human; Kinetics; Molecular Weight;
Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0301-0457
- Country of Publication
- GERMANY
- CAS Registry/EC Number
- 0 (Proteochondroitin Sulfates); 9001-32-5 (Fibrinogen)


Record 35 from database: MEDLINE
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- Title
- Molecular events that control the protein C anticoagulant pathway.
- Author
- Esmon CT
- Address
- Cardiovascular Biology Research Program, Oklahoma Medical Research
Foundation, Oklahoma City.
- Source
- Thromb Haemost, 1993 Jul 1, 70:1, 29-35
- Abstract
- Despite its rather recent identification, the protein C activation system
has afforded many investigators with unique opportunities to probe the molecular
basis by which cofactors function. Thrombomodulin clearly exerts its specificity
switch both by interacting directly with the fibrinogen binding site on thrombin
(exosite 1) and by altering the conformation within the enzyme center. At least
in the case of thrombomodulin, these conformational changes appear to overcome
repulsive interactions between acidic residues in the substrate and the enzyme.
To determine whether the models derived from attempts at the molecular analysis
of the protein C activation complex are at all relevant to the other coagulation
complexes will require further examination, but the concept that residues near
the cleavage site contact residues in the free enzyme in an unfavorable fashion,
and that the cofactors overcome these inhibitory interactions is a hypothesis
that is directly testable for all of the complexes. The availability of crystal
structures for the coagulation enzymes, coupled with the capacity to mutagenize
both the substrate and the enzyme, promises to provide new insights into
molecular events that control coagulation.
- Language of Publication
- English
- Unique Identifier
- 94054288
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- MeSH Heading (Major)
- Blood Coagulation|*PH; Protein C|*ME
- MeSH Heading
- Animal; Calcium|PH; Chondroitin Sulfates|CH; Enzyme Activation|PH; Enzyme
Precursors|BL; Human; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.;
Thrombomodulin|CH

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0340-6245
- Country of Publication
- GERMANY
- CAS Registry/EC Number
- 0 (Enzyme Precursors); 0 (Protein C); 0 (Thrombomodulin); 7440-70-2
(Calcium); 9007-28-7 (Chondroitin Sulfates)


Record 36 from database: MEDLINE
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- Title
- Hair follicle proteoglycans.
- Author
- Couchman JR
- Address
- Department of Cell Biology, University of Alabama, Birmingham 35294-0019.
- Source
- J Invest Dermatol, 1993 Jul, 101:1 Suppl, 60S-64S
- Abstract
- Proteoglycans are polymorphic macromolecules present in all mammalian
tissues, including the skin and its appendages. They consist of a core protein
to which one or more glycosaminoglycan chains are covalently attached. Broadly,
they can be divided into classes based on location and core protein structure.
These classes include cell surface proteoglycans, basement membrane
proteoglycans, small leucine-rich proteoglycans, large proteoglycans aggregating
with hyaluronan, and intracellular granule proteoglycans. They have a wide range
of functions, but little is known of the proteoglycans that are present in the
epithelial and stromal compartments of hair follicles. However, the
transmembrane proteoglycan syndecan may be important in follicle morphogenesis,
both with respect to the epithelium and dermal papilla cells. Syndecan may
possess both heparan and chondroitin sulfate chains, interacts with growth
factors as well as fibronectin and interstitial collagens, and can associate in
a transmembrane relationship with the cellular cytoskeleton. It is strongly
expressed in mesenchymal cells coincident with stromal-epithelial interactions
during tissue morphogenesis. Proteoglycans are present in all basement
membranes, including those surrounding the epithelial compartment of hair
follicles. Additionally, and quite unlike the dermis, the dermal papilla is
enriched in basement-membrane components, especially a chondroitin
6-sulfate-containing proteoglycan, BM-CSPG. The function of this proteoglycan is
not known, but developmental studies indicate that it may have a role in
stabilizing basement membranes. In the hair cycle, BM-CSPG decreases through
catagen and is virtually absent from the telogen papilla. One or more heparan
sulfate proteoglycans, including perlecan, are also present in papilla and
follicular basement membranes. Some of the leucine-rich proteoglycans, such as
decorin, are associated with interstitial collagens, and may influence
fibrillogenesis. Because small amounts of types I and III collagens may be
present in anagen papillae, decorin may also be a constituent.
- Language of Publication
- English
- Unique Identifier
- 93315896
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- MeSH Heading (Major)
- Hair|*CH; Proteoglycans|*AN/PH
- MeSH Heading
- Animal; Basement Membrane|CH; Human; Membrane Glycoproteins|AN; Support,
U.S. Gov't, P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0022-202X
- Country of Publication
- UNITED STATES
- CAS Registry/EC Number
- 0 (decorin); 0 (syndecan); 0 (Membrane Glycoproteins); 0 (Proteoglycans)


Record 37 from database: MEDLINE
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- Title
- Altered proteoglycan gene expression and the tumor stroma.
- Author
- Iozzo RV; Cohen I
- Address
- Department of Pathology and Cell Biology, Thomas Jefferson University,
Philadelphia, Pennsylvania 19107.
- Source
- Experientia, 1993 May 15, 49:5, 447-55
- Abstract
- Tumor stroma is a specialized form of tissue that is associated with
epithelial neoplasms. Recent evidence indicates that significant changes in
proteoglycan content occur in the tumor stroma and that these alterations could
support tumor progression and invasion as well as tumor growth. Our main
hypothesis is that the generation of tumor stroma is under direct control of the
neoplastic cells and that, via a feedback loop, altered proteoglycan gene
expression would influence the behavior of tumor cells. In this review, we will
focus primarily on the work from our laboratory related to the altered
expression of chondroitin sulfate proteoglycan and its role in tumor development
and progression. The connective tissue stroma of human colon cancer is enriched
in chondroitin sulfate and the stromal cell elements, primarily colon
fibroblasts and smooth muscle cells, are responsible for this biosynthetic
increase. These changes can be reproduced in vitro by using either tumor
metabolites or co-cultures of human colon carcinoma cells and colon mesenchymal
cells. The levels of decorin, a leucine-rich proteoglycan involved in the
regulation of matrix assembly and cell proliferation, are markedly elevated in
the stroma of colon carcinoma. These changes correlate with a marked increase in
decorin mRNA levels and a concurrent hypomethylation of decorin gene, a DNA
alteration associated with enhanced gene expression. Elucidation of decorin gene
structure has revealed an unexpected degree of complexity in the 5' untranslated
region of the gene with two leader exons that are alternatively spliced to the
second coding exon.(ABSTRACT TRUNCATED AT 250 WORDS)
- Language of Publication
- English
- Unique Identifier
- 93272928
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- MeSH Heading (Major)
- Proteoglycans|*GE/*ME
- MeSH Heading
- Alternative Splicing; Animal; Base Sequence; Cell Division; Extracellular
Matrix|UL; Gene Expression Regulation, Neoplastic; Human; Methylation; Molecular
Sequence Data; Promoter Regions (Genetics); RNA, Messenger|GE; Support, Non-U.S.
Gov't; Support, U.S. Gov't, P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- ISSN
- 0014-4754
- Country of Publication
- SWITZERLAND
- CAS Registry/EC Number
- 0 (decorin); 0 (Proteoglycans); 0 (RNA, Messenger)


Record 38 from database: MEDLINE
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- Title
- Molecular cloning and analysis of the protein modules of aggrecans.
- Author
- Upholt WB; Chandrasekaran L; Tanzer ML
- Address
- Department of BioStructure and Function, School of Dental Medicine,
University of Connecticut Health Center, Farmington 06030-3705.
- Source
- Experientia, 1993 May 15, 49:5, 384-92
- Abstract
- The large aggregating chondroitin sulfate proteoglycan of cartilage,
aggrecan, has served as a prototype of proteoglycan structure. Molecular cloning
has elucidated its primary structure and revealed both known and unknown
domains. To date the complete structures of chicken, rat and human aggrecans
have been deduced, while partial sequences have been reported for bovine
aggrecan. A related proteoglycan, human versican, has also been cloned and
sequenced. Both aggrecan and versican have two lectin domains, one at the
amino-terminus which binds hyaluronic acid and one at the carboxyl-terminus
whose physiological ligand is unknown. Both lectins have homologous counterparts
in other types of proteins. Within the aggrecans the keratan sulfate domain may
be variably present and also has a prominent repeat in some species. The
chondroitin sulfate domain has three distinct regions which vary in their
prominence in different species. The complex molecular structure of aggrecans is
consistent with the concept of exon shuffling and aggrecans serve as suitable
prototypes for comprehending the evolution of multi-domain proteins.
- Language of Publication
- English
- Unique Identifier
- 93272923
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- MeSH Heading (Major)
- Proteoglycans|BI/CH/*GE
- MeSH Heading
- Amino Acid Sequence; Animal; Cloning, Molecular; DNA|GE; Human; Molecular
Sequence Data; Proteochondroitin Sulfates|CH/GE; Sequence Homology, Amino Acid

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- ISSN
- 0014-4754
- Country of Publication
- SWITZERLAND
- CAS Registry/EC Number
- 0 (aggrecan); 0 (Proteochondroitin Sulfates); 0 (Proteoglycans); 126968-45-4
(versican); 9007-49-2 (DNA)


Record 39 from database: MEDLINE
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- Title
- Roles of aggrecan, a large chondroitin sulfate proteoglycan, in cartilage
structure and function.
- Author
- Watanabe H; Yamada Y; Kimata K
- Address
- Craniofacial Developmental Biology and Regeneration Branch, National
Institute of Dental Research, National Institutes of Health, Bethesda MD 20892,
USA. watanabe@yoda.nidr.nih.gov
- Source
- J Biochem (Tokyo), 1998 Oct, 124:4, 687-93
- Abstract
- Aggrecan, a large aggregating proteoglycan, is one of the major structural
components of cartilage. Its core protein contains three glubular domains and
two glycosaminoglycan-attachment domains. These domains play various roles to
maintain cartilage structure and function. An N-terminal globular domain binds
hyaluronan and link protein to form huge aggregates. The chondroitin sulfate
(CS) chains attach to the CS domain and provide a hydrated, viscous gel that
absorbs compressive load. Two autosomal recessive chondrodysplasias, cartilage
matrix deficiency (cmd) in mice and nanomelia in chicken are both caused by
aggrecan gene mutations. Cmd homozygotes die shortly after birth, while the
heterozygotes are born normal. However, cmd heterozygotes develop late onset of
spinal disorder, which suggests aggrecan as a candidate gene predisposing
individuals to spinal problems. Nanomelia is a useful model to elucidate
intracellular trafficking of proteoglycans. Further studies on aggrecan will
lead to prophylaxis and treatment of joint destructive diseases such as
osteoarthrosis and to elucidation of cartilage development, which is essential
for skeletal formation.
- Language of Publication
- English
- Unique Identifier
- 98429582
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- MeSH Heading (Major)
- Cartilage|*AH/*PH; Proteochondroitin Sulfates|*CH/GE/*PH;
Proteoglycans|*CH/GE/*PH
- MeSH Heading
- Animal; Cartilage Diseases|GE/PP; Chickens; Human; Mice; Mice, Mutant
Strains

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0021-924X
- Country of Publication
- JAPAN


Record 40 from database: MEDLINE
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- Title
- Hydrocephalus, lumbar canal stenosis and Maroteaux-Lamy syndrome
(mucopolysaccharidosis type 6). Case report.
- Author
- Sheridan M; Chaseling R; Johnston IH
- Address
- Royal Alexandra Hospital for Children, Camperdown NSW, Australia.
- Source
- J Neurosurg Sci, 1992 Oct-Dec, 36:4, 215-7
- Abstract
- A case of communicating hydrocephalus and lumbar canal stenosis in a child
with mucopolysaccharidosis type 6 is reported. We review the literature and
discuss the aetiology of communicating hydrocephalus in this condition.
- Language of Publication
- English
- Unique Identifier
- 93308513
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- MeSH Heading (Major)
- Hydrocephalus|*ET/PP/SU; Mucopolysaccharidosis VI|CF/*CO; Spinal
Stenosis|*ET/PP/SU
- MeSH Heading
- Arachnoid|ME/PA; Case Report; Cerebrospinal Fluid|ME; Cerebrospinal Fluid
Pressure; Cerebrospinal Fluid Shunts; Child; Chondroitin Sulfates|ME; Female;
Human; Hypertrophy; Laminectomy; Ligaments|ME/PA; Pia Mater|MI/PA

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW OF REPORTED CASES
- ISSN
- 0390-5616
- Country of Publication
- ITALY
- CAS Registry/EC Number
- 9007-28-7 (Chondroitin Sulfates)


Record 41 from database: MEDLINE
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- Title
- Overview of the corneal toxicity of surgical solutions and drugs: and
clinical concepts in corneal edema.
- Author
- Hyndiuk RA; Schultz RO
- Address
- Department of Ophthalmology, Medical College of Wisconsin, Milwaukee 53226.
- Source
- Lens Eye Toxic Res, 1992, 9:3-4, 331-50
- Abstract
- Surgical solutions and drugs are important in ocular surgery. These include
irrigating solutions, viscoelastic substances, mydriatics and miotics, and a
growing number of other agents designed to enhance intraocular surgery and its
outcome. Potential for damage to the corneal endothelium and other tissues is
related to the chemical composition, pH, and osmolality of the irrigating
solutions that bathe tissues. Quality balanced salt solutions (BSS) are usually
safe for use as an intraocular solution in patients with normal corneal
endothelium. If prolonged irrigation times are expected, or the patient already
has decompensated endothelium, i.e., primary or secondary endotheliopathy, the
use of a "complete" BSS solution is indicated to minimize damage.
Intraocular sulfite-containing epinephrine may cause severe corneal edema and
should be avoided, or if used, be well diluted. Sulfite-free epinephrine
solution is now available and does not cause the endothelial toxicity that one
may see with sulfite-containing epinephrine solutions. Current formulations of
acetylcholine and carbachol used as miotics in surgery have been evaluated in
humans and caution is recommended in using acetylcholine solutions
intracamerally in patients with already decompensated endothelium. Chondroitin
sulfate, hydroxypropyl methylcellulose, and sodium hyaluronate are non-toxic to
animal endothelial cells under conditions analogous to cataract extraction in
humans but can be toxic to endothelium if there is continued contact with
endothelium for hours. Chondroitin sulfate has been shown to have more of a
protective effect in mechanical pseudophakos trauma probably because of its
cohesiveness and tendency to coat the endothelium. Viscoelastics cause a
significant rise in intraocular pressure of > 30 mm Hg in 3-10% of patients.
Very high intraocular pressures are often seen postoperatively after
viscoelastic use surgically in patients who preoperatively have a history of
ocular hypertension or glaucoma.
- Language of Publication
- English
- Unique Identifier
- 93249970
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- MeSH Heading (Major)
- Corneal Edema|*CI; Ophthalmic Solutions|*AE; Postoperative Complications|*CI
- MeSH Heading
- Cell Count; Endothelium, Corneal|DE; Eye Diseases|SU; Human; Hydrogen-Ion
Concentration; Irrigation; Osmolar Concentration; Support, Non-U.S. Gov't;
Support, U.S. Gov't, P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 1042-6922
- Country of Publication
- UNITED STATES
- CAS Registry/EC Number
- 0 (Ophthalmic Solutions)


Record 42 from database: MEDLINE
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- Title
- The chemical morphology of the vitreous.
- Author
- Scott JE
- Address
- Manchester University, UK.
- Source
- Eye, 1992, 6 ( Pt 6):, 553-5
- Abstract
- The water of the vitreous is stabilised by an ordered meshwork of very fine
collagen fibrils that are tied together in loosely parallel bundles or sprays by
bridges of sulphated glycosaminoglycan. Some fibril bundles run at right angles
to other bundles. In these respects vitreous resembles a very dilute corneal
stroma. The glycosaminoglycans of the vitreous (hyaluronan and chondroitin
sulphate) aggregate with themselves and with each other in solution. The protein
cores of the proteoglycans are attached to collagen fibrils. Thus, a
three-component cross-linked structure is formed: collagen
fibril-->proteoglycan protein core-->glycosaminoglycan
chain-->glycosaminoglycan chain-->protein core-->collagen fibril.
Hyaluronan can aggregate directly with chondroitin-6-sulphate, or with
aggregated glycan cross-links, thus entering into an infinite meshwork.
- Language of Publication
- English
- Unique Identifier
- 93170515
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- MeSH Heading (Major)
- Vitreous Body|*CH/UL
- MeSH Heading
- Collagen|AN; Glycosaminoglycans|AN; Human; Hyaluronic Acid|AN;
Proteoglycans|AN

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0950-222X
- Country of Publication
- ENGLAND
- CAS Registry/EC Number
- 0 (Glycosaminoglycans); 0 (Proteoglycans); 9004-61-9 (Hyaluronic Acid);
9007-34-5 (Collagen)


Record 43 from database: MEDLINE
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- Title
- Analysis of glycosaminoglycans and their oligosaccharide fragments by
capillary electrophoresis.
- Author
- Grimshaw J
- Address
- School of Chemistry, Queen's University, Belfast, Northern Ireland, UK.
j.grimshaw@qub.ac.uk
- Source
- Electrophoresis, 1997 Nov, 18:12-13, 2408-14
- Abstract
- Glycosaminoglycans are high molecular mass polymers found in living tissues.
They are degraded by site specific enzymes to oligosaccharide fragments.
Polymers and oligomers all carry negative charge and are found as salts soluble
in water. Consequently, capillary electrophoresis has come to the fore as an
analytical technique in this field. This review discusses application of the
technique to the chondroitin-dermatan, heparin and hyaluronan groups of polymer
and the derived oligosaccharides. Direct and indirect UV detection are discussed
as well as detection methods involving precolumn derivatization. Capillary
electrophoresis has found use in the characterisation of heparin and in
following the changes in chondroitin and hyaluronan during the onset of
arthritic disease in humans. Some glycosaminoglycans have been used as
asymmetric anions in the separation of enantiomers of low molecular mass
compounds by capillary electrophoresis.
- Language of Publication
- English
- Unique Identifier
- 98115590
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- MeSH Heading (Major)
- Electrophoresis, Capillary|*MT; Glycosaminoglycans|*AN; Oligosaccharides|*AN
- MeSH Heading
- Carbohydrate Sequence; Human; Molecular Sequence Data; Polymers

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0173-0835
- Country of Publication
- GERMANY


Record 44 from database: MEDLINE
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- Title
- Inhibitory molecules in development and regeneration.
- Author
- Silver J
- Address
- Department of Neurosciences, School of Medicine, Case Western Reserve
University, Cleveland, Ohio 44106.
- Source
- J Neurol, 1994 Dec, 242:1 Suppl 1, S22-4
- Abstract
- In addition to chemotrophic and contact guidance theories that explain how
long projection neurons weave intricate patterns of connectivity within
developing or regenerating neuronal networks, there has been recent interest in
mechanisms that guide axons by actively constraining, inhibiting or repelling
axon growth cones. Developmental boundaries are especially important in regions
where large numbers of growing axons must change direction in order to remain on
course towards their potential targets. Regenerative boundaries can also have
severe pathological consequences since they limit the potential for axon
regrowth following injury or diseases. Some of the molecular mechanisms that
generate repulsive environments in the embryo are re-expressed in the adult
following injury. In the developing retina, a chondroitin sulfate-proteoglycan
appears to play an essential role in controlling the sequence of ganglion cell
differentiation and initial direction of axons. In several lesion models,
re-expression of a chondroitin sulfate-proteoglycan by reactive astrocytes
limits regeneration through glial scars; conversely, in experiments where
boundary molecules have been manipulated by chondroitinase digestion, axons are
stimulated to regrow or re-route to inappropriate pathways.
- Language of Publication
- English
- Unique Identifier
- 95213751
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- MeSH Heading (Major)
- Alzheimer Disease|*PP; Axons|*PH; Nerve Regeneration|*PH; Proteochondroitin
Sulfates|*PH
- MeSH Heading
- Animal; Cell Adhesion Molecules, Neuronal|PH; Extracellular Matrix
Proteins|PH; Gliosis|PP; Human; Nerve Tissue Proteins|PH; Neurites|PH;
Neuroglia|PH; Retina|GD; Up-Regulation (Physiology)

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0340-5354
- Country of Publication
- GERMANY


Record 45 from database: MEDLINE
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- Title
- Proteoglycans: the "Teflon" of the airways?
- Author
- Page CP
- Address
- Sackler Institute of Pulmonary Pharmacology, King's College London Medical
School, UK.
- Source
- Thorax, 1997 Oct, 52:10, 924-5
- Abstract
- Proteoglycans are a family of structurally distinct, polyanionic complex
carbohydrates composed of repeating disaccharide units. Proteoglycans include
heparin, heparan sulphate, chondroitin 4-sulphate, chondroitin 6-sulphate,
dermatan sulphate, and hyaluronic acid. Heparin is found in the granules of a
subset of mast cells where it is bound to various mediators including histamine.
Heparan sulphate has a much wider distribution in the body, being associated
with stromal matrices, basement membrane and many cell surfaces, particularly
the surface of endothelial cells. Heparin is an anticoagulant, but it is now
very apparent that it possesses many other biological activities that have
relevance to our understanding of lung diseases, particularly inflammatory
diseases of the airway. Recent evidence suggests in the airway when administered
by inhalation that could be exploited therapeutically.
- Language of Publication
- English
- Unique Identifier
- 98068194
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- MeSH Heading (Major)
- Heparin|*PH/TU; Lung Diseases|DT/*ME/PA
- MeSH Heading
- Cell Adhesion|PH; Human

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0040-6376
- Country of Publication
- ENGLAND


Record 46 from database: MEDLINE
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- Title
- Proteoglycans in male reproductive tract.
- Author
- Périn JP; Alliel PM; Jollès P; Bonnet F
- Address
- Laboratoire des ProtÆeines, UniversitÆe de Paris V, France.
- Source
- EXS, 1994, 70:, 191-7
- Abstract
- Proteoglycans in male reproductive tract have been mainly characterized in
testicular extracellular matrix and somatic cells. Heparan sulfate, chondroitin
sulfate and hybrid chondroitin/heparan sulfate proteoglycans coexist within the
testes. Their biological roles are not currently established, however, the
molecular characterization of some of them is indicative that they might be
involved in various regulatory processes during spermatogenesis.
- Language of Publication
- English
- Unique Identifier
- 94129147
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- MeSH Heading (Major)
- Genitalia, Male|CH/*PH; Proteoglycans|*AN/BI/CH/*ME
- MeSH Heading
- Adult; Amino Acid Sequence; Animal; Base Sequence; Glycosaminoglycans|AN/ME;
Human; Male; Molecular Sequence Data; Prostate|CH/ME; Prostatic Hyperplasia|ME;
Sertoli Cells|ME; Testis|CH/ME

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- Country of Publication
- SWITZERLAND


Record 47 from database: MEDLINE
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- Title
- Regulation of proteoglycan expression in fibrotic liver and cultured
fat-storing cells.
- Author
- Gressner AM; Krull N; Bachem MG
- Address
- Department of Clinical Chemistry, Philipps University, Marburg, Germany.
- Source
- Pathol Res Pract, 1994 Oct, 190:9-10, 864-82
- Abstract
- Considerable progress has been made in recent years with the molecular
dissection of proteoglycans in normal and fibrotic human and rat liver.
Proteoglycans constitute a major fraction of extracellular, pericellular and
intracellular glycoconjugates. In former times, proteoglycans were classified
nearly exclusively on the basis of the composition of their carbohydrate chain
(glycosaminoglycan, GAG) attached to the core protein. Accordingly, three main
types are discerned in liver, which are in order of decreasing concentrations
heparan sulfate (HS, more than 60% of total GAG), dermatan sulfate and
chondroitin-4,6-sulfate isomers. Keratan sulfate has not been detected in rat
and human liver. Recently, proteoglycans have been characterized by sequencing
and cloning of the core proteins to which a number of specific glycosaminoglycan
side chains are covalently linked. Accordingly, decorin and biglycan have been
identified as major chondroitin sulfate/dermatan sulfate proteoglycans in the
extracellular space. In addition, evidence was obtained recently for the
expression of aggrecan and lumican, both keratan sulfate bearing proteoglycans,
and of syndecan in liver. Using in situ hybridization techniques the temporal
and spatial pattern of expression of biglycan, decorin and aggrecan has been
assessed. These studies together with Northern blot hybridizations performed
with isolated parenchymal and nonparenchymal liver cells confirm that
fat-storing cells (Ito cells, perisinusoidal lipocytes), are the most important,
principal cellular site of proteoglycan production in diseased liver. The level
of expression is regulated by a number of cytokines among which TGF beta, TNF
alpha and TGF alpha play significant roles. The effects of these cytokines on
proteoglycan expression are dependent on the stage of phenotypic transition of
fat storing cells to the activated myofibroblast. Taken together, these data
point to the potentially significant role which proteoglycans might fulfil in
the regulation of cellular functions and in the maintenance of the
supramolecular organization of the extracellular matrix in normal and in
diseased liver during the process of fibrogenesis.
- Language of Publication
- English
- Unique Identifier
- 95207001
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- MeSH Heading (Major)
- Adipocytes|*CH; Gene Expression Regulation|*GE; Liver Cirrhosis|*ME;
Proteoglycans|*BI/GE
- MeSH Heading
- Animal; Cells, Cultured; Extracellular Matrix Proteins|CH;
Glycosaminoglycans|BI; Human; Support, Non-U.S. Gov't

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- ISSN
- 0344-0338
- Country of Publication
- GERMANY


Record 48 from database: MEDLINE
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- Title
- Activation of proteoglycan synthesis in injured liver--a brief review of
molecular and cellular aspects.
- Author
- Gressner AM
- Address
- Department of Clinical Chemistry, Philipps University, Marburg, Germany.
- Source
- Eur J Clin Chem Clin Biochem, 1994 Apr, 32:4, 225-37
- Abstract
- In the past years, considerable progress has been made with the molecular
dissection of proteoglycans in normal and fibrotic human and rat liver. Three
main types of glycosaminoglycans are found in liver, which, in order of
decreasing concentration, are: heparan sulphate (more than 0.6 of total
glycosaminoglycans), dermatan sulphate and chondroitin-4,6-sulphate isomers.
Keratan sulphate has not been detected in rat and human liver. In fibrotic liver
matrix, there is a more than 4-fold increase of the overall concentration of
glycosaminoglycans, which is most pronounced for chondroitin sulphate and
dermatan sulphate and less prominent for heparan sulphate. In fact, the latter
glycosaminoglycan decreases fractionally. Stimulated synthesis rather than
reduced breakdown in response to liver injury has been determined as the main
mechanism of enhanced deposition. Fat-storing cells, a special type of
nonparenchymal liver cells located in the subendothelial space of Disse, are the
principal cellular source of hepatic preoteoglycans. In areas of
necroinflammation, these cells transform into myofibroblasts, which express the
genes for decorin, biglycan, syndecan and presumably other proteoglycans
characterized by cloned core proteins. Proteoglycan synthesis in these cells is
stimulated in a paracrine way mainly by TGF-beta, which is elaborated by
activated Kupffer cells/macrophages and released from disintegrated
thrombocytes. Furthermore, TGF-beta is also secreted by myofibroblasts, which
are stimulated in an autocrine pathway by TGF-beta. Myofibroblasts can also
activate resting (non-transformed) fat-storing cells in a paracrine way. In
addition to TGF-beta, significant roles are also played by TNF-alpha,
TGF-alpha/EGF, PDGF and FGF. Their effects depend on expression of the
respective growth factor receptor that determines the stage of fat-storing cell
transformation, on the interaction with other cytokines/growth factors, and on
the extracellular matrix supporting these cells. Available data point to a
potentially significant role which proteoglycans might fulfil in the regulation
of cellular functions and in the maintenance of the supramolecular organization
of the extracellular matrix in normal and diseased liver, in particular during
the process of liver fibrogenesis.
- Language of Publication
- English
- Unique Identifier
- 94312497
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- MeSH Heading (Major)
- Liver Diseases|*ME; Proteoglycans|*BI
- MeSH Heading
- Animal; Human; Liver|ME; Rats

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0939-4974
- Country of Publication
- GERMANY


Record 49 from database: MEDLINE
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- Title
- Molecular cloning and analysis of the protein modules of aggrecans.
- Author
- Upholt WB; Chandrasekaran L; Tanzer ML
- Address
- Department of BioStructure and Function, School of Dental Medicine,
University of Connecticut Health Center, Farmington 06030-3705.
- Source
- EXS, 1994, 70:, 37-52
- Abstract
- The large aggregating chondroitin sulfate proteoglycan of cartilage,
aggrecan, has served as a prototype of proteoglycan structure. Molecular cloning
has elucidated its primary structure and revealed both known and unknown
domains. To date the complete structures of chicken, rat and human aggrecans
have been deduced, while partial sequences have been reported for bovine
aggrecan. A related proteoglycan, human versican, has also been cloned and
sequenced. Both aggrecan and versican have two lectin domains, one at the
amino-terminus which binds hyaluronic acid and one at the carboxyl-terminus
whose physiological ligand is unknown. Both lectins have homologous counterparts
in other types of proteins. Within the aggrecans the keratan sulfate domain may
be variably present and also has a prominent repeat in some species. The
chondroitin sulfate domain has three distinct regions which vary in their
prominence in different species. The complex molecular structure of aggrecans is
consistent with the concept of exon shuffling and aggrecans serve as suitable
prototypes for comprehending the evolution of multi-domain proteins.
- Language of Publication
- English
- Unique Identifier
- 94129152
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- MeSH Heading (Major)
- Proteoglycans|*BI/*CH/GE
- MeSH Heading
- Amino Acid Sequence; Animal; Cattle; Chickens; Cloning, Molecular|MT;
Comparative Study; Consensus Sequence; Evolution; Human; Molecular Sequence
Data; Proteochondroitin Sulfates|BI/CH; Rats; RNA, Messenger|ME

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- Country of Publication
- SWITZERLAND


Record 50 from database: MEDLINE
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- Title
- Altered proteoglycan gene expression and the tumor stroma.
- Author
- Iozzo RV; Cohen I
- Address
- Department of Pathology and Cell Biology, Thomas Jefferson University,
Philadelphia, Pennsylvania 19107.
- Source
- EXS, 1994, 70:, 199-214
- Abstract
- Tumor stroma is a specialized form of tissue that is associated with
epithelial neoplasms. Recent evidence indicates that significant changes in
proteoglycan content occur in the tumor stroma and that these alterations could
support tumor progression and invasion as well as tumor growth. Our main
hypothesis is that the generation of tumor stroma is under direct control of the
neoplastic cells and that, via a feedback loop, altered proteoglycan gene
expression would influence the behavior of tumor cells. In this review, we will
focus primarily on the work from our laboratory related to the altered
expression of chondroitin sulfate proteoglycan and its role in tumor development
and progression. The connective tissue stroma of human colon cancer is enriched
in chondroitin sulfate and the stromal cell elements, primarily colon
fibroblasts and smooth muscle cells, are responsible for this biosynthetic
increase. These changes can be reproduced in vitro by using either tumor
metabolites or co-cultures of human colon carcinoma cells and colon mesenchymal
cells. The levels of decorin, a leucine-rich proteoglycan involved in the
regulation of matrix assembly and cell proliferation, are markedly elevated in
the stroma of colon carcinoma. These changes correlate with a marked increase in
decorin mRNA levels and a concurrent hypomethylation of decorin gene, a DNA
alteration associated with enhanced gene expression. Elucidation of decorin gene
structure has revealed an unexpected degree of complexity in the 5' untranslated
region of the gene with two leader exons that are alternatively spliced to the
second coding exon. Furthermore, a transforming growth factor beta
(TGF-beta)-negative element is present in the promotor region of decorin
gene.(ABSTRACT TRUNCATED AT 250 WORDS)
- Language of Publication
- English
- Unique Identifier
- 94129148
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- MeSH Heading (Major)
- Connective Tissue|*ME; Gene Expression|*; Neoplasms|*ME;
Proteoglycans|*BI/UL
- MeSH Heading
- Alternative Splicing; Animal; Base Sequence; Consensus Sequence; Gene
Expression Regulation, Neoplastic; Human; Molecular Sequence Data; Promoter
Regions (Genetics); RNA, Messenger|ME; Support, Non-U.S. Gov't; Support, U.S.
Gov't, P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- Country of Publication
- SWITZERLAND


Record 51 from database: MEDLINE
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- Title
- CD44: structure, function, and association with the malignant process.
- Author
- Naot D; Sionov RV; Ish Shalom D
- Address
- Lautenberg Center for General and Tumor Immunology, Hebrew
University-Hadassah Medical School, Jerusalem, Israel.
- Source
- Adv Cancer Res, 1997, 71:, 241-319
- Abstract
- CD44 is a ubiquitous multistructural and multifunctional cells surface
adhesion molecule involved in cell-cell and cell-matrix interactions. Twenty
exons are involved in the genomic organization of this molecule. The first five
and the last 5 exons are constant, whereas the 10 exons located between these
regions are subjected to alternative splicing, resulting in the generation of a
variable region. Differential utilization of the 10 variable region exons, as
well as variations in N-glycosylation, O-glycosylation, and
glycosaminoglycanation (by heparan sulfate or chondroitin sulfate), generate
multiple isoforms (at least 20 are known) of different molecular sizes (85-230
kDa). The smallest CD44 molecule (85-95 kDa), which lacks the entire variable
region, is standard CD44 (CD44s). As it is expressed mainly on cells of
lymphohematopoietic origin, CD44s is also known as hematopoietic CD44 (CD44H).
CD44s is a single-chain molecule composed of a distal extracellular domain
(containing, the ligand-binding sites), a membrane-proximal region, a
transmembrane-spanning domain, and a cytoplasmic tail. The molecular sequence
(with the exception of the membrane-proximal region) displays high interspecies
homology. After immunological activation, T lymphocytes and other leukocytes
transiently upregulate CD44 isoforms expressing variant exons (designated
CD44v). A CD44 isform containing the last 3 exon products of the variable region
(CD44V8-10, also known as epithelial CD44 or CD44E), is preferentially expressed
on epithelial cells. The longest CD44 isoform expressing in tandem eight exons
of the variable region (CD44V3-10) was detected in keratinocytes. Hyaluronic
acid (HA), an important component of the extracellular matrix (ECM), is the
principal, but by no means the only, ligand of CD44. Other CD44 ligands include
the ECM components collagen, fibronectin, laminin, and chondroitin sulfate.
Mucosal addressin, serglycin, osteopontin, and the class II invariant chain (Ii)
are additional, ECM-unrelated, ligands of the molecule. In many, but not in all
cases, CD44 does not bind HA unless it is stimulated by phorbol esters,
activated by agonistic anti-CD44 antibody, or deglycosylated (e.g., by
tunicamycin). CD44 is a multifunctional receptor involved in cell-cell and
cell-ECM interactions, cell traffic, lymph node homing, presentation of
chemokines and growth factors to traveling cells, and transmission of growth
signals. CD44 also participates in the uptake and intracellular degradation of
HA, as well as in transmission of signals mediating hematopoiesis and apoptosis.
Many cancer cell types as well as their metastases express high levels of CD44.
Whereas some tumors, such as gliomas, exclusively express standard CD44, other
neoplasms, including gastrointestinal cancer, bladder cancer, uterine cervical
cancer, breast cancer and non-Hodgkin's lymphomas, also express CD44 variants.
Hence CD44, particularly its variants, may be used as diagnostic or prognostic
markers of at least some human malignant diseases. Furthermore, it has been
shown in animal models that injection of reagents interfering with CD44-ligand
interaction (e.g., CD44s- or CD44v-specific antibodies) inhibit local tumor
growth and metastatic spread. These findings suggest that CD44 may confer a
growth advantage on some neoplastic cells and, therefore, could be used as a
target for cancer therapy. It is hoped that identification of CD44 variants
expressed on cancer but not on normal cells will lead to the development of
anti-CD44 reagents restricted to the neoplastic growth.
- Language of Publication
- English
- Unique Identifier
- 97266064
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- MeSH Heading (Major)
- Antigens, CD44|*PH; Cell Adhesion Molecules|*PH; Hyaluronic Acid|*ME;
Neoplasms|*PA
- MeSH Heading
- Alternative Splicing; Animal; Apoptosis; Arthritis, Rheumatoid|PP; Binding
Sites; Cell Adhesion; Cell Aggregation; Cell Movement; Cytokines|ME;
Cytoskeleton|PH; Endometrium|PH; Endothelium|CY; Extracellular Matrix|ME;
Female; Genes, Structural; Glycosylation; Growth Substances|ME; Hematopoiesis;
Human; Ligands; Malaria|IM; Membrane Glycoproteins|PH; Menstruation; Neoplasm
Metastasis; Nomenclature; Support, Non-U.S. Gov't; Wound Healing

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- ISSN
- 0065-230X
- Country of Publication
- UNITED STATES


Record 52 from database: MEDLINE
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- Title
- Basement membranes and pulmonary development.
- Author
- Sannes PL; Wang J
- Address
- Department of Anatomy, Physiological Sciences, and Radiology, College of
Veterinary Medicine, North Carolina State University, Raleigh 27606, USA.
philip_sannes@ncsu.edu
- Source
- Exp Lung Res, 1997 Mar, 23:2, 101-8
- Abstract
- Basement membranes (BM) are specialized extracellular matrices (ECM) which
serve as complex interfaces between epithelia, peripheral nerves, or muscle
cells and their surrounding tissue microenvironments. Their composition is known
to include type IV collagen, laminin, entactin, heparan sulfate proteoglycan
(HSPG, perlecan), and chondroitin sulfate proteoglycan (CSPG). By
immunohistochemistry, collagen IV, laminin, and entactin are detectable from day
14 of gestation on, and become progressively more prominent with time. Perleaan
has not been examined in prentatal lungs, but is widely distributed and abundant
in all lung MBs from birth throughout development. CSPG has a somewhat
discontinuous and lightly reactive appearance in alveolar BMs at birth but the
staining becomes continuous and darker in the adult. This contrasts with
glycosaminoglycan, chondroitin sulfate, which is prominently expressed in
prenatal and early postnatal stages, but progressively diminishes with advancing
development. As an interface between cell populations and surrounding ECMs, BMs
act as a physical barrier to some cells and molecules, while serving as
attachment points and binding sites for others. Basic fibroblast growth factor
is an example of the latter, because it localizes with all BM components by
immunostaining throughout development and reflects the multifactorial array of
potential effectors in the complex processes of proliferation and
differentiation.
- Language of Publication
- English
- Unique Identifier
- 97244109
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- MeSH Heading (Major)
- Lung|CH/*EM/*GD
- MeSH Heading
- Animal; Basement Membrane|CH/EM/GD; Extracellular Matrix|CH/PH; Fetal
Development; Human; Mesoderm|PH; Support, Non-U.S. Gov't; Support, U.S. Gov't,
P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0190-2148
- Country of Publication
- UNITED STATES


Record 53 from database: MEDLINE
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- Title
- Functions of brain chondroitin sulfate proteoglycans during developments:
interactions with adhesion molecules.
- Author
- Grumet M; Friedlander DR; Sakurai T
- Address
- Department of Pharmacology, New York University Medical Center, New York
10016, USA.
- Source
- Perspect Dev Neurobiol, 1996, 3:4, 319-30
- Abstract
- Chondroitin sulfate proteoglycans (CSPGs), including neurocan and
phosphocan, are believed to be major components of brain extracellular matrix
that interact with other matrix proteins and cell surface receptors. In
addition, several brain CSPGs such as receptor protein tyrosine phosphatase beta
are expressed as cell surface receptors that interact with proteins in the
extracellular matrix and with receptors on neural cells. Recent in vitro studies
demonstrate that, although the brain CSPGs neurocan and phosphocan can promote
transient adhesion of neuronal cells, they inhibit stable cell adhesion and
neurite growth promoted by the cell adhesion molecule Ng-CAM/L1. Neurocan and
phosphocan bind with high affinity to Ng-CAM/L1 and N-CAM which may be their
major receptors on neurons. These CSPGs also bind to other adhesion molecules,
such as tenascin-C, and can differentially modulate adhesion of glia of
tenascin-C. Both the glycosaminoglycan and the core glycoproteins contribute to
the function of the brain CSPGs. When expressed in regions containing low levels
of adhesion molecules, various CSPGs including phosphocan, neurocan, versican,
aggrecan, and NG2 proteoglycan may act as barriers to cell migration and axonal
growth. In regions containing high levels of adhesion proteins, brain CSPGs may
still act to maintain certain boundaries while allowing selective axonal
extension to proceed. There are numerous regions of overlap in the expression
patterns of CSPGs and adhesion molecules in vivo, and the relative levels of
these molecules as well as the organization of the extracellular matrix may be
important factors that regulate the rate of axonal growth locally. Differential
expression of CSPGs may be important for modulating cell adhesion as well as
axonal growth and guidance during neural development, and continued expression
may prevent these processes in the normal nature nervous system as well as
following brain injury.
- Language of Publication
- English
- Unique Identifier
- 97166461
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- MeSH Heading (Major)
- Aging|*PH; Brain|*ME; Cell Adhesion Molecules|*PH; Proteochondroitin
Sulfates|*PH
- MeSH Heading
- Animal; Human; Nerve Tissue Proteins|PH; Support, U.S. Gov't, P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 1064-0517
- Country of Publication
- UNITED STATES


Record 54 from database: MEDLINE
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- Title
- The NG2 chondroitin sulfate proteoglycan: a multifunctional proteoglycan
associated with immature cells.
- Author
- Levine JM; Nishiyama A
- Address
- Department of Neurobiology and Behavior, State University of New York at
Stony Brook 11794, USA.
- Source
- Perspect Dev Neurobiol, 1996, 3:4, 245-59
- Abstract
- In this review, we discuss the properties of the NG2 chondroitin sulfate
proteoglycan, a structurally unique, integral membrane proteoglycan that is
found on the surfaces of several different types of immature cells. NG2 is
associated with multipotential glial precursor cells (O2A progenitor cells),
chondroblasts of the developing cartilage, brain capillary endothelial cells,
aortic smooth muscle cells, skeletal myoblasts and human melanoma cells. One
common feature of these diverse cell types is that they retain the ability to
divide throughout the life of the organism. The NG2 proteoglycan is a
multifunctional protein; in vitro studies have shown that NG2 binds type VI
collagen, interacts with and modulates the activity of the platelet-derived
growth factor-alpha receptor, and inhibits neurite outgrowth. These functional
properties are analogous to those of other proteoglycans such as syndecan,
betaglycan, and neurocan, suggesting that structurally divergent proteoglycans
can carry out similar functions within the organism.
- Language of Publication
- English
- Unique Identifier
- 97166456
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- MeSH Heading (Major)
- Antigens|CH/ME/*PH; Proteoglycans|CH/ME/*PH
- MeSH Heading
- Animal; Cell Aging; Human; Support, Non-U.S. Gov't; Support, U.S. Gov't,
P.H.S.; Tissue Distribution

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 1064-0517
- Country of Publication
- UNITED STATES


Record 55 from database: MEDLINE
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- Title
- Viscoelastic substances in ophthalmology.
- Author
- Liesegang TJ
- Address
- Section of Ophthalmology, Mayo Clinic, Jacksonville, Florida.
- Source
- Surv Ophthalmol, 1990 Jan-Feb, 34:4, 268-93
- Abstract
- The desirable properties of a viscoelastic substance for ophthalmologic
applications are intimately tied to its chemical and rheologic properties. This
report describes the relevant rheologic properties (e.g., viscosity,
viscoelasticity, pseudoplasticity, cohesiveness, and coatability) of the
available viscoelastic substances and presents the general principles of their
use as well as some specific technical aspects. In addition, the various uses of
viscoelastic substances in ophthalmic surgery are outlined. There is no single
ideal substance for all circumstances. With a knowledge of the rheologic
properties of each substance, the ophthalmologist will be able to choose among
the different ones as necessary to suit each clinical situation.
- Language of Publication
- English
- Unique Identifier
- 90260754
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- MeSH Heading (Major)
- Biocompatible Materials|*; Eye|*SU
- MeSH Heading
- Acrylic Resins; Animal; Chondroitin Sulfates; Collagen; Human; Hyaluronic
Acid; Methylcellulose|AA; Rheology; Viscosity

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- ISSN
- 0039-6257
- Country of Publication
- UNITED STATES
- CAS Registry/EC Number
- 0 (Acrylic Resins); 0 (Biocompatible Materials); 9003-05-8 (polyacrylamide);
9004-61-9 (Hyaluronic Acid); 9004-65-3 (hydroxypropyl methylcellulose);
9004-67-5 (Methylcellulose); 9007-28-7 (Chondroitin Sulfates); 9007-34-5
(Collagen)


Record 56 from database: MEDLINE
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- Title
- Glycosaminoglycans in autoimmunity.
- Author
- Hansen C; Otto E; Kuhlemann K; Förster G; Kahaly GJ
- Address
- Department of Medicine III, Johannes Gutenberg-University Hospital, Mainz,
Germany.
- Source
- Clin Exp Rheumatol, 1996 May, 14 Suppl 15:, S59-67
- Abstract
- Alteration of the distribution pattern and composition of glycosaminoglycans
(GAG) and proteoglycans may play an important role in the development of
autoimmune diseases. Recent experiments indicate that anti-DNA antibodies
cross-reacting with hyaluronic acid, heparan sulphate and chondroitin sulphate
are present in patients with systemic lupus erythematosus. Furthermore, elevated
hyaluronic acid antibody levels correlating with the disease score have been
found in the sera of patients with autoimmune thyroid disease in comparison to
controls. In vitro, T lymphocytes from patients with this disease increased the
production of hyaluronic acid by cultured human retro-orbital fibroblasts.
Fibroblast stimulation, as well as elevated collagen and GAG production, could
be shown in chicken cell lines which spontaneously develop an autoimmune
syndrome analogous to human scleroderma. To analyse the structure and
distribution pattern of different GAG compounds in the tissues and body fluids
of patients with autoimmune diseases a highly specific HPLC method was
developed, which revealed increased urinary chondroitin sulphate and dermatan
sulphate concentrations in patients with autoimmune thyroid disease in
comparison to controls, concentrations which were positively correlated with
disease severity and disease activity. Furthermore, the renal GAG excretion in
patients with autoimmune diabetes mellitus was studied, and markedly higher
excretion in patients compared to healthy controls was found, which was
correlated with the duration of the disease and diabetic late complications.
Thus, GAG polysaccharides not only appear to play a major role in the
pathogenesis of autoimmune diseases, but have been successfully introduced as an
activity marker of the disease.
- Language of Publication
- English
- Unique Identifier
- 96426671
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- MeSH Heading (Major)
- Autoimmunity|*PH; Glycosaminoglycans|CH/*ME
- MeSH Heading
- Animal; Antibody Formation|PH; Autoimmune Diseases|IM/ME; Diabetes Mellitus,
Insulin-Dependent|IM; Human; Immunity, Cellular|PH; Thyroid Gland|IM

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0392-856X
- Country of Publication
- ITALY


Record 57 from database: MEDLINE
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- Title
- Adhesion molecules in neural crest development.
- Author
- Newgreen DF; Tan SS
- Address
- Embryology Laboratory, Murdoch Institute, Parkville, Victoria, Australia.
- Source
- Pharmacol Ther, 1993 Dec, 60:3, 517-37
- Abstract
- Peripheral nerve cells, various endocrine and pigment cells and cranial
connective tissue cells of vertebrates stem mainly from the embryonic neural
crest. This originates with the central nervous system, but the crest cells
detach from this tissue, via a decrease of cell-cell adhesion involving,
particularly, a reduction of the adherens junction cell adhesive molecule A-CAM.
This epithelio-mesenchymal transformation allows crest cells to migrate along
pathways that are defined partly by the distribution of substrate adhesion
molecules, the archetype being fibronectin, an extracellular matrix molecule
recognized by integrin receptors on crest cells. Many other molecules, however,
may act in the same way. In contrast, some molecules may define migration
pathways by reducing adhesion; chondroitin sulfate proteoglycan is a candidate
for this role. Pathway selection is most likely achieved by balanced
combinations of molecules that promote and reduce adhesion. Cessation of
migration, in the case of the nervous ganglia, correlated with re-expression of
cell-cell adhesion molecules like A-CAM and others, consistent with an adhesive
basis, although functional tests have not yet been performed. The development of
the neural crest system provides a useful model that emphasizes the role of
adhesion in morphogenesis.
- Language of Publication
- English
- Unique Identifier
- 94353009
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- MeSH Heading (Major)
- Cell Adhesion Molecules|*PH; Neural Crest|*EM
- MeSH Heading
- Amino Acid Sequence; Animal; Cell Adhesion|PH; Cell Movement|PH;
Collagen|PH; Extracellular Matrix|PH; Fibronectins|PH; Human; Intrinsic
Factor|PH; Laminin|PH; Molecular Sequence Data; Morphogenesis

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- ISSN
- 0163-7258
- Country of Publication
- ENGLAND
- CAS Registry/EC Number
- 0 (Cell Adhesion Molecules); 0 (Fibronectins); 0 (Laminin); 9007-34-5
(Collagen); 9008-12-2 (Intrinsic Factor)


Record 58 from database: MEDLINE
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- Title
- Functional domains of the human C1q A-chain.
- Author
- Trinder PK; Maeurer MJ; Kaul M; Petry E; Loos M
- Address
- Institute of Medical Microbiology, Johannes Gutenberg University, Hochhaus
am Augustusplatz, Mainz, Germany.
- Source
- Behring Inst Mitt, 1993 Dec, :93, 180-8
- Abstract
- This brief review was inspired by discussions relating to the IIIrd.
International C1 Workshop (this volume) and the realization that certain
functional properties of the C1q molecule are limited exclusively to the
A-chain. The collagen-like region of the A-chain contains a major binding site
for non-immunoglobulin substances, which include C-reactive protein, serum
amyloid P, LPS and DNA. This binding site is immediately adjacent to, and
partially overlapping with, an arthritis-modulating epitope common to the C1q
A-chain and various types of collagen, including cartilage type II collagen. At
the N-terminal end of the C1q A-chain is a leader peptide sequence that anchors
the intact C1q molecule firmly in the membrane of macrophages, the C1q molecule
can thus be classified as a type II membrane protein, functioning as an
additional ceptor for molecules known to react with C1q in fluid phase such as
the Fc region of IgG, LPS and polyanionic molecules (e.g. chondroitin sulphate,
heparin, dextran sulphate etc.). The various domains within the A-chain, and
their respective functions (or potential functions), are presented and discussed
in the context of the intact C1 molecule and with regard to any wider functional
relevance.
- Language of Publication
- English
- Unique Identifier
- 94226567
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- MeSH Heading (Major)
- Complement 1q|*CH/*ME
- MeSH Heading
- Amino Acid Sequence; Animal; Arthritis, Adjuvant|IM; Binding Sites;
Collagen|CH/ME; Comparative Study; Human; Macromolecular Systems; Molecular
Sequence Data; Protein Conformation; Sequence Homology, Amino Acid; Signal
Peptides|CH/ME

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0301-0457
- Country of Publication
- GERMANY
- CAS Registry/EC Number
- 0 (Macromolecular Systems); 0 (Signal Peptides); 80295-33-6 (Complement 1q);
9007-34-5 (Collagen)


Record 59 from database: MEDLINE
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- Title
- The mast cell--a potential link between inflammation and cellular
cholesterol deposition in atherogenesis.
- Author
- Kovanen PT
- Address
- Wihuri Research Institute, Helsinki, Finland.
- Source
- Eur Heart J, 1993 Dec, 14 Suppl K:, 105-17
- Abstract
- Mast cells are present in the arterial intima, the site of atherogenesis. In
fatty streaks (the initial stage of atherogenesis) some of these cells are
detected in the close vicinity of cholesterol-loaded macrophage foam cells. To
ascertain whether mast cells could be involved in the formation of foam cells, a
model system was developed in which isolated rat serosal mast cells were
incubated with mouse peritoneal macrophages in a medium enriched with either low
density lipoproteins (LDL) or high density lipoproteins (HDL3). Stimulation of
the mast cells was found to induce 50-fold enhancement of LDL uptake by the
macrophages. When stimulated, mast cells exocytose their secretory granules,
which lose their membranes in the process. The granules then come in contact
with the medium, which dissolves their histamine, a fraction of their heparin
proteoglycans and all their chondroitin sulphate proteoglycans, leaving
insoluble 'granule remnants'. These remnants consist of neutral proteases
embedded in a heparin proteoglycan matrix. Some of the LDL particles in the
incubation medium bind to this matrix, become degraded by the matrix-bound
proteases, and fuse into larger particles on the surfaces of the remnants. These
LDL particles are ingested by the macrophages as they phagocytose the remnants.
Simultaneously, the soluble heparin proteoglycans interact with other LDL
particles, forming insoluble complexes which are also phagocytosed by the
macrophages. Cholesterol from the phagocytosed LDL particles ultimately becomes
esterified in the macrophages, with formation of foam cells. In addition, mast
cells block the removal of cholesterol from the foam cells: the remnant enzymes
proteolyse HDL particles, so lessening their ability to induce efflux of
cholesterol from the foam cells. These observations suggest that mast cells play
an active role in the intracellular deposition of cholesteryl esters that is
characteristic of early atherosclerotic lesions.
- Language of Publication
- English
- Unique Identifier
- 94178292
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- MeSH Heading (Major)
- Atherosclerosis|ET/*ME/PA; Cholesterol|*ME; Inflammation|CO/*ME; Mast
Cells|ME/*PH
- MeSH Heading
- Animal; Cell Degranulation; Exocytosis; Heparin|ME; Human; Lipoproteins,
LDL|ME; Macrophages|ME; Peptide Peptidohydrolases|ME; Phagocytosis;
Proteoglycans|ME; Rats

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0195-668X
- Country of Publication
- ENGLAND
- CAS Registry/EC Number
- EC 3.4.- (Peptide Peptidohydrolases); 0 (Lipoproteins, LDL); 0
(Proteoglycans); 57-88-5 (Cholesterol); 9005-49-6 (Heparin)


Record 60 from database: MEDLINE
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- Title
- Effects of extracellular matrix components on cell locomotion.
- Author
- McCarthy J; Turley EA
- Address
- Department of Laboratory Medicine and Pathology, University of Minnesota,
Minneapolis.
- Source
- Crit Rev Oral Biol Med, 1993, 4:5, 619-37
- Abstract
- The extracellular matrix (ecm), which is composed of collagens,
glycoproteins, and proteoglycans, has emerged as an important regulator of cell
locomotion. This review describes some of the mechanisms by which the ecm may
regulate locomotion, focusing primarily on cell extension and lamellae
formation. Ecm-receptor interactions form an important part of cell recognition
of ecm. Such interactions can result in altered cell adhesion, signal
transduction, and cytoskeletal organization, all of which impact on cell
locomotion. It is important to note that although the effects of single ecm
components have been studied, generally, the cell is likely to perceive ecm in
vivo as a macromolecular complex. It will fall to future work to define how
complexes of ecm regulate cell behavior. Because of our own particular research
bias, we focus on reviewing the role of fibronectin, integrins, chondroitin
sulfate, hyaluronan, and hyaluronan receptors in the regulation of cell
locomotion and examine their effect on adhesion, signal transduction, and
cytoskeletal integrity. Cytoskeleton assembly mechanisms, particularly those
that might be regulated by the ecm, are also described. These events are
summarized in a working model of ecm-promoted locomotion.
- Language of Publication
- English
- Unique Identifier
- 94122309
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- MeSH Heading (Major)
- Cell Movement|*; Extracellular Matrix|*PH
- MeSH Heading
- Animal; Cell Adhesion; Cell Adhesion Molecules; Cell Communication;
Cytoskeleton|PH; Human; Integrins; Receptors, Cell Surface; Signal Transduction

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- ISSN
- 1045-4411
- Country of Publication
- UNITED STATES
- CAS Registry/EC Number
- 0 (extracellular matrix receptor); 0 (Cell Adhesion Molecules); 0
(Integrins); 0 (Receptors, Cell Surface)


Record 61 from database: MEDLINE
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- Title
- Proteoglycans and the modulation of cell adhesion by steric exclusion.
- Author
- Morris JE
- Address
- Department of Zoology, Oregon State University, Corvallis 97331.
- Source
- Dev Dyn, 1993 Apr, 196:4, 246-51
- Abstract
- The hypothesis that cell aggregation may be driven by linear polymers in the
matrix, particularly glycosaminoglycans, is revisited in light of more recent
evidence. A model is proposed that extends the concept of steric exclusion to
include a role in determining the directionality of cell migration and neurite
extension. Recent literature is reviewed to support the conclusion that in
living tissues the theoretical conditions for driving aggregation and migration
by steric exclusion are met. The ability of a linear polymer to exclude cells is
a function of its viscosity, which is optimum with glycosaminoglycans similar to
chondroitin sulfate. It is ineffective with low viscosity glycosaminoglycans
such as most heparin or heparan sulfate. Hyaluronic acid, a massive polymer,
excludes cells poorly when present as an open matrix gel but forms an effective
exclusion barrier when attached to the cell surface. According to a model for
steric exclusion in organogenesis, when cells have a glycocalyx of linear
polymer, they should disperse and migrate down a viscosity gradient of excluding
matrix polymer; when they shed or internalize their surface coat in the
continued presence of matrix, they should be excluded into a smaller volume and
thus stimulated to aggregate.
- Language of Publication
- English
- Unique Identifier
- 94033691
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- MeSH Heading (Major)
- Cell Adhesion|*PH; Proteoglycans|*PH
- MeSH Heading
- Animal; Cell Aggregation|PH; Cell Movement|PH; Extracellular Matrix|PH;
Fetal Development|PH; Human; Models, Biological; Support, U.S. Gov't, P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 1058-8388
- Country of Publication
- UNITED STATES
- CAS Registry/EC Number
- 0 (Proteoglycans)


Record 62 from database: MEDLINE
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- Title
- Proteoglycans of basement membranes.
- Author
- Timpl R
- Address
- Max-Planck-Institut für Biochemie, Martinsried, Germany.
- Source
- Experientia, 1993 May 15, 49:5, 417-28
- Abstract
- Proteoglycans carrying either heparan sulfate and/or chondroitin sulfate
side chains are typical constituents of basement membranes. The most prominent
proteoglycan (perlecan) consists of a 400-500 kDa core protein and three heparan
sulfate chains. Electron microscopy and cDNA sequencing show a complex and
elongated domain structure for the core protein which in part is homologous to
that of the laminin A chain. This structure may be varied by alternative
splicing and proteolysis. Integration into basement membranes probably occurs by
heparan sulfate binding to laminin and collagen IV, core protein binding to
nidogen and by limited self assembly. The proteoglycan is in addition a
cell-adhesive protein which is recognized by beta 1 integrins. Several more
proteoglycans with smaller core proteins (10-160 kDa) apparently exist in
basement membranes but are less well characterized. Biological functions include
control of filtration through basement membranes and binding of growth factors
and protease inhibitors.
- Language of Publication
- English
- Unique Identifier
- 93272926
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- MeSH Heading (Major)
- Basement Membrane|*CH; Proteoglycans|*ME
- MeSH Heading
- Amino Acid Sequence; Animal; Cell Adhesion; Cell Division; Extracellular
Matrix Proteins|ME; Heparitin Sulfate|ME; Human; Molecular Sequence Data;
Peptide Peptidohydrolases|ME; Proteochondroitin Sulfates|ME; Support, Non-U.S.
Gov't; Tissue Distribution

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- ISSN
- 0014-4754
- Country of Publication
- SWITZERLAND
- CAS Registry/EC Number
- EC 3.4.- (Peptide Peptidohydrolases); 0 (Extracellular Matrix Proteins); 0
(Proteochondroitin Sulfates); 0 (Proteoglycans); 143972-95-6 (perlecan);
9050-30-0 (Heparitin Sulfate)


Record 63 from database: MEDLINE
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- Title
- Small proteoglycans.
- Author
- Kresse H; Hausser H; Schönherr E
- Address
- Institute of Physiological Chemistry and Pathobiochemistry, University of
Münster, Germany.
- Source
- Experientia, 1993 May 15, 49:5, 403-16
- Abstract
- In this review the structure and functions of two non-related proteoglycan
families are discussed. One family represents a group of extracellular matrix
macromolecules characterized by core proteins with leucine-rich repeat motifs.
Within this family special attention is given to those members which carry
chondroitin or dermatan sulfate glycosaminoglycan chains. The second family is
characterized by repeat sequences of serine and glycine. Their members are
products of a single core protein gene and are characteristic constituents of
secretory vesicles in cells of the haematopoietic lineage.
- Language of Publication
- English
- Unique Identifier
- 93272925
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- MeSH Heading (Major)
- Proteoglycans|CH/ME/*PH
- MeSH Heading
- Animal; Collagen|ME; Extracellular Matrix Proteins|CH/PH; Hematopoietic Stem
Cells|UL; Human; Molecular Weight; Repetitive Sequences, Nucleic Acid; Support,
Non-U.S. Gov't; Viral Core Proteins|CH

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- ISSN
- 0014-4754
- Country of Publication
- SWITZERLAND
- CAS Registry/EC Number
- 0 (decorin); 0 (serglycin); 0 (Extracellular Matrix Proteins); 0
(Proteoglycans); 0 (Viral Core Proteins); 9007-34-5 (Collagen)


Record 64 from database: MEDLINE
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- Title
- The link proteins.
- Author
- Neame PJ; Barry FP
- Address
- Shriners Hospital for Crippled Children, Tampa, Florida.
- Source
- Experientia, 1993 May 15, 49:5, 393-402
- Abstract
- Aggregates of chondroitin-keratan sulfate proteoglycan (aggrecan) and
hyaluronic acid (hyaluronan) are the major space-filling components of
cartilage. A glycoprotein, link protein (LP; 40-48 kDa) stabilizes the aggregate
by binding to both hyaluronic acid and aggrecan. In the absence of LP,
aggregates are smaller (as estimated by rotary shadowing of electron
micrographs) and less stable (they dissociate at pH 5) than they are in the
presence of LP. The proteoglycan aggregate, including LP, is dissociated in the
presence of chaotropes such as 4 M guanidine hydrochloride. On removal of the
chaotrope, the complex will reassociate. This forms the basis of the isolation
of LP from cartilage and has been described in detail elsewhere. Tryptic
digestion of the proteoglycan aggregates results in a high molecular weight
product that consists of hyaluronic acid to which is bound LP and the N-terminal
globular domain of aggrecan (hyaluronic acid binding region; HABR) in a 1:1
stoichiometry. The amino acid sequences of LP and HABR are surprisingly similar.
The amino acid sequence can be divided into three domains; an N-terminal domain
that falls into the immunoglobulin super-family and two C-terminal domains that
are similar to each other. The DNA structure echoes this similarity, in that the
major domains are reflected in three separate exons in both LP and HABR. The two
C-terminal domains are largely responsible for the association with HA and are
related to two recently described hyaluronate-binding proteins, CD44 and TSG-6.
A variety of approaches, including analysis of the forms of LP found in vivo,
rotary shadowing and analysis of the sequence in the immunoglobulin-like domain,
have shed considerable light on the structure-function relationships of LP. This
review describes the structure and function of LP in detail, focusing on what
can be inferred from the similarity of LP, HABR and related molecules such as
immunoglobulins and lymphocyte HA-receptors.
- Language of Publication
- English
- Unique Identifier
- 93272924
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- MeSH Heading (Major)
- Proteins|CL/*PH; Proteoglycans|CH/CL/*PH
- MeSH Heading
- Amino Acid Sequence; Animal; Comparative Study; Exons; Gene Expression;
Genes, Structural; Human; Hyaluronic Acid|ME; Molecular Sequence Data;
Nomenclature; Peptide Fragments; Protein Structure, Tertiary; Proteochondroitin
Sulfates|CH; RNA, Messenger|GE; Sequence Alignment; Structure-Activity
Relationship; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- ISSN
- 0014-4754
- Country of Publication
- SWITZERLAND
- CAS Registry/EC Number
- 0 (aggrecan); 0 (link proteins); 0 (Peptide Fragments); 0 (Proteins); 0
(Proteochondroitin Sulfates); 0 (Proteoglycans); 0 (RNA, Messenger); 126968-45-4
(versican); 9004-61-9 (Hyaluronic Acid)


Record 65 from database: MEDLINE
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- Title
- Genetic defects in proteoglycan biosynthesis.
- Author
- Quentin-Hoffmann E; Harrach B; Robenek H; Kresse H
- Address
- Institute of Physiological Chemistry and Pathobiochemistry, University of
Münster, Federal Republic of Germany.
- Source
- Padiatr Padol, 1993, 28:1, 37-41
- Abstract
- An overview on the structure of proteoglycans and on genetic defects in
proteoglycan biosynthesis is given. Several patients with progeroid-like
symptoms have been shown to have abnormalities in the biosynthesis of
chondroitin/dermatan sulfate proteoglycans. A partial inactivity of
galactosyltransferase I which catalyzes the second glycosyl transfer reaction in
the assembly of glycosaminoglycan chains has been shown to represent the primary
defect in one of the patients. A diminished concentration of a
collagen-associated proteoglycan is considered to play a pathogenetic role in
the development of loose skin.
- Language of Publication
- English
- Unique Identifier
- 93189280
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- MeSH Heading (Major)
- Ehlers-Danlos Syndrome|*GE/ME/PA; Galactosyltransferases|*DF;
Progeria|*GE/ME/PA; Proteoglycans|*BI
- MeSH Heading
- Carbohydrate Sequence; Child, Preschool; Human; Molecular Sequence Data;
Syndrome

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0030-9338
- Country of Publication
- AUSTRIA
- CAS Registry/EC Number
- EC 2.4.1.- (Galactosyltransferases); EC 2.4.1.133 (xylosylprotein
4-beta-galactosyltransferase); 0 (Proteoglycans)


Record 66 from database: MEDLINE
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- Title
- Association of apo B lipoproteins with arterial proteoglycans: pathological
significance and molecular basis.
- Author
- Camejo G; Hurt Camejo E; Wiklund O; Bondjers G
- Address
- Preclinical Research, Astra HÂassle AB, MÂolndal, Sweden.
- Source
- Atherosclerosis, 1998 Aug, 139:2, 205-22
- Abstract
- Retention of apo B-100 lipoproteins, low density lipoprotein (LDL) and
probably lipoprotein(a), Lp(a), by intima proteoglycans (PGs) appears to
increase the residence time needed for their structural, hydrolytic and
oxidative modifications. If the rate of LDL entry exceeds the tissue capacity to
eliminate the modified products, this process may be a contributor to
atherogenesis and lesion advancement. LDL binds to PGs of the intima, by
association of specific positive segments of the apo B-100 with the
negatively-charged glycosaminoglycans (GAGs) made of chondroitin sulfate (CS),
dermatan sulfate (DS) and probably heparan sulfate (HS). Small, dense LDL has a
higher affinity for CS-PGs than large buoyant particles, probably because they
expose more of the segments binding the GAGs than larger LDL. PGs cause
irreversible structural alterations of LDL that potentiate hydrolytic and
oxidative modifications. These alterations also increase LDL uptake by
macrophages and smooth muscle cells. These in vitro data suggest that part of
the atherogenicity of LDL may depend on its tendency to form complexes with
arterial PGs in vivo. Ex vivo results support this hypothesis. Subjects with
coronary heart disease have LDL with significantly higher affinity for arterial
PGs. This is also a characteristic of subjects with the atherogenic lipoprotein
phenotype, with high levels of small, dense LDL. The LDL-PG affinity, however
can be modified by dietary or pharmacological interventions that change the
composition and size of LDL. Lesion-prone intima contain PGs with a high
affinity for LDL. Increased LDL entrapment at these sites may be a key step in a
cyclic atherogenic process.
- Language of Publication
- English
- Unique Identifier
- 98376171
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- MeSH Heading (Major)
- Apolipoproteins B|GE/*ME; Arteries|*ME; Lipoproteins|*ME; Proteoglycans|*ME
- MeSH Heading
- Amino Acid Sequence; Animal; Atherosclerosis|ET; Human; Molecular Sequence
Data; Support, Non-U.S. Gov't

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0021-9150
- Country of Publication
- IRELAND


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- Title
- The role of the invariant chain in mucosal immunity.
- Author
- Barrera CA; Almanza RJ; Ogra PL; Reyes VE
- Address
- Department of Pediatrics, University of Texas Medical Branch, Galveston,
Tex., USA.
- Source
- Int Arch Allergy Immunol, 1998 Oct, 117:2, 85-93
- Abstract
- The invariant chain (Ii) due to its intimate association with major
histocompatibility complex (MHC) alpha and beta chains is a determining element
in the development of immune responses. Ii plays a major role in the assembly,
the intracellular transport and peptide selection by class II MHC. A segment of
Ii designated as CLIP (class II-associated Ii peptide) binds into the antigen
binding site of class II MHC molecules until class II MHC reach intracellular
compartments that contain peptides from internalized antigens. This association
limits the self endogenous peptides that can bind to class II MHC molecules. The
removal of CLIP from class II MHC catalyzes the binding of antigenic peptides
and their subsequent cell surface expression. An isoform of Ii, known as
chondroitin sulfate-modified Ii (IiCS), that is surface-expressed enhances T
cell activation while acting as a coreceptor for CD44. The expression of class
II MHC molecules by mucosal epithelial cells has generated interest in the role
that these cells may have in mucosal immunity. Since in classical
antigen-presenting cells (APC) the biology of class II MHC is regulated by Ii,
it is necessary to bring into perspective the known functions of Ii in
conventional APC to understand the role that Ii may play in mucosal epithelial
cells as potential regulators of local immune responses.
- Language of Publication
- English
- Unique Identifier
- 99002971
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- MeSH Heading (Major)
- Antigens, Differentiation, B-Lymphocyte|CL/*PH; Histocompatibility Antigens
Class II|CL/IM/*PH; Immunity, Mucosal|*
- MeSH Heading
- Antigen-Presenting Cells|IM; Epithelial Cells|IM; Human; Support, Non-U.S.
Gov't; Support, U.S. Gov't, P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 1018-2438
- Country of Publication
- SWITZERLAND


Record 68 from database: MEDLINE
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- Title
- Biological activities and clinical application of M-CSF.
- Author
- Motoyoshi K
- Address
- Third Department of Internal Medicine, National Defense Medical College,
Saitama, Japan.
- Source
- Int J Hematol, 1998 Feb, 67:2, 109-22
- Abstract
- Macrophage colony-stimulating factor (M-CSF) was found to be a glycoprotein
with a molecular weight of 85 kDa which stimulated macrophage colony formation
of mouse bone marrow cells in a semisolid agar culture system in 1978. M-CSF
stimulates differentiation of progenitor cells to mature monocytes, and prolongs
the survival of monocytes. It enhances expression of differentiation antigens
and stimulates chemotactic, phagocytic and the killing activities of monocytes.
Macrophage CSF also stimulates production of several cytokines such as
granulocyte-macrophage CSF, granulocyte CSF and interleukin (IL)-6 by priming
monocytes, and directly stimulates production and secretion of IL-8 and reactive
nitrogen intermediates. In addition to the stimulation of hematopoiesis, M-CSF
also stimulates differentiation and proliferation of osteoclast progenitor cells
and cytotrophoblasts. Proteoglycan type M-CSF, which contains chondroitin
sulfate chains, was found in 1992. In a large-scale double-blind controlled
study on acute myeloid leukemia (AML), it has been shown that the administration
of M-CSF to patients after consolidation chemotherapies shortens the periods of
neutropenia and thrombopenia after chemotherapy and reduces the incidence and
shortens the duration of febrile neutropenia, as well as shortening the period
required to finish three courses of intensive consolidation therapy.
- Language of Publication
- English
- Unique Identifier
- 98295055
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- MeSH Heading (Major)
- Macrophage Colony-Stimulating Factor|*PH/*TU
- MeSH Heading
- Human; Neutropenia|TH; Thrombocytopenia|TH

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0925-5710
- Country of Publication
- IRELAND


Record 69 from database: MEDLINE
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- Title
- Proteoglycans in cell regulation.
- Author
- Templeton DM
- Address
- Department of Clinical Biochemistry, University of Toronto, Canada.
- Source
- Crit Rev Clin Lab Sci, 1992, 29:2, 141-84
- Abstract
- Proteoglycans are a diverse group of proteins carrying one or more
glycosaminoglycan side chains linked to the protein as O-glycosides. Our
appreciation of these structures has matured from a curiosity about unusual
structural glycoproteins, to confer upon them a central role in cell biology.
The major classes of glycosaminoglycans are heparan sulfate and heparin,
chondroitin and dermatan sulfates, keratan sulfate and hyaluronic acid. The
latter is unique in that it does not contain sulfate residues, and appears to be
synthesized, at least sometimes, free of a carrier protein. There is now a
wealth of information on the ability of these structures to influence the growth
and development of cells and tissues. Many direct and specific effects of
proteoglycans will undoubtedly be found, and there are likely to be indirect
effects of the glycosaminoglycans relating to their polyelectrolyte nature.
Convincing arguments that biological activity resides in certain proteoglycan
core proteins are also appearing. The following discussion concerns the role of
proteoglycans in the regulation and action of autocrine and polypeptide growth
factors, direct mitogenic and antimitogenic actions of glycosaminoglycans, the
role of these structures in regulating gene expression, and the biological
activities of proteoglycan core proteins. The probable role of proteoglycans in
normal glomerular cell function, and in progressive renal disease, will be
presented as a harbinger of the significant role we can expect them to play in
diagnosis and therapy in the near future.
- Language of Publication
- English
- Unique Identifier
- 93039639
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- MeSH Heading (Major)
- Cells|*PH; Proteoglycans|CL/*PH
- MeSH Heading
- Amino Acid Sequence; Animal; Fibroblast Growth Factor|CH/PH; Gene Expression
Regulation|PH; Glycosaminoglycans|PH; Growth Substances|CH/PH; Human; Kidney
Diseases|TH; Molecular Sequence Data; Peptides|PH; Support, Non-U.S. Gov't

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- ISSN
- 1040-8363
- Country of Publication
- UNITED STATES
- CAS Registry/EC Number
- 0 (Glycosaminoglycans); 0 (Growth Substances); 0 (Peptides); 0
(Proteoglycans); 62031-54-3 (Fibroblast Growth Factor)


Record 70 from database: MEDLINE
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- Title
- Maternal malaria and parasite adhesion.
- Author
- Fried M; Duffy PE
- Address
- U.S. Army Medical Research Unit-K, Kisumu, Kenya.
- Source
- J Mol Med, 1998 Mar, 76:3-4, 162-71
- Abstract
- Malaria during pregnancy continues to be a major health problem in endemic
countries, with clinical consequences, including death, for both mother and
child. Just as cerebral malaria results from parasite sequestration in the
brain, maternal malaria results from parasite sequestration in the placenta, and
a distinct subpopulation of parasites which bind chondroitin sulfate A but not
CD36 causes the syndrome. Women have little or no immunological experience with
this parasite prior to first pregnancy, making primigravid women particularly
vulnerable to infection. Parasites adhere to the surface of trophoblastic villi,
eliciting the accumulation of inflammatory leukocytes in the intervillous space,
and the necrosis of adjacent placental tissue. Maternal malaria results in poor
pregnancy outcomes, although the responsible mechanisms have not been defined.
In holoendemic areas both placental infection and poor outcome decrease in
frequency with successive pregnancies; protection may result from control of
parasite adhesion, suggesting an attractive target for new therapies.
- Language of Publication
- English
- Unique Identifier
- 98195227
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- MeSH Heading (Major)
- Malaria|*PS; Plasmodium|*CY; Pregnancy Complications, Parasitic|*PS
- MeSH Heading
- Animal; Cell Adhesion|PH; Erythrocytes|PS; Female; Human; Placenta|PS;
Pregnancy; Support, Non-U.S. Gov't

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0946-2716
- Country of Publication
- GERMANY


Record 71 from database: MEDLINE
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- Title
- Lipoprotein (a) regulates plasmin generation and inhibition.
- Author
- Edelberg J; Pizzo SV
- Address
- Duke University Medical Center, Durham, NC 27710.
- Source
- Chem Phys Lipids, 1994 Jan, 67-68:, 363-8
- Abstract
- The relationship between lipoprotein (a) (Lp(a)) and atherosclerosis has
been appreciated for a number of years. Only in recent years, however, has the
structural relationship of Lp(a) to plasminogen resulted in studies of the
effect of this lipoprotein on fibrinolysis. Lp(a) inhibits activation of
plasminogen by tissue-type (t-PA) and urinary-type (u-PA) plasminogen
activators. These inhibitory reactions are surface-dependent. When Lp(a) binds
to fibrin, fibrinogen, heparin or cells it blocks activation of plasminogen by
t-PA. u-PA-mediated activation of plasminogen is blocked on surfaces including
heparin and chondroitin sulfate. Lp(a) also favors inhibition of plasmin by
alpha 2-antiplasmin (alpha 2-AP). The ability of Lp(a) to compete with plasmin
for fibrin binding displaces plasmin into solution where alpha 2-AP rapidly
inhibits this proteinase. These effects are all antifibrinolytic. Lp(a) also
exhibits one profibrinolytic effect, since it blocks inhibition of t-PA by
plasminogen activator type 1 in the presence of fibrinogen or heparin. Thus,
Lp(a) modulates most of the reactions involved in plasmin generation and
inhibition. Its overall effect will depend primarily on the concentrations of
Lp(a), PAI-1 and t-PA in vivo.
- Language of Publication
- English
- Unique Identifier
- 94243986
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- MeSH Heading (Major)
- Lipoprotein(a)|*ME/PH; Plasmin|*AI/*BI
- MeSH Heading
- Antiplasmin|ME; Atherosclerosis|ET; Fibrin|ME; Fibrinolysis|PH; Human;
Tissue Plasminogen Activator|ME; Urokinase|ME

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0009-3084
- Country of Publication
- IRELAND


Record 72 from database: MEDLINE
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- Title
- Proteoglycans of basement membranes.
- Author
- Timpl R
- Address
- Max-Planck-Institut fÂur Biochemie, Martinsried, Germany.
- Source
- EXS, 1994, 70:, 123-44
- Abstract
- Proteoglycans carrying either heparan sulfate and/or chondroitin sulfate
side chains are typical constituents of basement membranes. The most prominent
proteoglycan (perlecan) consists of a 400-500 kDa core protein and three heparan
sulfate chains. Electron microscopy and cDNA sequencing show a complex and
elongated domain structure for the core protein which in part is homologous to
that of the laminin A chain. This structure may be varied by alternative
splicing and proteolysis. Integration into basement membranes probably occurs by
heparan sulfate binding to laminin and collagen IV, core protein binding to
nidogen and by limited self assembly. The proteoglycan is in addition a
cell-adhesive protein which is recognized by beta 1 integrins. Several more
proteoglycans with smaller core proteins (10-160 kDa) apparently exist in
basement membranes but are less well characterized. Biological functions include
control of filtration through basement membranes and binding of growth factors
and protease inhibitors.
- Language of Publication
- English
- Unique Identifier
- 94129144
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- MeSH Heading (Major)
- Proteoglycans|BI/*CH/*ME
- MeSH Heading
- Amino Acid Sequence; Animal; Basement Membrane|ME; Collagen|ME; Consensus
Sequence; Heparitin Sulfate|ME; Human; Laminin|ME; Molecular Sequence Data;
Proteochondroitin Sulfates|ME; Support, Non-U.S. Gov't

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- Country of Publication
- SWITZERLAND


Record 73 from database: MEDLINE
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- Title
- Proteoglycans: many forms and many functions.
- Author
- Hardingham TE; Fosang AJ
- Address
- Biochemistry Division, Kennedy Institute, Hammersmith, London, United
Kingdom.
- Source
- FASEB J, 1992 Feb 1, 6:3, 861-70
- Abstract
- Proteoglycans are produced by most eukaryotic cells and are versatile
components of pericellular and extracellular matrices. They belong to many
different protein families. Their functions vary from the physical effects of
the proteoglycan aggrecan, which binds with link protein to hyaluronan to form
multimolecular aggregates in cartilage; to the intercalated membrane protein
CD44 that has a proteoglycan form and is a receptor and a cell-binding site for
hyaluronan; to heparan sulfate proteoglycans of the syndecan and other families
that provide matrix binding sites and cell-surface receptors for growth factors
such as fibroblast growth factor (FGF). One feature that recurs in proteoglycan
biology is that their structure is open to extensive modulation during cellular
expression. Examples of protein changes are known, but a major source of
structural variation is in the glycosaminoglycan chains. The number of chains
and their length can vary, as well as their pattern of sulfation. This may
result in the switching of different chain types with different properties,
e.g., chondroitin sulfate and heparan sulfate, and it may also result in the
selective expression of sulfated chain sequences that have specific functions.
The control of glycosaminoglycan structure is not well understood, but it does
appear to be used to change the properties of proteoglycans to suit different
biological needs. Proteoglycan forms of proteins are thus important modifiers of
the organization of the pericellular and extracellular matrices and modulators
of the processes that occur there.
- Language of Publication
- English
- Unique Identifier
- 92155478
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- MeSH Heading (Major)
- Proteoglycans|*CH/*PH
- MeSH Heading
- Animal; Carrier Proteins|PH; Collagen; Glycosaminoglycans|BI; Glycosylation;
Growth Substances|ME; Human; Membrane Glycoproteins|PH; Molecular Structure;
Receptors, Lymphocyte Homing|PH; Support, Non-U.S. Gov't

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0892-6638
- Country of Publication
- UNITED STATES
- CAS Registry/EC Number
- 0 (aggrecan); 0 (decorin); 0 (syndecan); 0 (Carrier Proteins); 0
(Glycosaminoglycans); 0 (Growth Substances); 0 (Membrane Glycoproteins); 0
(Proteoglycans); 0 (Receptors, Lymphocyte Homing); 123939-84-4 (biglycan);
126468-95-9 (fibromodulin); 9007-34-5 (Collagen)


Record 74 from database: MEDLINE
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- Title
- Neuropathies associated with monoclonal gammapathies [see comments]
- Author
- Nemni R; Gerosa E; Piccolo G; Merlini G
- Address
- Clinica Neurologica, Istituto Scientifico S. Raffaele, Milano, Italy.
- Source
- Haematologica, 1994 Nov, 79:6, 557-66
- Abstract
- There is increasing evidence that monoclonal proteins are implicated in the
development of peripheral neuropathy. Approximately ten percent of patients with
peripheral neuropathy of unknown cause have a monoclonal protein and this rate
is significantly higher than prevalence rates of monoclonal protein in
comparable segments of the general population. Extensive clinical,
electrophysiological and immunopathological evidences indicate that peripheral
neuropathy associated with monoclonal protein are heterogeneous, including: 1.
the demyelinating, predominantly sensory neuropathies associated with anti-MAG
antibodies; 2. the axonal, sensory neuropathies associated with anti-sulfatide
and anti-chondroitin sulfate antibodies; 3. the motor neuropathies associated
with anti-GM1 antibodies. Patients with chronic polyneuropathies should be
evaluated for underlying plasma cell dyscrasia.
- Language of Publication
- English
- Unique Identifier
- 95203811
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- MeSH Heading (Major)
- Paraproteinemias|*CO/DI/TH; Peripheral Nervous System
Diseases|DI/EP/*ET/IM/TH
- MeSH Heading
- Adult; Aged; Autoantibodies|IM; Autoantigens|IM; Carbohydrate Sequence;
Combined Modality Therapy; Demyelinating Diseases|ET/IM; Female; Human;
Immunosuppressive Agents|TU; Male; Middle Age; Molecular Sequence Data; Motor
Neuron Disease|ET/IM; Nerve Tissue Proteins|IM; Paraproteins|IM; Plasmapheresis;
Prednisone|TU; Support, Non-U.S. Gov't

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0390-6078
- Country of Publication
- ITALY


Record 75 from database: MEDLINE
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- Title
- The biology and action of colony stimulating factor-1.
- Author
- Stanley ER; Berg KL; Einstein DB; Lee PS; Yeung YG
- Address
- Department of Developmental and Molecular Biology, Albert Einstein College
of Medicine, Bronx, New York.
- Source
- Stem Cells (Dayt), 1994, 12 Suppl 1:, 15-24; discussion 25
- Abstract
- Colony stimulating factor 1 (CSF-1) is a growth factor for mononuclear
phagocytic cells. Through alternative mRNA splicing and differential
post-translational proteolytic processing, CSF-1 can either be secreted into the
circulation as a glycoprotein or chondroitin sulfate-containing proteoglycan or
expressed as a membrane-spanning glycoprotein on the surface of synthesizing
cells. The discovery that the osteopetrotic (op/op) mutant mouse possesses an
inactivating mutation in the CSF-1 gene has greatly contributed to our
understanding of CSF-1 biology. CSF-1 directly regulates some non-mononuclear
phagocytic cells that express the CSF-1 receptor tyrosine kinase, but is not
required for their development. However, it directly regulates the development
and maintenance of tissue macrophage subpopulations that appear to have
important trophic and/or scavenger roles in tissue morphogenesis and function.
Depending on the tissue, this regulation may be local (via the cell-surface
form) localized (via the sequestered proteoglycan form) or humoral. It appears
that the CSF-1 dependent tissue macrophage subpopulations, via their effects on
other cell types, can significantly affect functions in tissues as diverse as
testis, brain and skin, and their absence in op/op mice may explain the
pleiotropy of the op/op phenotype. To investigate post-CSF-1 receptor signaling
in the macrophage, procedures have been developed for the purification and
sequence determination of the proteins that are rapidly phosphorylated on
tyrosine in response to CSF-1. Several have been identified and the behavior of
one of them, protein tyrosine phosphatase 1C (PTP1C), is discussed.
- Language of Publication
- English
- Unique Identifier
- 95211015
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- MeSH Heading (Major)
- Macrophage Colony-Stimulating Factor|GE/PD/*PH
- MeSH Heading
- Animal; Human; Macrophages|PH; Mice; Mice, Knockout; Mutation;
Osteopetrosis|GE; Protein-Tyrosine-Phosphatase|ME; Receptors, Macrophage
Colony-Stimulating Factor|PH; Signal Transduction|PH; Support, Non-U.S. Gov't;
Support, U.S. Gov't, P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 1066-5099
- Country of Publication
- UNITED STATES


Record 76 from database: MEDLINE
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- Title
- The clinical role of immunoscintigraphy for the detection of ocular
melanoma.
- Author
- Schaling DF; Pauwels EK
- Address
- Department of Ophthalmology, University Hospital, Leiden, The Netherlands.
- Source
- Q J Nucl Med, 1996 Dec, 40:4, 335-40
- Abstract
- The value of immunoscintigraphy in the diagnosis of choroidal melanoma is
discussed and compared with other diagnostic procedures with isotopes and
diagnostic modalities like fluorescein angiography, standardized ultrasonography
and magnetic resonance imaging. Consecutive studies with immunoscintigraphy in
choroidal melanoma show a sensitivity of 41 to 49%, which can be improved by use
of single photon emission computerized tomography (SPECT). Another technique
which has improved the results of radio-immunoscintigraphy is the use of a
three-step labelling procedure with biotinylated anti-tumor antibodies and
avidin. The specificity of the 225.28S antibody is discussed with regard to the
expression of the chondroitin sulfate proteoglycan (CSPG)--to which the 225.28S
antibody is directed--in normal tissue and in other malignant tumours.
- Language of Publication
- English
- Unique Identifier
- 97202921
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- MeSH Heading (Major)
- Choroid Neoplasms|*RI; Melanoma|*RI; Radioimmunodetection|*
- MeSH Heading
- Comparative Study; Fluorescein Angiography; Human; Magnetic Resonance
Imaging; Tomography, Emission-Computed, Single-Photon

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- Country of Publication
- ITALY


Record 77 from database: MEDLINE
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- Title
- Facilitatory and inhibitory effects of glial cells and extracellular matrix
in axonal regeneration.
- Author
- Carbonetto S
- Address
- Centre for Research in Neuroscience, McGill University, Montreal General
Hospital Research Institute, Quebec, Canada.
- Source
- Curr Opin Neurobiol, 1991 Oct, 1:3, 407-13
- Abstract
- Recent studies have shown that Schwann cells stimulate nerve regeneration by
producing nerve growth factor in response to macrophage activation as well as by
mediating growth through cell-surface and extracellular matrix adhesion
molecules. Neurons sprouting in the central nervous system, however, encounter a
hostile environment including mature oligodendrocytes with contact inhibitors of
growth cone motility, masses of proliferating astrocytes with surface properties
that may block regeneration, and an extracellular environment relatively rich in
chondroitin sulfate and tenascin forming a matrix less permissive for
regeneration than that found in the peripheral nervous system. In addition, as
neurons mature, integrins and cell adhesion molecules are reduced in number
(transcriptionally) or in efficacy (post-translationally).
- Language of Publication
- English
- Unique Identifier
- 92338612
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- MeSH Heading (Major)
- Axons|*PH; Extracellular Matrix|*PH; Nerve Regeneration|*PH; Neuroglia|*PH
- MeSH Heading
- Animal; Human

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0959-4388
- Country of Publication
- ENGLAND


Record 78 from database: MEDLINE
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- Title
- Investigational approaches to pulmonary hypertension.
- Author
- Rabinovitch M
- Address
- University of Toronto, Hospital for Sick Children, Ontario, Canada.
- Source
- Toxicol Pathol, 1991, 19:4 Pt 1, 458-69
- Abstract
- Pulmonary vascular disease (PVD) revolves around a series of switches in the
smooth muscle cell (SMC) phenotype. Differentiation of SMC from precursor cells
causes muscularization of normally non-muscular peripheral arteries; hypertrophy
and hyperplasia of existing SMC and increased connective tissue protein
synthesis cause thickening of the wall, and migration of SMC into the
subendothelial space is the basis of intimal proliferation. To uncover the
pathophysiologic mechanisms of these changes, we have used a variety of animal
models and cell culture systems. From rats in which hypertensive PVD was induced
by exposure to chronic hypoxia or following injection of the pyrrolizidine
alkaloid, monocrotaline, we have identified increased pulmonary artery (PA)
elastolytic activity which occurs early and which accompanies progressive rather
than reversible PVD. Inhibition of elastolytic activity prevents or reduces PVD.
We are cloning the gene for this new enzyme to study its regulation in PVD. To
address the mechanism of SMC proliferation under conditions of high PA pressure
and flow, we cultured endothelial cells on polyvinylchloride membranes and
pulsated them at high pressure. This caused reduced synthesis of heparan
sulfate. The resulting decrease binding of fibroblast growth factor would lessen
its mitogenic effect and modulate SMC proliferation in response to other growth
factors from platelets or serum. To study SMC migration, we cultured endothelial
and SMC from the ductus arteriosus (a fetal vessel which spontaneously develops
intimal proliferation in late gestation). The migratory SMC phenotype is a
function of increased production of fibronectin governed by a translational
control mechanism, and increased endothelial hyaluronan regulated by
transforming growth factor beta. SMC migration is also related to impaired
assembly of elastin, the result of a chondroitin sulfate-induced decrease in
elastin binding proteins and the production of a novel 'defunct' 52 kD
tropoelastin.
- Language of Publication
- English
- Unique Identifier
- 92263033
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- MeSH Heading (Major)
- Hypertension, Pulmonary|*ET/PA
- MeSH Heading
- Animal; Cell Division; Cell Movement; Cells, Cultured; Ductus
Arteriosus|CY/PH; Human; Muscle, Smooth|CY; Support, Non-U.S. Gov't

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- ISSN
- 0192-6233
- Country of Publication
- UNITED STATES


Record 79 from database: MEDLINE
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- Title
- A role for glycosaminoglycans in the development of collagen fibrils.
- Author
- Parry DA; Flint MH; Gillard GC; Craig AS
- Address
-
- Source
- FEBS Lett, 1982 Nov 22, 149:1, 1-7
- Abstract
- Extensive data on the glycosaminoglycan (GAG) composition and the collagen
fibril diameter distribution have been collected for a diverse range of
connective tissues. It is shown that tissues with the smallest diameter collagen
fibrils (mass-average diameter less than 60 nm) have high concentrations of
hyaluronic acid and that tissues with the largest diameter collagen fibrils
(mass-average diameter approximately 200 nm) have high concentrations of
dermatan sulphate. It is suggested that the lateral growth of fibrils beyond a
diameter of about 60 nm is inhibited by the presence of an excess of hyaluronic
acid but that this inhibitory effect may be removed by an increasing
concentration of chondroitin sulphate and/or dermatan sulphate. It is also
postulated that high concentrations of chondroitin sulphate will inhibit fibril
growth beyond a mass-average diameter of approximately 150 nm. Such an
inhibition may in turn be removed by an increasing concentration of dermatan
sulphate such that it becomes the dominant GAG present in the tissue.
- Language of Publication
- English
- Unique Identifier
- 83105707
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- MeSH Heading (Major)
- Collagen|*ME; Connective Tissue|*ME/PH; Glycosaminoglycans|*ME
- MeSH Heading
- Aging; Animal; Guinea Pigs; Human; Rats; Skin|ME; Support, Non-U.S. Gov't

- Publication Type
- JOURNAL ARTICLE; REVIEW
- ISSN
- 0014-5793
- Country of Publication
- NETHERLANDS
- CAS Registry/EC Number
- 0 (Glycosaminoglycans); 9007-34-5 (Collagen)


Record 80 from database: MEDLINE
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- Title
- Cartilage proteoglycans: structure and potential functions.
- Author
- Roughley PJ; Lee ER
- Address
- Shriners Hospital for Crippled Children, Montreal, Quebec, Canada.
- Source
- Microsc Res Tech, 1994 Aug, 28:5, 385-97
- Abstract
- Hyaline cartilage contains five well-characterized proteoglycans in its
extracellular matrix, and it is likely that others exist. The largest in size
and most abundant by weight is aggrecan, a proteoglycan that possesses over 100
chondroitin sulfate and keratan sulfate chains. Aggrecan is also characterized
by its ability to interact with hyaluronic acid to form large proteoglycan
aggregates. Both the high anionic charge on the individual aggrecan molecules
endowed by the sulfated glycosaminoglycan chains and the localization within the
matrix endowed by aggregate formation are essential for aggrecan function. The
molecule provides cartilage with its osmotic properties, which give articular
cartilage its ability to resist compressive loads. The other proteoglycans are
characterized by their ability to interact with collagen. They are much smaller
than aggrecan in size but may be present in similar molar amounts. Decorin,
biglycan, and fibromodulin are closely related in protein structure but differ
in glycosaminoglycan composition and function. Decorin and biglycan possess one
and two dermatan sulfate chains, respectively, whereas fibromodulin bears
several keratan sulfate chains. Decorin and fibromodulin both interact with the
type II collagen fibrils in the matrix and may play a role in fibrillogenesis
and interfibril interactions. Biglycan is preferentially localized in the
pericellular matrix, where it may interact with type VI collagen. Finally, type
IX collagen can also be considered as a proteoglycan, as its alpha 2(IX) chain
may bear a glycosaminoglycan chain. It may serve as a bridge between the
collagen fibrils or with the interspersed aggrecan network.
- Language of Publication
- English
- Unique Identifier
- 95003201
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- MeSH Heading (Major)
- Cartilage|CH/PH/*UL; Proteoglycans|CH/*PH/*UL
- MeSH Heading
- Aging|PH; Animal; Carbohydrate Sequence; Human; Joint Diseases|PP; Molecular
Sequence Data; Support, Non-U.S. Gov't

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- ISSN
- 1059-910X
- Country of Publication
- UNITED STATES


Record 81 from database: MEDLINE
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- Title
- Mechanisms of astrocyte-directed neurite guidance.
- Author
- Powell EM; Meiners S; DiProspero NA; Geller HM
- Address
- Department of Pharmacology, UMDNJ-Robert Wood Johnson Medical School, 675
Hoes Lane, Piscataway, NJ 08854, USA. epowell@umdnj.edu
- Source
- Cell Tissue Res, 1997 Nov, 290:2, 385-93
- Abstract
- Astrocytes have recently become better recognized as playing vital roles in
regulating the patterning of central nervous system neurites during development
and following injury. In general, astrocytes have been shown to be supportive of
neurite extension, but alterations in the biochemical properties of astrocytes
in particular areas during development and in gliotic tissue may act to confine
neurite outgrowth and thus provide guidance cues. In vivo studies indicate that
restrictive astrocytes function through their altered expression of specific
extracellular matrix molecules, including tenascin, chondroitin, and keratan
sulfate proteoglycans. In addition, several in vitro models suggest that other
cell surface molecules are utilized by restrictive astrocytes to direct neurite
trajectories.
- Language of Publication
- English
- Unique Identifier
- 97465869
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- MeSH Heading (Major)
- Astrocytes|*CY/PH; Cell Communication|*; Nervous System|*CY; Neurites|*PH;
Neurons|*CY/PH
- MeSH Heading
- Animal; Extracellular Matrix|PH; Human; Nerve Tissue Proteins|PH; Signal
Transduction|PH; Support, U.S. Gov't, P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0302-766X
- Country of Publication
- GERMANY


Record 82 from database: MEDLINE
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- Title
- Experimental and clinical pharmacology of glycosaminoglycans (GAGs).
- Author
- Soldani G; Romagnoli J
- Address
- Laboratory of Pharmacology, Faculty of Veterinary Medicine, University of
Pisa, Italy.
- Source
- Drugs Exp Clin Res, 1991, 17:1, 81-5
- Abstract
- The experimental and clinical pharmacology of glycosaminoglycans (GAGs) is
discussed, including that of heparin and related compounds, hyaluronic acid and
chondroitin sulfates.
- Language of Publication
- English
- Unique Identifier
- 92007106
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- MeSH Heading (Major)
- Glycosaminoglycans|*PD
- MeSH Heading
- Human

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0378-6501
- Country of Publication
- SWITZERLAND
- CAS Registry/EC Number
- 0 (Glycosaminoglycans)


Record 83 from database: MEDLINE
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- Title
- The role of heparan sulfate proteoglycans in the pathogenesis of Alzheimer's
disease.
- Author
- Small DH; Williamson T; Reed G; Clarris H; Beyreuther K; Masters CL;
Nurcombe V
- Address
- Department of Pathology, University of Melbourne, Parkville, Victoria,
Australia.
- Source
- Ann N Y Acad Sci, 1996 Jan, 777:, 316-21
- Abstract
- The hallmark of Alzheimer's disease (AD) is the deposition of amyloid
plaques and neurofibrillary tangles in the brain. The relationship between
amyloid deposition and the cognitive deficit is still unclear. The amyloid beta
A4 protein is produced by proteolytic cleavage of the amyloid protein precursor
(APP). Very little is known about the normal function of APP and the role the
protein may play in pathogenesis. Several studies have shown that APP is
important for the regulation of neurite outgrowth. Our studies support these
findings and indicate that the neurite outgrowth-promoting effects of APP are
stimulated by an interaction between APP and specific proteoglycans. Using
site-directed mutagenesis, a heparan sulfate binding site which mediates this
effect has been mapped to the N-terminus of APP (residues 96-110, HBD-1). A
peptide homologous to HBD-1 blocks the trophic effects of APP in cell culture.
To purify specific proteoglycans which stimulate the action of APP, an affinity
column was constructed using a biotinylated peptide homologous to HBD-1 coupled
to streptavidin-agarose. Two proteoglycans were isolated from a crude brain cell
conditioned medium by affinity chromatography. The purified proteoglycans bound
APP saturably with high affinity and stimulated the action of APP on neurite
outgrowth from chick sympathetic neurons. Digestion of the proteoglycan fraction
with heparitinase I or chondroitinase ABC demonstrated the presence of two major
proteins, a heparan sulfate proteoglycan with a core protein of 63-67 kD
molecular mass and a chondroitin sulfate proteoglycan with a core protein of
100-110 kD molecular mass. The results demonstrate that APP binds to at least
two proteoglycans and that this interaction may regulate the trophic effects of
the protein. The interaction of specific APP-binding proteoglycans with amyloid
plaques may disturb the normal function of APP and contribute to the neuritic
degeneration that is commonly seen around the amyloid plaque cores.
- Language of Publication
- English
- Unique Identifier
- 96187038
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- MeSH Heading (Major)
- Alzheimer Disease|*ET; Heparitin Sulfate|*PH; Proteoglycans|*PH
- MeSH Heading
- Amyloid beta-Protein Precursor|PH; Extracellular Matrix|ME; Human; Support,
Non-U.S. Gov't

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0077-8923
- Country of Publication
- UNITED STATES


Record 84 from database: MEDLINE
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- Title
- Small proteoglycans.
- Author
- Kresse H; Hausser H; Schönherr E
- Address
- Institute of Physiological Chemistry and Pathobiochemistry, University of
MÂunster, Germany.
- Source
- EXS, 1994, 70:, 73-100
- Abstract
- In this review the structure and functions of two non-related proteoglycan
families are discussed. One family represents a group of extracellular matrix
macromolecules characterized by core proteins with leucine-rich repeat motifs.
Within this family special attention is given to those members which carry
chondroitin or dermatan sulfate glycosaminoglycan chains. The second family is
characterized by repeat sequences of serine and glycine. Their members are
products of a single core protein gene and are characteristic constituents of
secondary vesicles in cells of the haematopoietic lineage.
- Language of Publication
- English
- Unique Identifier
- 94129154
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- MeSH Heading (Major)
- Proteoglycans|*CH/GE/*ME
- MeSH Heading
- Amino Acid Sequence; Animal; Comparative Study; Glycosaminoglycans|CH;
Human; Molecular Sequence Data; Protein Conformation; Protein Processing,
Post-Translational; Support, Non-U.S. Gov't; Translation, Genetic

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- Country of Publication
- SWITZERLAND


Record 85 from database: MEDLINE
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- Title
- The link proteins.
- Author
- Neame PJ; Barry FP
- Address
- Shriners Hospital for Crippled Children, Tampa, Florida.
- Source
- EXS, 1994, 70:, 53-72
- Abstract
- Aggregates of chondroitin-keratan sulfate proteoglycan (aggrecan) and
hyaluronic acid (hyaluronan) are the major space-filling components of
cartilage. A glycoprotein, link protein (LP; 40-48 kDa) stabilizes the aggregate
by binding to both hyaluronic acid and aggrecan. In the absence of LP,
aggregates are smaller (as estimated by rotary shadowing of electron
micrographs) and less stable (they dissociate at pH 5) than they are in the
presence of LP. The proteoglycan aggregate, including LP, is dissociated in the
presence of chaotropes such as 4 M guanidine hydrochloride. On removal of the
chaotrope, the complex will reassociate. This forms the basis of the isolation
of LP from cartilage and has been described in detail elsewhere. Tryptic
digestion of the proteoglycan aggregates results in a high molecular weight
product that consists of hyaluronic acid to which is bound LP and the N-terminal
globular domain of aggrecan (hyaluronic acid binding region; HABR) in a 1:1
stoichiometry. The amino acid sequences of LP and HABR are surprisingly similar.
The amino acid sequence can be divided into three domains; an N-terminal domain
that falls into the immunoglobulin super-family and two C-terminal domains that
are similar to each other. The DNA structure echoes this similarity, in that the
major domains are reflected in three separate exons in both LP and HABR. The two
C-terminal domains are largely responsible for the association with HA and are
related to two recently described hyaluronate-binding proteins, CD44 and TSG-6.
A variety of approaches, including analysis of the forms of LP in vivo, rotary
shadowing and analysis of the sequence in the immunoglobulin-like domain, have
shed considerable light on the structure-function relationships of LP. This
review describes the structure and function of LP in detail, focusing on what
can be inferred from the similarity of LP, HABR and related molecules such as
immunoglobulins and lymphocyte HA-receptors.
- Language of Publication
- English
- Unique Identifier
- 94129153
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- MeSH Heading (Major)
- Protein Structure, Secondary|*; Proteins|*CH/GE/*ME
- MeSH Heading
- Amino Acid Sequence; Animal; Cartilage|ME; Comparative Study; Human; Models,
Structural; Molecular Sequence Data; Proteoglycans|CH/GE/ME; Sequence Homology,
Amino Acid; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- Country of Publication
- SWITZERLAND


Record 86 from database: MEDLINE
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- Title
- Proteoglycans and hyaluronan in female reproductive organs.
- Author
- Yanagishita M
- Address
- Bone Research Branch, National Institute of Dental Research, National
Institutes of Health, Bethesda, Maryland 20892.
- Source
- EXS, 1994, 70:, 179-90
- Abstract
- Proteoglycans and hyaluronan have been isolated from various female
reproductive organs and fetal membranes. Special attention has been directed to
changes in the composition of these molecules in the tissue during pregnancy and
ovulation. Various chondroitin sulfate/dermatan sulfate proteoglycans, which
represent extracellular matrix proteoglycans, are closely related to the
organization of connective tissues. Heparan sulfate proteoglycans are widely
distributed on the plasma membrane of most mammalian cells including those in
the female reproductive organs. They are involved in various aspects of
cell-to-cell or cell-to-extracellular matrix interactions. Although the precise
biological functions of these proteoglycans are not currently clear, recent
advances in biochemistry and molecular biology techniques promise an exciting
new development in this area.
- Language of Publication
- English
- Unique Identifier
- 94129146
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- MeSH Heading (Major)
- Genitalia, Female|CH/*PH; Proteoglycans|CH/*IP/*ME
- MeSH Heading
- Animal; Connective Tissue|PH; Epithelium|CH/PH; Extracellular Matrix|ME;
Extracellular Matrix Proteins|CH/ME; Female; Fetal Membranes|CH;
Glycosaminoglycans|CH/IP/ME; Human; Mammals; Ovary|CH/PH; Pregnancy; Umbilical
Cord|CH; Uterus|CH/PH; Vagina|CH/PH

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- Country of Publication
- SWITZERLAND


Record 87 from database: MEDLINE
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- Title
- Structure and biological functions of keratan sulfate proteoglycans.
- Author
- Greiling H
- Address
- Institute of Clinical Chemistry and Pathobiochemistry, Medical Faculty,
University of Technology (RWTH), Aachen, Germany.
- Source
- EXS, 1994, 70:, 101-22
- Abstract
- The skeletal and corneal keratan sulfate proteoglycans show a different
metabolic and structural heterogeneity. The domain structure of the carbohydrate
chain has been shown to be different in various animal species. There are two
major types of skeletal keratan sulfate proteoglycans with and without fucose.
The protein cores of the corneal chicken keratan sulfate proteoglycan (lumican)
and those of another small keratan sulfate proteoglycan (fibromodulin) have been
sequenced. Keratan sulfate oligosaccharides belong to the members of an antigen
family of the poly-N-acetyllactosamine series. Monoclonal antibodies and
immunoassay procedures for keratan sulfate proteoglycans have been prepared. In
osteoarthritis, no significant specific increase of keratan sulfate has been
found. Keratan sulfate is a functional substitute for chondroitin sulfate in
O2-deficient tissues.
- Language of Publication
- English
- Unique Identifier
- 94129143
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- MeSH Heading (Major)
- Keratan Sulfate|*CH/GE/*ME; Proteochondroitin Sulfates|*CH/GE/*ME
- MeSH Heading
- Animal; Atherosclerosis|ME; Base Sequence; Carbohydrate Conformation;
Carbohydrate Sequence; Collagen|ME; Cornea|ME; Corneal Dystrophies,
Hereditary|ME; Human; Lysosomes|ME; Molecular Sequence Data

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- Country of Publication
- SWITZERLAND


Record 88 from database: MEDLINE
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- Title
- Thrombomodulin structure and function.
- Author
- Sadler JE
- Address
- Howard Hughes Medical Institute, Department of Medicine, Washington
University School of Medicine, St. Louis, MO 63110, USA.
esadler@imgate.wustl.edu
- Source
- Thromb Haemost, 1997 Jul, 78:1, 392-5
- Abstract
- Thrombomodulin is protein cofactor expressed on endothelial cell surfaces
that modifies the substrate specificity of thrombin, apparently by an allosteric
mechanism. The thrombin-thrombomodulin complex activates protein C, initiating
an essential anticoagulant pathway. The cofactor function of membrane-associated
thrombomodulin requires the last three of six tandemly repeated EGF-like domains
(numbers 4, 5, and 6), as well as a Ser/Thr-rich spacer between EGF-like domain
6 and the transmembrane domain. The Ser/Thr-rich domain is variably modified
with a chondroitin sulfate chain that influences the affinity of thrombin
binding and the calcium ion dependence of cofactor function. The structure of
EGF-like domain 4 has been determined by NMR spectroscopy, and the structure of
a complex between thrombin and a peptide from thrombomodulin EGF-like domain 5
was determined by X-ray crystallography. These structures are small steps toward
an understanding of how thrombomodulin regulates thrombin.
- Language of Publication
- English
- Unique Identifier
- 97341985
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- MeSH Heading (Major)
- Thrombomodulin|*CH/PH
- MeSH Heading
- Amino Acid Sequence; Human; Models, Molecular; Molecular Sequence Data;
Protein Binding; Protein C|ME; Structure-Activity Relationship; Thrombin|ME

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0340-6245
- Country of Publication
- GERMANY


Record 89 from database: MEDLINE
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- Title
- x82p4and the adhesion of neoplastic cells.
- Author
- Rudzki Z; Jothy S
- Address
- Department of Pathology, McGill University, Montreal, Quebec, Canada.
- Source
- Mol Pathol, 1997 Apr, 50:2, 57-71
- Abstract
- CD44 is a family of transmembrane glycoproteins that act mainly as a
receptor for hyaluronan. It can also bind some other extracellular matrix
ligands (chondroitin sulphate, heparan sulphate, fibronectin, serglycin,
osteopontin) with lower affinity. CD44 is encoded by a single gene containing 20
exons, 10 of which (v1-v10) are variant exons inserted by alternative splicing.
The standard, ubiquitously expressed isoform of CD44, does not contain sequences
encoded by these variant exons. Numerous variant isoforms of CD44 containing
different combinations of exons v1-v10 inserted into the extracellular domain
can be expressed in proliferating epithelial cells and activated lymphocytes.
CD44 plays a significant role in lymphocyte homing. Both alternative splicing
and glycosylation influence receptor function of the molecule, usually reducing
its affinity to hyaluronan. The cytoplasmic domain of CD44 communicates with the
cytoskeleton via ankyrin and proteins belonging to the ezrin-moesin-radixin
family. Relatively little is known about the intracellular events following
interactions of CD44 with its ligands. Some variant isoforms, especially those
containing sequences encoded by v6-v10, are overexpressed in both human and
animal neoplasms. In a rat pancreatic adenocarcinoma model one of the variant
CD44 isoforms was proved to be determinant in the metastatic process. For some
human neoplasms (carcinomas of the digestive tract, non-Hodgkin's lymphomas,
thyroid carcinomas, and others) correlations have been made between the
particular pattern of CD44 variants produced by neoplastic cells and
clinicopathological parameters of tumours, such as grade, stage, presence of
metastases, and survival. In vitro studies indicate that modifications of CD44
expression result in different ligand recognition and influence cell motility,
invasive properties, and metastatic potential of experimental tumours.
Investigation of CD44 neoexpression can be useful both in early cancer diagnosis
and in predicting tumour behaviour. It can also contribute to better
understanding of molecular mechanisms leading to neoplastic transformation.
- Language of Publication
- English
- Unique Identifier
- 97374703
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- MeSH Heading (Major)
- Antigens, CD44|CH/GE/ME/*PH; Cell Adhesion|*PH; Neoplasms|ME/*PA/PP
- MeSH Heading
- Alternative Splicing; Animal; Carcinoma|ME/PA/PP; Colorectal
Neoplasms|ME/PA/PP; Cytoskeleton|PH; Human; Hyaluronic Acid|CH/PH; Ligands;
Lymphocytes|ME/PH; Lymphoma|ME/PA/PP; Mammals; Melanoma|ME/PA/PP; Mice; Neoplasm
Invasiveness|PP; Neoplasm Metastasis|PP; Rats; Support, Non-U.S. Gov't

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, ACADEMIC
- Country of Publication
- ENGLAND


Record 90 from database: MEDLINE
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- Title
- Thrombin specificity.
- Author
- Guillin MC; Bezeaud A; Bouton MC; Jandrot Perrus M
- Address
- Laboratoire de Recherche sur l'HÆemostase et la Thrombose, FacultÆe de
MÆedecine Xavier Bichat, Paris, France.
- Source
- Thromb Haemost, 1995 Jul, 74:1, 129-33
- Abstract
- A model of thrombin interaction with distinct substrates or ligands has been
derived from the crystallographic studies of thrombin-inhibitors complexes, and
buttressed by functional studies with mutant thrombins, thrombin proteolytic
derivatives or antibodies against thrombin. The unique specificity of thrombin
for its substrates and ligands may be ascribed to multiple interactions with
both the active site cleft and exosite(s) distinct from the active site. Two
prominent insertion loops around Trp 50 and Trp 148 project over the active site
cleft and play an important role in the substrates selection. Several substrates
(fibrinogen, thrombin receptor, heparin cofactor II) or ligands (thrombomodulin,
glycoprotein Ib) interact with a large exosite located on the surface of the
loop segment 65-76, mainly constituted of basic amino acids, designated anion
binding exosite 1. Interaction with these various macromolecules appears to
involve a limited number of residues within the large exosite 1. It is
conceivable that exosite 1 contains distinct subsites, although most of them may
overlap. A second basic exosite (anion binding exosite 2) is located close to
the carboxy-terminal B chain helix. Exosite 2 interacts with heparin, the
chondroitin sulfate moiety of thrombomodulin and prothrombin activation fragment
2. Interaction of ligands with either exosite 1 or exosite 2 leads to
conformational changes of the thrombin molecule, that may be important
determinants of thrombin specificity. Whether exosite 2 cooperates with exosite
1 for thrombin interaction with fibrin(ogen) or the thrombin receptor remains to
be determined.
- Language of Publication
- English
- Unique Identifier
- 96116777
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- MeSH Heading (Major)
- Thrombin|CH/GE/IM/*ME
- MeSH Heading
- Amino Acid Sequence; Animal; Arginine; Autoantibodies|IM; Binding Sites;
Blood Coagulation Factors|CH/ME; Fibrinogen|CH/ME; Human; Isoantibodies|IM;
Lysine; Macromolecular Systems; Molecular Sequence Data; Point Mutation;
Protease Inhibitors|ME; Protein Binding; Receptors, Thrombin|ME; Substrate
Specificity; Support, Non-U.S. Gov't

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0340-6245
- Country of Publication
- GERMANY


Record 91 from database: MEDLINE
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- Title
- Syndecan, a developmentally regulated cell surface proteoglycan that binds
extracellular matrix and growth factors.
- Author
- Bernfield M; Sanderson RD
- Address
- Children's Hospital, Harvard Medical School, Boston, Massachusetts 02115.
- Source
- Philos Trans R Soc Lond B Biol Sci, 1990 Mar 12, 327:1239, 171-86
- Abstract
- Cellular behaviour during development is dictated, in part, by the insoluble
extracellular matrix and the soluble growth factor peptides, the major molecules
responsible for integrating cells into morphologically and functionally defined
groups. These extracellular molecules influence cellular behaviour by binding at
the cell surface to specific receptors that transduce intracellular signals in
various ways not yet fully clear. Syndecan, a cell surface proteoglycan found
predominantly on epithelia in mature tissues binds both extracellular matrix
components (fibronectin, collagens I, III, V, and thrombospondin) and basic
fibroblast growth factor (bFGF). Syndecan consists of chondroitin sulfate and
heparan sulphate chains linked to a 31 kilodalton (kDa) integral membrane
protein. Syndecan represents a family of integral membrane proteoglycans that
differ in extracellular domains, but share cytoplasmic domains. Syndecan behaves
as a matrix receptor: it binds selectively to components of the extracellular
matrix, associates intracellularly with the actin cytoskeleton when cross-linked
at the cell surface, its extracellular domain is shed upon cell rounding and it
localizes solely to basolateral surfaces of simple epithelia. Mammary epithelial
cells made syndecan-deficient become fibroblastic in morphology and cell
behaviour, showing that syndecan maintains epithelial cell morphology. Syndecan
changes in quantity, location and structure during development: it appears
initially on four-cell embryos (prior to its known matrix ligands), becomes
restricted in the pre-implementation embryo to the cells that will form the
embryo proper, changes its expression due to epithelial-mesenchymal interactions
(for example, induced in kidney mesenchyme by the ureteric bud), and with
association of cells with extracellular matrix (for example, during B-cell
differentiation), and ultimately, in mature tissues becomes restricted to
epithelial tissues. The number and size of its glycosaminoglycan chains vary
with changes in cell shape and organization yielding tissue type-specific
polymorphic forms of syndecan. Its interactions with the major extracellular
effector molecules that influence cell behaviour, its role in maintaining cell
shape and its spatial and temporal changes in expression during development
indicate that syndecan is involved in morphogenesis.
- Language of Publication
- English
- Unique Identifier
- 90207462
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- MeSH Heading (Major)
- Extracellular Matrix|*ME; Growth Substances|*ME; Membrane
Glycoproteins|GE/ME/*PH; Proteoglycans|GE/ME/*PH
- MeSH Heading
- Amino Acid Sequence; Animal; Embryo|PH; Heparitin Sulfate|GE; Human;
Molecular Sequence Data; Protein Binding; Proteochondroitin Sulfates|GE;
Sequence Homology, Nucleic Acid; Support, Non-U.S. Gov't; Support, U.S. Gov't,
P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0080-4622
- Country of Publication
- ENGLAND
- CAS Registry/EC Number
- 0 (heparan sulfate proteoglycan); 0 (syndecan); 0 (Growth Substances); 0
(Membrane Glycoproteins); 0 (Proteochondroitin Sulfates); 0 (Proteoglycans);
9050-30-0 (Heparitin Sulfate)


Record 92 from database: MEDLINE
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- Title
- Plasmalogens, phospholipases A2 and signal transduction.
- Author
- Farooqui AA; Yang HC; Horrocks LA
- Address
- Neurovation Inc. and Department of Medical Biochemistry, Ohio State
University, Columbus 43210, USA.
- Source
- Brain Res Brain Res Rev, 1995 Sep, 21:2, 152-61
- Abstract
- Several lines of evidence indicate that the breakdown of plasmalogens in
neural membranes during neurodegenerative diseases is a receptor-mediated
process catalyzed by a plasmalogen-selective phospholipase A2. This enzyme has
recently been purified from bovine brain. It does not require Ca2+ and is
localized in cytosol. It has a molecular mass of 39 kDa and is strongly
inhibited by glycosaminoglycans, with the pattern of inhibition being heparan
sulfate > hyaluronic acid > chondroitin sulfate > heparin. This
plasmalogen-selective phospholipase A2 is also inhibited by gangliosides and
sialoglycoproteins. Substrate specificity and the effects of metal ions,
detergents and inhibitors suggest that this phospholipase A2 is different from
the well-known 85 kDa Ca(2+)-dependent cytosolic phospholipase A2 that has
recently been cloned and is not plasmalogen-selective. The plasmalogen-selective
phospholipase A2 may be regulated by glycosaminoglycans and sialoglycoconjugates
and may be involved in the regulation of K+ channels. This enzyme, which plays a
major role in the release of fatty acids during ischemic injury and reperfusion,
shows promise as a major target for drug therapy.
- Language of Publication
- English
- Unique Identifier
- 97020287
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- MeSH Heading (Major)
- Cell Membrane|*CH/EN; Phospholipases A|*ME; Signal Transduction|*PH
- MeSH Heading
- Animal; Human; Support, U.S. Gov't, P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0165-0173
- Country of Publication
- NETHERLANDS


Record 93 from database: MEDLINE
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- Title
- Cell-extracellular matrix interactions in the ductus arteriosus and
perinatal pulmonary circulation.
- Author
- Rabinovitch M
- Address
- Hospital for Sick Children, Ontario, Canada.
- Source
- Semin Perinatol, 1996 Dec, 20:6, 531-41
- Abstract
- Our studies and those of others have shown that changes in the extracellular
matrix have profound effects on vascular remodeling. In the ductus, increased
production of endothelial hyaluronan and smooth muscle cell chondroitin sulfate
and fibronectin and impaired elastin fiber assembly are features critical to
smooth muscle cell migration into the subendothelium and intimal cushion
formation. There is a developmentally orchestrated process that involves
post-transcriptional mechanisms of gene regulation. Closure of the ductus
arteriosus is associated with further changes in matrix expression and
programmed cell death. The changes in the extracellular matrix that induce
neointimal formation are also observed in pathological conditions in pulmonary
and coronary arteries. Plasticity of the pulmonary circulation in the perinatal
period also involves matrix regulation, and processes that prevent the normal
decrease in pulmonary vascular resistance will result in impaired matrix
regulation, and in the development of structural changes in the pulmonary
arteries, including abnormal smooth muscle cell differentiation, hypertrophy and
proliferation, which sustain the elevation in pulmonary artery pressure.
- Language of Publication
- English
- Unique Identifier
- 97246180
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- MeSH Heading (Major)
- Ductus Arteriosus|CH/EM/*PH/UL; Extracellular Matrix|*PH/UL; Pulmonary
Circulation|*
- MeSH Heading
- Animal; Endothelium, Vascular|CH/PH/UL; Extracellular Matrix Proteins|PH;
Human; Infant, Newborn; Pulmonary Artery|PH

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0146-0005
- Country of Publication
- UNITED STATES


Record 94 from database: MEDLINE
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- Title
- Brevican: a major proteoglycan in adult brain.
- Author
- Yamaguchi Y
- Address
- Burnham Institute, La Jolla, California 92037, USA.
- Source
- Perspect Dev Neurobiol, 1996, 3:4, 307-17
- Abstract
- A diverse set of proteoglycans is expressed in the developing and adult
brain. This is in stark contrast to the fact that most extracellular matrix
components, including fibronectin, laminin, and collagens, are not expressed in
adult brain parenchyma. This suggests that proteoglycans may play a major
functional role in cell-cell and cell-matrix interactions in the brain. Brevican
is a member of the aggrecan/versican family of proteoglycans, containing a
hyaluronic acid-binding domain in its N-terminus and a lectin-like domain in its
C-terminus. Brevican has the smallest core protein among this family and is one
of the most abundant chondroitin sulfate proteoglycans in the adult brain.
Expression of brevican is highly specific in the brain and increases as the
brain develops. These observations suggest that brevican may play a role in
maintaining the extracellular environment of mature brain as a major constituent
of the adult brain extracellular matrix.
- Language of Publication
- English
- Unique Identifier
- 97166460
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- MeSH Heading (Major)
- Aging|*ME; Brain|GD/*ME; Nerve Tissue Proteins|*ME; Proteochondroitin
Sulfates|*ME; Proteoglycans|GE/*ME/PH
- MeSH Heading
- Animal; Chemistry; Cloning, Molecular; Human; Support, U.S. Gov't, P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 1064-0517
- Country of Publication
- UNITED STATES


Record 95 from database: MEDLINE
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- Title
- Brain aggrecan.
- Author
- Schwartz NB; Domowicz M; Krueger RC Jr; Li H; Mangoura D
- Address
- Department of Pediatrics, University of Chicago, Illinois 60615, USA.
- Source
- Perspect Dev Neurobiol, 1996, 3:4, 291-306
- Abstract
- During development, the extracellular matrix (ECM) is a complex dynamic
structure whose components and organization help to establish the requisite
position and state of differentiation. Until recently, the large chondroitin
sulfate proteoglycan, aggrecan, has been localized predominantly to skeletal
tissue and considered a hallmark of cartilage differentiation. We have
identified the presence of aggrecan in two other highly differentiated systems,
brain and notochord, with clearly distinct expression patterns. In chick
cartilage, aggrecan starts to be expressed at embryonic day 5 in limb rudiments,
continues through the entire period of chondrocyte development, and remains a
biochemical marker of the cartilage phenotype thereafter. In brain, aggrecan has
a very low level of expression beginning at day 7, increases up to day 13,
markedly decreases after day 16, and is not expressed posthatching. This pattern
coincides with migration and establishment of neuronal nuclei in the chick
telencephalon and has been proposed to be a component of the migration arrest
mechanism. In very primitive embryos, aggrecan is detected as early as stage 16
in the notochord, long before chondrogenesis occurs, is then expressed up to day
5 and decreases thereafter. The expression of aggrecan occurs during the time of
active neural crest migration and through the onset of sclerotomal
differentiation, and correlates with the notochords' ability to inhibit neural
crest cell migration. Animal models defective in aggrecan biosynthesis have been
invaluable in delineating these functions. In addition we have characterized
these proteoglycans by chemical, biosynthetic, and molecular analyses. Although
significant post-translation differences distinguish the cell-specific aggrecan
species, their core proteins are the products of a single gene. Our findings of
the expression of the same gene (aggrecan) in multiple ontogenously unrelated
differentiating tissue systems and at different times over the developmental
life of an organism provide an elegant model system to study the regulation and
interplay in expression of that gene, as well as the effect of alterations in
that single gene simultaneously in several developing programs.
- Language of Publication
- English
- Unique Identifier
- 97166459
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- MeSH Heading (Major)
- Brain|*ME; Proteoglycans|*ME
- MeSH Heading
- Animal; Cartilage|ME; Human; Notochord|ME; Proteochondroitin Sulfates|ME;
Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 1064-0517
- Country of Publication
- UNITED STATES


Record 96 from database: MEDLINE
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- Title
- Versican.
- Author
- Lebaron RG
- Address
- Division of Life Sciences, Cell and Molecular Biology, University of Texas
at San Antonio 78249, USA.
- Source
- Perspect Dev Neurobiol, 1996, 3:4, 261-71
- Abstract
- Proteoglycans have long been recognized as participating in a number of
biological activities ranging from structural roles to regulation of
transcription. Versican is a large chondroitin sulfate proteoglycan expressed in
several tissues, including the nervous system. Significant progress has been
made in the understanding of the molecular structure and biological activity of
versican. The progress is largely due to the application of recombinant DNA
methodology and the generation of domain-specific anti-versican antibodies. In
the central and peripheral nervous system, versican is expressed by glial cells
and is implicated in the regulation of cell adhesion, migration, pattern
formation, and regeneration.
- Language of Publication
- English
- Unique Identifier
- 97166457
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- MeSH Heading (Major)
- Proteochondroitin Sulfates|*/CH/GE/PH
- MeSH Heading
- Animal; Extracellular Matrix Proteins|ME; Gene Expression Regulation;
Glycoproteins|CH; Glycosaminoglycans|CH; Human; Support, U.S. Gov't, P.H.S.;
Tissue Distribution

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 1064-0517
- Country of Publication
- UNITED STATES


Record 97 from database: MEDLINE
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- Title
- Biology and action of colony--stimulating factor-1.
- Author
- Stanley ER; Berg KL; Einstein DB; Lee PS; Pixley FJ; Wang Y; Yeung YG
- Address
- Department of Developmental and Molecular Biology, Albert Einstein College
of Medicine, New York, New York 10461, USA.
- Source
- Mol Reprod Dev, 1997 Jan, 46:1, 4-10
- Abstract
- Colony-stimulating factor-1 (CSF-1), also known as macrophage
colony-stimulating factor, controls the survival, proliferation, and
differentiation of mononuclear phagocytes and regulates cells of the females
reproductive tract. It appears to play an autocrine and/or paracrine role in
cancers of the ovary, endometrium, breast, and myeloid and lymphoid tissues.
Through alternative mRNA splicing and differential post-translational
proteolytic processing, CSF-1 can either be secreted into the circulation as a
glycoprotein or chondroitin sulfate-containing proteoglycan or be expressed as a
membrane-spanning glycoprotein on the surface of CSF-1-producing cells. Studies
with the op/op mouse, which possesses an inactivating mutation in the CSF-1
gene, have established the central role of CSF-1 in directly regulating
osteoclastogenesis and macrophage production. CSF-1 appears to preferentially
regulate the development of macrophages found in tissues undergoing active
morphogenesis and/or tissue remodeling. These CSF-1 dependent macrophages may,
via putative trophic and/or scavenger functions, regulate characteristics such
as dermal thickness, male fertility, and neural processing. Apart from its
expression on mononuclear phagocytes and their precursors, CSF-1 receptor
(CSF-1R) expression on certain nonmononuclear phagocytic cells in the female
reproductive tract and studies in the op/op mouse indicate that CSF-1 plays
important roles in female reproduction. Restoration of circulating CSF-1 to
op/op mice has preliminarily defined target cell populations that are regulated
either humorally or locally by the synthesis of cell-surface CSF-1 or by
sequestration of the CSF-1 proteoglycan. The CSF-1R is a tyrosine kinase encoded
by the c-fms proto-oncogene product. Studies by several groups have used cells
expressing either the murine or human CSF-1R in fibroblasts to pinpoint the
requirement of kinase activity and the importance of various receptor tyrosine
phosphorylation sites for signaling pathways stimulated by CSF-1. To investigate
post-CSF-1R signaling in the macrophage, proteins that are rapidly
phosphorylated on tyrosine in response to CSF-1 have been identified, together
with proteins associated with them. Studies on several of these proteins,
including protein tyrosine phosphates 1C, the c-cbl proto-oncogene product, and
protein tyrosine phosphatase-phi are discussed.
- Language of Publication
- English
- Unique Identifier
- 97135820
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- MeSH Heading (Major)
- Macrophage Colony-Stimulating Factor|GE/PD/*PH
- MeSH Heading
- Animal; Caenorhabditis elegans|EM/GE; Female; Fetal Development; Helminth
Proteins|PH; Human; Macrophages|DE/PH; Male; Membrane Proteins|PH; Mice; Mice,
Mutant Strains; Osteopetrosis|EM/GE; Phosphorylation; Protein Binding; Protein
Processing, Post-Translational; Protein-Tyrosine-Phosphatase|PH; Proto-Oncogene
Proteins|PH; Proto-Oncogenes; Receptors, Macrophage Colony-Stimulating
Factor|ME; Signal Transduction; Support, U.S. Gov't, P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 1040-452X
- Country of Publication
- UNITED STATES


Record 98 from database: MEDLINE
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- Title
- Pheno- and genotypic characteristics of human non-Hodgkin lymphoma
xenografts.
- Author
- Kopper L; Bánkfalvi A; Mihalik R; Timár J; Glant T
- Address
- Institute of Pathology and Experimental Cancer Research, Semmelweis Medical
University, Budapest, Hungary.
- Source
- Acta Histochem Suppl, 1990, 39:, 455-9
- Abstract
- The three human non-Hodgkin lymphoma xenografts with different morphological
appearance (lymphoblastic, centroblastic, centrocytic) had many common pheno-
and genotypic features positivity of B-cell markers, 14q+ chromosomal
abnormality, etc.). Furthermore, two lines (HT 58 and 130) expressed lambda
light chain monoclonally. The third line (HT 117) showed bigenotypic
rearrangement of light genes. A set of new anti-proteoglycan markers, especially
anti-chondroitin sulfate mAbs made possible to individualize the xenografts.
- Language of Publication
- English
- Unique Identifier
- 91180408
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- MeSH Heading (Major)
- Lymphoma, Non-Hodgkin's|GE/*PA
- MeSH Heading
- Animal; Antibodies, Monoclonal|DU; Cell Line; Chromosomes, Human, Pair 14;
DNA, Neoplasm|AN/GE; Genotype; Human; Neoplasm Transplantation; Phenotype;
Transplantation, Heterologous

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0567-7556
- Country of Publication
- GERMANY
- CAS Registry/EC Number
- 0 (Antibodies, Monoclonal); 0 (DNA, Neoplasm)


Record 99 from database: MEDLINE
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- Title
- The small proteoglycans of cartilage matrix.
- Author
- Stanescu V
- Address
- URA 584, CNRS Clinique M. Lamy, Hôpital des Enfants-Malades, Paris, France.
- Source
- Semin Arthritis Rheum, 1990 Dec, 20:3 Suppl 1, 51-64
- Abstract
- The small proteoglycans (PGs) of cartilage matrix represent a small fraction
of the total mass of PGs, but with a small size they can be present in
equivalent moles to the large PGs. Three types of PGs with a wide skeletal and
extraskeletal distribution, biglycan (PGI), decorin (PGII) and fibromodulin have
distinct but homologous core proteins containing leucin-rich sequences.
Carbohydrate substituants (one or two chondroitin sulfate/dermatan sulfate
chains for decorin and biglycan respectively, chains of keratan sulfate for
fibromodulin and oligosaccharides) present variations from tissue to tissue and
with age and other factors. Decorin and fibromodulin appear to interact with
collagen and to participate in the regulation of collagen matrices. In vitro
experiments indicate a role for small PGs in adhesion, multiplication,
differentiation, and migration of cells. Recent data on molecular biology of the
small PGs contribute to a better understanding of their functions and make the
evaluation of their role in hereditary diseases.
- Language of Publication
- English
- Unique Identifier
- 91142796
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- MeSH Heading (Major)
- Cartilage|*ME/PA; Proteoglycans|GE/IP/*ME
- MeSH Heading
- Animal; Cell Adhesion; Chemistry; Collagen|ME; Drug Interactions;
Glycosaminoglycans|CH; Human; Keratan Sulfate|ME; Molecular Weight;
Oligosaccharides|CH

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0049-0172
- Country of Publication
- UNITED STATES
- CAS Registry/EC Number
- 0 (Glycosaminoglycans); 0 (Oligosaccharides); 0 (Proteoglycans); 9007-34-5
(Collagen); 9056-36-4 (Keratan Sulfate)


Record 100 from database: MEDLINE
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- Title
- Clinical implications of cartilage metabolism in arthritis.
- Author
- Krane SM; Goldring MB
- Address
- Department of Medicine, Harvard Medical School, Massachusetts General
Hospital, Boston 02114.
- Source
- Eur J Rheumatol Inflamm, 1990, 10:1, 4-9
@
- Abstract
- The ability of articular cartilage to withstand repeated mechanical loading
with relatively little wear over a lifetime results from the properties of the
extracellular matrix (ECM) and the optimal function of the chondrocytes which
are responsible for the synthesis and presumably maintenance of this ECM. The
properties of the ECM are accounted for by the relationship of the major
aggregating, polyanionic, negatively charged proteoglycans with their potent
viscoelastic properties to the network of collagens and several noncollagenous
proteins. The major collagen (type II) interacts with type IX collagen in a
highly specific manner. Type IX collagen has a chondroitin sulfate side chain
and can also bind to the aggregating proteoglycans through a basic amino
terminal domain. In inflammation, injury and probably repeated wear, function of
the chondrocytess disturbed, mediated by the action of potent cytokines, which
results in release of degradative enzymes and alterations in the pattern of
synthesis of the ECM. Identification of the critical cytokines and the sequence
of events that result from their action should provide the basis for rational
prophylaxis and therapy of disorders such as osteoarthritis and rheumatoid
arthritis. Articular cartilage has unique mechanical properties which permit
repeated mechanical loading with relatively little wear over a lifetime. These
properties result from the special character of the extracellular matrix (ECM)
and optimal functioning of the component cells (chondrocytes) which are
responsible for the synthesis and presumably, maintenance of this matrix.
Articular chondrocytes survive and perform these critical functions in an
anaerobic environment remote from the vasculature and must derive their
nutrition from the synovial fluid.(ABSTRACT TRUNCATED AT 250 WORDS)
- Language of Publication
- English
- Unique Identifier
- 91031640
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- MeSH Heading (Major)
- Arthritis|*ME; Cartilage, Articular|*ME
- MeSH Heading
- Animal; Collagen|ME; Extracellular Matrix|ME; Human; Proteins|ME;
Proteoglycans|ME; Support, U.S. Gov't, P.H.S.

- Publication Type
- JOURNAL ARTICLE; REVIEW; REVIEW, TUTORIAL
- ISSN
- 0140-1610
- Country of Publication
- ENGLAND
- CAS Registry/EC Number
- 0 (Proteoglycans); 9007-34-5 (Collagen)

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