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Chondroitin

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Search all fields for: chondroitin on February 25, 1999

Published in 1966 through 1999

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Documents: 1 to 100 of 130

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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

Record 67 from database: MEDLINE
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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