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Chondroitin

Results for your query:
Search all fields for: chondroitin on February 25, 1999
Published in 1966 through 1999
Only select references with abstracts available
Show references published in English only
Show references pertaining to humans
With an article type of: REVIEW

 

Documents: 1 to 100 of 130

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Title

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...1...
The role of glucosamine sulfate and chondroitin sulfates in the treatment of degenerative joint disease.
...2...
Danaparoid. A review of its pharmacology and clinical use in the management of heparin-induced thrombocytopenia.
...3...
College of American Pathologists Conference XXXI on laboratory monitoring of anticoagulant therapy: the clinical use and laboratory monitoring of low-molecular-weight heparin, danaparoid, hirudin and related compounds, and argatroban.
...4...
Danaparoid in the prevention of thromboembolic complications.
...5...
A comparative review of the adverse effect profiles of heparins and heparinoids.
...6...
Characterization of appican, the chondroitin sulfate proteoglycan form of the Alzheimer amyloid precursor protein.
...7...
Immunology of chondroitin/dermatan sulfate.
...8...
Thrombomodulin as a model of molecular mechanisms that modulate protease specificity and function at the vessel surface.
...9...
CD44 in inflammation and metastasis.
...10...
Pathogenesis and therapy of neuropathies associated with monoclonal gammopathies.
Menu Position #10
...11...
MHC class II antigen processing: biology of invariant chain.
...12...
Effects of cryopreservation upon vein function in vivo.
...13...
Update on chemonucleolysis.
...14...
New antithrombotic agents for the prevention and treatment of deep vein thrombosis.
...15...
Cell surface chondroitin sulfate proteoglycans in tumor cell adhesion, motility and invasion.
...16...
Heparinoid anticoagulation and topical fibrin sealant in heparin-induced thrombocytopenia.
...17...
Glycosaminoglycans: structure and interaction.
...18...
Mechanisms for the anticoagulant effect of heparin and related polysaccharides.
...19...
Mucosal mast cells in the rat and in man.
...20...
Viscoelastic agents.
Menu Position #20
...21...
Keratan sulphate--a 'reserve' polysaccharide?
...22...
Structure-function relationships of the thrombin-thrombomodulin interaction.
...23...
The structure, function and turnover of aggrecan, the large aggregating proteoglycan from cartilage.
...24...
Mapping of proteoglycans in atherosclerotic lesions.
...25...
Mesangial cell proteoglycans: synthesis and metabolism.
...26...
Advances in corneal preservation.

This study describes how a "mixture" based on chondroitin is so "alive" that a eye-ball not only stays alive in it, but grows -- while awaiting transplantation!

...27...
Chondroitin sulfate proteoglycans as mediators of axon growth and pathfinding.
...28...
Chondroprotection with chondroitin sulfate.
...29...
Neurocan and phosphacan: two major nervous tissue-specific chondroitin sulfate proteoglycans.
...30...
Arterial wall proteoglycans--biological properties related to pathogenesis of atherosclerosis.
Menu Position #30
...31...
Proteoglycans and cell adhesion. Their putative role during tumorigenesis.
...32...
Glycosaminoglycan chondroprotection: pharmacological vistas.
...33...
Angiogenesis in wound healing and tumor metastasis.
...34...
C1q inhibitor (chondroitin-4-sulfate proteoglycan): structure and function.
...35...
Molecular events that control the protein C anticoagulant pathway.
...36...
Hair follicle proteoglycans.
...37...
Altered proteoglycan gene expression and the tumor stroma.
...38...
Molecular cloning and analysis of the protein modules of aggrecans.
...39...
Roles of aggrecan, a large chondroitin sulfate proteoglycan, in cartilage structure and function.
...40...
Hydrocephalus, lumbar canal stenosis and Maroteaux-Lamy syndrome (mucopolysaccharidosis type 6). Case report.
Menu Position #40
...41...
Overview of the corneal toxicity of surgical solutions and drugs: and clinical concepts in corneal edema.
...42...
The chemical morphology of the vitreous.
...43...
Analysis of glycosaminoglycans and their oligosaccharide fragments by capillary electrophoresis.
...44...
Inhibitory molecules in development and regeneration.
...45...
Proteoglycans: the "Teflon" of the airways?
...46...
Proteoglycans in male reproductive tract.
...47...
Regulation of proteoglycan expression in fibrotic liver and cultured fat-storing cells.
...48...
Activation of proteoglycan synthesis in injured liver--a brief review of molecular and cellular aspects.
...49...
Molecular cloning and analysis of the protein modules of aggrecans.
...50...
Altered proteoglycan gene expression and the tumor stroma.
Menu Position #50
...51...
CD44: structure, function, and association with the malignant process.
...52...
Basement membranes and pulmonary development.
...53...
Functions of brain chondroitin sulfate proteoglycans during developments: interactions with adhesion molecules.
...54...
The NG2 chondroitin sulfate proteoglycan: a multifunctional proteoglycan associated with immature cells.
...55...
Viscoelastic substances in ophthalmology.
...56...
Glycosaminoglycans in autoimmunity.
...57...
Adhesion molecules in neural crest development.
...58...
Functional domains of the human C1q A-chain.
...59...
The mast cell--a potential link between inflammation and cellular cholesterol deposition in atherogenesis.
...60...
Effects of extracellular matrix components on cell locomotion.
Menu Position #60
...61...
Proteoglycans and the modulation of cell adhesion by steric exclusion.
...62...
Proteoglycans of basement membranes.
...63...
Small proteoglycans.
...64...
The link proteins.
...65...
Genetic defects in proteoglycan biosynthesis.
...66...
Association of apo B lipoproteins with arterial proteoglycans: pathological significance and molecular basis.
...67...
The role of the invariant chain in mucosal immunity.
...68...
Biological activities and clinical application of M-CSF.
...69...
Proteoglycans in cell regulation.
...70...
Maternal malaria and parasite adhesion.
Menu Position #70
...71...
Lipoprotein (a) regulates plasmin generation and inhibition.
...72...
Proteoglycans of basement membranes.
...73...
Proteoglycans: many forms and many functions.
...74...
Neuropathies associated with monoclonal gammapathies [see comments]
...75...
The biology and action of colony stimulating factor-1.
...76...
The clinical role of immunoscintigraphy for the detection of ocular melanoma.
...77...
Facilitatory and inhibitory effects of glial cells and extracellular matrix in axonal regeneration.
...78...
Investigational approaches to pulmonary hypertension.
...79...
A role for glycosaminoglycans in the development of collagen fibrils.
...80...
Cartilage proteoglycans: structure and potential functions.
Menu Position #80
...81...
Mechanisms of astrocyte-directed neurite guidance.
...82...
Experimental and clinical pharmacology of glycosaminoglycans (GAGs).
...83...
The role of heparan sulfate proteoglycans in the pathogenesis of Alzheimer's disease.
...84...
Small proteoglycans.
...85...
The link proteins.
...86...
Proteoglycans and hyaluronan in female reproductive organs.
...87...
Structure and biological functions of keratan sulfate proteoglycans.
...88...
Thrombomodulin structure and function.
...89...
x82p4and the adhesion of neoplastic cells.
...90...
Thrombin specificity.
Menu Position #90
...91...
Syndecan, a developmentally regulated cell surface proteoglycan that binds extracellular matrix and growth factors.
...92...
Plasmalogens, phospholipases A2 and signal transduction.
...93...
Cell-extracellular matrix interactions in the ductus arteriosus and perinatal pulmonary circulation.
...94...
Brevican: a major proteoglycan in adult brain.
...95...
Brain aggrecan.
...96...
Versican.
...97...
Biology and action of colony--stimulating factor-1.
...98...
Pheno- and genotypic characteristics of human non-Hodgkin lymphoma xenografts.
...99...
The small proteoglycans of cartilage matrix.
...100...
Clinical implications of cartilage metabolism in arthritis.
Menu Position #100

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NLM database Documents

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

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MeSH Heading (Major)
Chondroitin Sulfates|CH/ME/*TU; Glucosamine|ME/*TU; Osteoarthritis|*DT
MeSH Heading
Drug Therapy, Combination; Human

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

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

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MeSH Heading (Major)
Chondroitin Sulfates|AE/*PD/PK/*TU; Dermatan Sulfate|AE/*PD/PK/*TU; Heparitin Sulfate|AE/*PD/PK/*TU; Thrombocytopenia|CI/*DT/PP
MeSH Heading
Blood Coagulation|DE; Drug Combinations; Heparin|AE; Heparinoids|AE/PD/PK/TU; Human

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

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

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MeSH Heading (Major)
Anticoagulants|AD/*TU
MeSH Heading
Chondroitin Sulfates|AD/TU; Dermatan Sulfate|AD/TU; Drug Combinations; Drug Monitoring|MT; Heparin|AD/TU; Heparin, Low-Molecular-Weight|AD/TU; Heparitin Sulfate|AD/TU; Hirudin|AA/AD/TU; Human; Pathology, Clinical|MT; Pipecolic Acids|AD/TU; Thromboembolism|BL/DT

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

 

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

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MeSH Heading (Major)
Chondroitin Sulfates|CH/PD/*TU; Dermatan Sulfate|CH/PD/*TU; Heparin|CH/PD/*TU; Heparitin Sulfate|CH/PD/*TU; Postoperative Complications|*PC; Thromboembolism|*PC
MeSH Heading
Drug Combinations; Human; Randomized Controlled Trials

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

Record 5 from database: MEDLINE
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Title
A comparative review of the adverse effect profiles of heparins and heparinoids.
Author
Borris LC; Lassen MR
Address
Department of Orthopaedics, Aalborg Hospital, Denmark.
Source
Drug Saf, 1995 Jan, 12:1, 26-31
Abstract
On the basis of the results of the 11 studies reviewed, thromboprophylaxis with unfractionated heparin, low molecular weight (LMW) heparin or a heparinoid (danaparoid sodium; Org 10172) in patients undergoing total hip replacement did not show any important clinical differences with respect to the tolerability profiles of the different compounds. However, as a result of the great variability in the presentation and evaluation of blood losses and bleeding complications in these studies, it is mandatory to perform a direct comparison of the different compounds in question in a double-blind, prospective clinical study.
Language of Publication
English
Unique Identifier
95260439

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MeSH Heading (Major)
Chondroitin Sulfates|AD/*AE/TU; Dermatan Sulfate|AD/*AE/TU; Fibrinolytic Agents|AD/*AE/TU; Heparin|AD/*AE/TU; Heparinoids|AD/*AE/TU; Heparitin Sulfate|AD/*AE/TU
MeSH Heading
Comparative Study; Hemorrhage|CI; Hip Prosthesis; Human; Molecular Weight; Postoperative Complications|CI; Thrombocytopenia|CI; Thrombosis|PC; Wound Infection|CI

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

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

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MeSH Heading (Major)
Alzheimer Disease|*ME/PP; Amyloid beta-Protein Precursor|GE/ME/*PH; Proteochondroitin Sulfates|*PH; Proteoglycans|ME/*PH
MeSH Heading
Amino Acid Sequence; Animal; Chondroitin Sulfates|ME; Human; Molecular Sequence Data

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

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

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MeSH Heading (Major)
Antigens|*IM; Chondroitin Sulfates|CH/*IM; Dermatan Sulfate|CH/*IM
MeSH Heading
Antibodies, Monoclonal|IM; Antibody Specificity; Carbohydrate Sequence; Epitopes|AN; Human; Molecular Sequence Data; Molecular Structure

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

Record 8 from database: MEDLINE
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Title
Thrombomodulin as a model of molecular mechanisms that modulate protease specificity and function at the vessel surface.
Author
Esmon CT
Address
Oklahoma Medical Research Foundation, Department of Pathology, University of Oklahoma Health Sciences Center, Oklahoma City, USA.
Source
FASEB J, 1995 Jul, 9:10, 946-55
Abstract
The protein C anticoagulant system generates an "on demand" physiologic anticoagulant response. The pathway is initiated when thrombin binds to the endothelial cell thrombin binding protein, thrombomodulin. The complex exhibits dramatically altered macromolecular specificity. It rapidly cleaves the protein C zymogen to form the anticoagulant, activated protein C. Complex formation between thrombin and thrombomodulin also prevents thrombin, the enzyme responsible for clot formation and a potent platelet activator, from being able to clot fibrinogen or to activate platelets. Structural, kinetic, and competition studies suggest that thrombomodulin blocks these clotting reactions by masking the binding sites for fibrinogen and the platelet thrombin receptor. Stimulation of protein C activation appears to occur through conformational changes in the extended binding pocket of thrombin. This prevents repulsive interactions with protein C that exist when the free enzyme attempts to dock with this substrate. In addition to protein-protein interactions, thrombomodulin has a covalently associated chondroitin sulfate moiety. Chondroitin sulfate binds to a basic surface on thrombin that is also involved in heparin interaction. The chondroitin sulfate enhances the affinity of thrombin for thrombomodulin approximately 10- to 20-fold, making thrombomodulin a more potent inhibitor of coagulation, altering thrombin's conformation and specificity, and accelerating thrombin inhibition by the serpin, antithrombin. These properties make thrombomodulin a molecular switch ideally suited to trigger an anticoagulant response when too much thrombin is generated. The importance of the system is documented by the clinical observation that patients deficient in protein C often die of massive thrombotic complications that can be reversed or prevented by infusion of protein C.
Language of Publication
English
Unique Identifier
95340068

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MeSH Heading (Major)
Blood Coagulation|*; Proteins|*ME; Thrombomodulin|*PH
MeSH Heading
Chondroitin Sulfates|ME; Comparative Study; Fibrinogen|ME; Human; Platelet Activation; Protein C|ME; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Thrombin|ME

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

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

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MeSH Heading (Major)
Antigens, CD44|*PH; Inflammation|*PP; Neoplasm Metastasis|*PP; Neoplasms|PA/*PP
MeSH Heading
Animal; Antigens, CD|PH; Chondroitin Sulfates|ME; Human; Hyaluronic Acid|ME; Proteoglycans|CH/ME; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.; Variation (Genetics)

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

Record 10 from database: MEDLINE
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Title
Pathogenesis and therapy of neuropathies associated with monoclonal gammopathies.
Author
Latov N
Address
Department of Neurology, College of Physicians and Surgeons, Columbia University, New York, NY 10032, USA.
Source
Ann Neurol, 1995 May, 37 Suppl 1:, S32-42
Abstract
Approximately 10% of patients with peripheral neuropathy of otherwise unknown etiology have an associated monoclonal gammopathy. Both the neuropathies and the monoclonal gammopathies in these patients are heterogeneous, but several distinct clinical syndromes that may respond to specific therapies can be recognized. It is important to recognize these syndromes because monoclonal gammopathies also occur in 1% of the normal adult population, and in some cases, monoclonal gammopathies are coincidental and unrelated to the neuropathy. In patients with IgM monoclonal gammopathies, IgM M proteins frequently have autoantibody activity and are implicated in the pathogenesis of the neuropathy. IgM M proteins that bind to myelin-associated glycoprotein (MAG) have been shown to cause demyelinating peripheral neuropathy; anti-GM1 antibody activity is associated with predominantly motor neuropathy, and anti-sulfatide or chondroitin sulfate antibodies are associated with sensory neuropathy. The IgM monoclonal gammopathies may be malignant or nonmalignant, and polyclonal antibodies with the same specificities are associated with similar clinical presentations in the absence of monoclonal gammopathy. IgG or IgA monoclonal gammopathies are associated with neuropathy in patients with osteosclerotic myeloma or the POEMS syndrome (polyneuropathy, organomegaly, endocrinopathy myeloma, and skin changes). Amyloidosis or cryoglobulinemic neuropathies can occur with either IgM or IgG and IgA monoclonal gammopathies. Therapeutic intervention depends on the specific clinical syndrome but is generally directed at removing the autoantibodies, reducing the number of monoclonal B cells, and interfering with the effector mechanisms.
Language of Publication
English
Unique Identifier
97122966

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MeSH Heading (Major)
Autoimmune Diseases|*ET/IM/TH; Paraproteinemias|*CO/EP/IM/TH; Peripheral Nervous System Diseases|EP/*ET/IM/TH
MeSH Heading
Adult; Aged; Amyloidosis|ET/IM/TH; Antibody Specificity; Antineoplastic Agents|TU; Autoantibodies|IM; Autoantigens|IM; Chondroitin Sulfates|IM; Gangliosides|IM; Human; IgA|IM; IgG|IM; IgM|IM; Immunoglobulins, Intravenous|TU; Middle Age; Myelin-Associated Glycoprotein|IM; Paraneoplastic Syndromes|ET/IM/TH; Paraproteins|AN/IM; Plasmapheresis; Sulfatides|IM

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

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

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MeSH Heading (Major)
Antigen Presentation|*IM; Histocompatibility Antigens Class II|*IM/ME
MeSH Heading
Animal; Chondroitin Sulfates|PH; Endocytosis|IM; Human; Peptides|IM; Protein Binding; Protein Processing, Post-Translational

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

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

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MeSH Heading (Major)
Cryopreservation|*MT; Veins|*/IM/PP/TR
MeSH Heading
Animal; Chondroitin Sulfates; Cryoprotective Agents; Dimethyl Sulfoxide; Human; Immunosuppression; Platelet Aggregation Inhibitors|PD; Thrombophlebitis|PC; Transplantation, Autologous; Transplantation, Homologous

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

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

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MeSH Heading (Major)
Chymopapain|*TU; Intervertebral Disk Chemolysis|*; Intervertebral Disk Displacement|*DT/SU
MeSH Heading
Animal; Chondroitin Lyases|TU; Collagenases|TU; Comparative Study; Human; Meta-Analysis; Randomized Controlled Trials

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

Record 14 from database: MEDLINE
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Title
New antithrombotic agents for the prevention and treatment of deep vein thrombosis.
Author
Boneu B
Address
Laboratoire de Recherche sur l'HÆemostase et la Thrombose Toulouse, France.
Source
Haemostasis, 1996 Oct, 26 Suppl 4:, 368-78
Abstract
Besides low molecular weight heparins (LMWHs) a number of new antithrombotic agents have been evaluated mainly in the prevention of deep vein thrombosis (DVT) and, to a lesser extent, in the treatment of established DVT. They include the Pentasaccharide, a synthetic ultra LMWH, Dermatan Sulphate, a glycosaminoglycan which activates heparin cofactor II, Orgaran, a mixture of Heparan and of Dermatan Sulphate, Hirulog and Hirudin, two direct thrombin inhibitors. The efficacy and safety of these compounds have been studied in comparison with a placebo or with unfractionated heparin but not with LMWH which is considered as a gold standard for these clinical indications. It is thus difficult at present to appreciate the advantages of these new antithrombotic agents over conventional LMWH therapy.
Language of Publication
English
Unique Identifier
97133746

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MeSH Heading (Major)
Fibrinolytic Agents|*TU; Pulmonary Embolism|DT/*PC; Thrombophlebitis|DT/*PC
MeSH Heading
Anticoagulants|TU; Antithrombin III|CH/ME; Binding Sites; Chondroitin Sulfates|TU; Clinical Trials; Dermatan Sulfate|TU; Drug Screening; Factor Xa|AI; Heparin|CH/ME/TU; Heparin, Low-Molecular-Weight|TU; Heparitin Sulfate|TU; Human; Multicenter Studies; Oligosaccharides|TU; Postoperative Complications|PC; Recurrence; Thrombin|AI

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

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

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MeSH Heading (Major)
Cell Adhesion|*PH; Cell Movement|*PH; Chondroitin|*BI; Proteoglycans|*BI
MeSH Heading
Human

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

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

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MeSH Heading (Major)
Anticoagulants|*TU; Chondroitin Sulfates|*TU; Coronary Artery Bypass|*; Dermatan Sulfate|*TU; Fibrin Tissue Adhesive|*TU; Heparin|*AE; Heparinoids|*TU; Heparitin Sulfate|*TU; Thrombocytopenia|*CI
MeSH Heading
Case Report; Human; Male; Middle Age

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

Record 17 from database: MEDLINE
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Title
Glycosaminoglycans: structure and interaction.
Author
Chakrabarti B; Park JW
Address
 
Source
CRC Crit Rev Biochem, 1980, 8:3, 225-313
Abstract
In the last few years, there has been considerable progress in the studies on glycosaminoglycans, a group of acidic polysaccharides present in the intercellular matrix of connective tissue. X-ray diffraction studies have indicated that these polymers can exist in the condensed phase in some helical form. Chiroptical and hydrodynamic measurements have provided significant information regarding the molecular conformation in solution and other physicochemical properties of the polymers. Studies related to the interaction properties of glycosaminoglycans with polypeptides, metal ions, and other molecules are numerous. This review covers mainly the results and their interpretations of both published and as yet unpublished material of the 1970s, but certain previous data are also included. A present-day concept regarding the structure and interaction properties of these molecules on the basis of various physicochemical measurements is presented. The biosynthesis and metabolism of glycosaminoglycans, and the structure of proteoglycans and glycoproteins, are not discussed.
Language of Publication
English
Unique Identifier
81023329

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MeSH Heading (Major)
Glycosaminoglycans|*
MeSH Heading
Animal; Cations; Chemistry; Chemistry, Physical; Chondroitin; Chondroitin Sulfates; Circular Dichroism; Dermatan Sulfate; Heparin; Heparitin Sulfate; Human; Hyaluronic Acid; Hydrogen-Ion Concentration; Keratan Sulfate; Macromolecular Systems; Metals|ME; Models, Molecular; Molecular Conformation; Spectrum Analysis; Support, U.S. Gov't, Non-P.H.S.; Support, U.S. Gov't, P.H.S.; Tissue Distribution; X-Ray Diffraction

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

Record 18 from database: MEDLINE
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Title
Mechanisms for the anticoagulant effect of heparin and related polysaccharides.
Author
Ofosu FA
Address
Canadian Red Cross Society, Blood Transfusion Service, Hamilton, Ontario.
Source
Nouv Rev Fr Hematol, 1988, 30:3, 155-60
Abstract
The anticoagulant actions of heparin and related polysaccharides can best be addressed by answering the following 2 questions: to what extent do unfractionated heparin, low molecular weight heparins, dermatan sulfate and heparan sulfate inhibit the activation of prothrombin in plasma depleted of antithrombin III and heparin cofactor II? What roles do antithrombin III and heparin cofactor II play in the expression of the overall anticoagulant effects of heparin, low molecular weight heparins, dermatan sulfate and heparan sulfate? Since only heparin can, but only weakly at best, inhibit the activation of prothrombin in plasma depleted of both antithrombin III and heparin cofactor II, it is obvious that the anticoagulant effects of heparin, low molecular weight heparins, dermatan sulfate and heparan sulfate are mediated primarily by their catalytic effects on the antiprotease actions of antithrombin III (heparin, low molecular weight heparins and heparan sulfate) and heparin cofactor II (dermatan sulfate). The catalytic efficiencies of various glycosaminoglycans (GAGs) on the inhibition of thrombin by undiluted plasma follow in the order of the ability of each GAG to inhibit the intrinsic pathway activation of prothrombin. The reasons for this observation probably follow from the effects of GAGs on the 2 positive amplification reactions of thrombin during blood coagulation. Factor VIIIa and factor Va, which directly or indirectly contribute to the rapid formation of prothrombinase, arise from the limited proteolysis of factor VIII and factor V by thrombin and/or factor Xa. On depletion of thrombin by enhanced formation of thrombin-antithrombin III or thrombin-heparin cofactor II, factor Xa provides the only mechanism by which factor VIII and factor V activation in plasma will proceed.(ABSTRACT TRUNCATED AT 250 WORDS)
Language of Publication
English
Unique Identifier
88335518

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MeSH Heading (Major)
Anticoagulants|*; Chondroitin|*AA; Dermatan Sulfate|*PD; Glycosaminoglycans|*PD; Heparin|*PD; Heparitin Sulfate|*PD
MeSH Heading
Antithrombin III|AI; Human; Support, Non-U.S. Gov't; Thrombin|AI

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

 

Record 19 from database: MEDLINE
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Title
Mucosal mast cells in the rat and in man.
Author
Enerbäck L
Address
 
Source
Int Arch Allergy Appl Immunol, 1987, 82:3-4, 249-55
Abstract
The proteoglycan structure of mucosal mast cells (MMC) of the two species has been analyzed with histochemical in situ techniques. The findings indicate that human MMC, like human mast cells of several other sites, contain a heparin proteoglycan, unlike rat MMC which lack heparin but contain an oversulphated chondroitin sulphate. However, the dye-binding of the human MMC proteoglycan, like that of the rat, is highly susceptible to blocking by formaldehyde. Human MMC also exhibit a lower critical electrolyte concentration (CEC) of dye-binding than mast cells of other connective tissue sites, suggesting a relatively lower charge density and/or molecular weight of the glycosaminoglycan of the MMC. These findings thus suggest that the human MMC like those of the rat have a distinctive proteoglycan structure. Recent findings of another group indicate that the human MMC like those of the rat have also a distinctive proteinase composition. Finally, the mast cell response of the nasal mucosa during birch pollen allergy shows fundamental similarities to the nematode response of the rat intestinal mucosa. During both conditions mast cells are redistributed from the lamina propria into the epithelium, probably as a result of migration of mast cells or mast cell precursors. Taken together, these findings suggest the existence of a distinctive MMC phenotype also in man.
Language of Publication
English
Unique Identifier
87193224

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MeSH Heading (Major)
Chondroitin|*AA; Chondroitin Sulfates|*AN; Heparin|*AA/AN; Mast Cells|*AN; Mucous Membrane|*CY; Proteoglycans|*AN; Rats|*AH
MeSH Heading
Animal; Comparative Study; Cystitis|PA; Hay Fever|PA; Human; Intestinal Diseases, Parasitic|PA; Organ Specificity; Peptide Hydrolases|AN; Phenotype; Species Specificity; Staining; Support, Non-U.S. Gov't

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

 

Record 20 from database: MEDLINE
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Title
Viscoelastic agents.
Author
Larson RS; Lindstrom RL; Skelnik DL
Address
Department of Ophthalmology, University of Minnesota School of Medicine, Minneapolis.
Source
CLAO J, 1989 Apr-Jun, 15:2, 151-60
Abstract
Viscoelastic materials possess a unique set of properties that result from their chemical structure. These properties enable them to protect the corneal endothelium and epithelium from mechanical trauma and to maintain an intraocular space, such as the anterior or vitreous chambers, even in the face of an open incision. Hence viscoelastic materials have been successfully applied to many areas of ophthalmic surgery, most notably anterior segment surgery, with few complications. There are currently three commercially available viscoelastic preparations, and several new preparations are in various stages of development.
Language of Publication
English
Unique Identifier
89249770

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MeSH Heading (Major)
Acrylic Resins|*TU; Chondroitin|*TU; Eye|PH/*SU; Hyaluronic Acid|*TU; Methylcellulose|*AA/TU
MeSH Heading
Anterior Eye Segment|PH/SU; Chemistry; Drug Combinations|TU; Endothelium, Corneal|PH; Human; Intraocular Pressure

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

 

Record 21 from database: MEDLINE
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Title
Keratan sulphate--a 'reserve' polysaccharide?
Author
Scott JE
Address
Manchester University, U.K.
Source
Eur J Clin Chem Clin Biochem, 1994 Apr, 32:4, 217-23
Abstract
The early history of keratan sulphate and its proteoglycans is briefly described. Studies were overlooked that could have had a profound influence on later work. Early methods of writing the structures of keratan and chondroitin sulphates obscured the fundamental relationships between them. Both are now seen to be based on the same polymer backbone poly(Gal beta 1:4 Glc beta 1-3). Confusion over the complicated sulphation patterns in keratan sulphate was clarified by the domain structure idea by the group of Helmut Greiling. Keratan sulphate is characteristic of avascular tissues (cartilages, intervertebral discs, corneal stromas) that get their oxygen supplies by diffusion. Stockwell's early idea that the distribution of keratan sulphate in cartilages was a response to the poor supply of oxygen has been generalised, to the hypothesis that keratan sulphate is a functional substitute for chondroitin sulphate under conditions of oxygen lack. The keratan:chondroitin sulphate ratios in discs, corneas of different species, and changes therein with age can be explained on this basis. The biochemical controlling step is probably the NAD:NADH ratio. Keratan sulphate may thus be a 'reserve' polysaccharide, able to do the job of chondroitin sulphate in adverse conditions of oxygen supply. Keratan and chondroitin/dermatan sulphates have similar functions in corneal stroma, and probably in the other connective tissues in which they are found. They swell the collagenous matrix, keeping the fibrils apart. Even more importantly, they probably act as tissue organisers, orienting the fibrils vis-a-vis each other via specific interactions of their proteoglycan protein cores with the fibrils.(ABSTRACT TRUNCATED AT 250 WORDS)
Language of Publication
English
Unique Identifier
94312496

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MeSH Heading (Major)
Keratan Sulfate|*CH/*PH; Polysaccharides|*PH
MeSH Heading
Animal; Carbohydrate Sequence; Human; Molecular Sequence Data; Support, Non-U.S. Gov't

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

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

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MeSH Heading (Major)
Receptors, Cell Surface|*ME; Thrombin|*ME
MeSH Heading
Amino Acid Sequence; Animal; Binding Sites; Blood Coagulation; Chondroitin Sulfates|ME; Human; Ligands; Molecular Sequence Data; Peptide Fragments|CS/ME; Protein Binding; Protein Conformation; Recombinant Fusion Proteins|ME; Structure-Activity Relationship; Support, U.S. Gov't, P.H.S.

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

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

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MeSH Heading (Major)
Cartilage|CH/ME/*PH; Proteoglycans|CH/ME/*PH
MeSH Heading
Amino Acid Sequence; Animal; Human; Molecular Sequence Data; Proteochondroitin Sulfates|CH/ME/PH; Structure-Activity Relationship; Support, Non-U.S. Gov't

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

Record 24 from database: MEDLINE
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Title
Mapping of proteoglycans in atherosclerotic lesions.
Author
Völker W; Schmidt A; Oortmann W; Broszey T; Faber V; Buddecke E
Address
University of Münster, Federal Republic of Germany.
Source
Eur Heart J, 1990 Aug, 11 Suppl E:, 29-40
Abstract
The involvement of sulphated glycosaminoglycans in atherosclerotic changes have been studied in human and rat arteries, and biochemical experiments have revealed that a significant increase in the contents of chondroitin sulphate/dermatan sulphate and cholesterol, but loss of heparan sulphate, occurs in human atherosclerotic arterial tissues. Electron micrographs have revealed that extracellular deposits of lipid are predominantly present in areas rich in chondroitin sulphate proteoglycans but not in areas rich in collagen bundles and dermatan sulphate proteoglycans. The different types of proteoglycans have been distinguished in situ by the cuprolinic blue staining method and enzymatic degradation experiments, and their topohistochemical distributi