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Open AccessJournal ArticleDOI

Activation of heparin cofactor II by dermatan sulfate.

Douglas M. Tollefsen, +2 more
- 10 Jun 1983 - 
- Vol. 258, Iss: 11, pp 6713-6716
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TLDR
It is suggested that HCII is the only thrombin inhibitor in human plasma that can be activated by dermatan sulfate.
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This article is published in Journal of Biological Chemistry.The article was published on 1983-06-10 and is currently open access. It has received 428 citations till now. The article focuses on the topics: Heparin cofactor II & Dermatan sulfate.

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Citations
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Journal ArticleDOI

Antithrombotic activity of avian crown dermatan sulfate

TL;DR: In vivo, avian crown dermatan sulfate more effectively prevented the development of thrombus in a rat deep vein thrombosis model and in an in vitro test, bovine intestine dermatans sulfate exhibited stronger effects on stimulation of heparin cofactor II and activation of Glu-plasminogen by tissue plasminogens activator.
Journal ArticleDOI

Evolution of thrombosis.

TL;DR: Thrombi undergo constant structural change as they age and are gradually replaced by fibrin in the arterial and venous circulation.
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The natural anticoagulants.

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Tolerability and Clinical Efficacy of Desmin in the Treatment of Superficial Thrombovaricophlebitis

TL;DR: Desmin proved capable of effectively improving the symptoms of patients affected by thrombovari cophlebitis, inducing rapid regression by the tenth day of treatment, and the systemic tolerability and local tolerance of the drug was good.
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Anticoagulant activity of a dermatan sulfate from the skin of the shark Scyliorhinus canicula.

TL;DR: The sharkskin dermatan sulfate constitutes a potentially useful drug of interest in anticoagulant therapy and had no effect on platelet aggregation and activation induced by various agonists.
References
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Journal ArticleDOI

A modified uronic acid carbazole reaction

TL;DR: It has been found possible to distinguish betweenHeparin, heparin derivatives, and other polyuronides of connective tissue by comparing the effect of chlorides on the color yield in both procedures by modifying Dische's carbazole reaction for uronic acid in the presence of borate.
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The Purification and Mechanism of Action of Human Antithrombin-Heparin Cofactor

TL;DR: It is suggested that heparin binds to the inhibitor and causes a conformational change which results in a more favorable exposure of the arginine reactive site, allowing a rapid interaction with thrombin.
Journal ArticleDOI

Glycosaminoglycans and their binding to biological macromolecules.

TL;DR: STRUCTURE and BIOSYNTHESIS of GL YCOSAMINOGL YCANS: Foundations and biosynthesis of GL ycans.
Journal ArticleDOI

Heparin cofactor II. Purification and properties of a heparin-dependent inhibitor of thrombin in human plasma.

TL;DR: A previously unrecognized heparin-dependent inhibitor of thrombin from human plasma is isolated and is a relatively ineffective inhibitor of coagulation factor Xa.
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The kinetics of hemostatic enzyme-antithrombin interactions in the presence of low molecular weight heparin.

TL;DR: It is demonstrated that binding of heparin to antithrombin is required for the mucopolysaccharide-dependent enhancement in the rates of neutralization of thrombin, factor IXa, factor Xa, or plasmin by the protease inhibitor.
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