Activation of heparin cofactor II by dermatan sulfate.
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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.About:
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.read more
Citations
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Inhibitory effect of the combination of xylitol and funoran on Streptococcus mutans biofilm formation on the uncoated surface
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Plasmin stimulates the release of dermatan sulfate from vascular smooth muscle cells in culture.
Toshiyuki Kaji,Syouichi Hiraga,Atsushi Mishima,Chika Yamamoto,Michiko Sakamoto,Fumitomo Koizumi +5 more
TL;DR: It was suggested that a endogenous thrombin inhibitor heparin cofactor II may be activated in the liquid phase by dermatan sulfate released from plasmin-stimulated vascular smooth muscle cells when the vascular is disrupted and plasma is exposed to extravessel.
References
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A modified uronic acid carbazole reaction
T. Bitter,Helen Muir +1 more
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.
Ulf Lindahl,Magnus Höök +1 more
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.
Journal ArticleDOI
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.
Related Papers (5)
Heparin cofactor II. Purification and properties of a heparin-dependent inhibitor of thrombin in human plasma.
Structure of a dermatan sulfate hexasaccharide that binds to heparin cofactor II with high affinity.
The protease specificity of heparin cofactor II. Inhibition of thrombin generated during coagulation.
K A Parker,Douglas M. Tollefsen +1 more