Activation of heparin cofactor II by dermatan sulfate.
TL;DR: 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.
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TL;DR: The results indicate that the wide diversity of polysaccharides from marine alga and invertebrates is a useful tool to elucidate structure/anticoagulant activity relationships.
387 citations
TL;DR: The results indicate that different structural features determine not only the anticoagulant potency of the sulfated fucans but also the mechanism by which they exert this activity, and the branched fucan from brown algae are direct inhibitors of thrombin, whereas the linear fucANS from echinoderms require the presence of antithrombin or heparin cofactor II for inhibition ofThrombin.
370 citations
TL;DR: The smallest fragment of dermatan sulfate that bound to heparin cofactor II with high affinity was isolated, and it was found that clustering of these disaccharides must occur during biosynthesis to form the high-affinity binding site for HCII.
306 citations
TL;DR: Assays with purified reagents show that the fucosylated chondroitin sulfate can potentiate the thrombin inhibition activity of both antithrombin and heparin cofactor II.
299 citations
TL;DR: Anticoagulant activities of the four fCSs can be attributed to the difference in sulfation pattern of the fucose branch of the chondroitin sulfate, and 2,4- O -disulfation is important for anticoagULant activity.
230 citations
References
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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.
5,798 citations
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.
1,293 citations
TL;DR: STRUCTURE and BIOSYNTHESIS of GL YCOSAMINOGL YCANS: Foundations and biosynthesis of GL ycans.
Abstract: STRUCTURE AND BIOSYNTHESIS OF GL YCOSAMINOGL YCANS . 387 Polysaccharide Chains 387 Disaccharide units 387 Polymer sequence 390 Polymer shape 393 Proteog/ycans 393
803 citations
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.
408 citations
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.
317 citations