Title : Structural and conformational aspects of the anticoagulant and anti-thrombotic activity of heparin and dermatan sulfate.

Pub. Date : 2004

PMID : 15078125






5 Functional Relationships(s)
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1 Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin). Dermatan Sulfate serpin family D member 1 Homo sapiens
2 Heparin and other iduronic acid-containing glycosaminoglycans (GAG) such as dermatan sulfate exert their anticoagulant properties primarily by accelerating the rate of inhibition of the natural protease inhibitors antithrombin III (AT, which inhibits both factor Xa and thrombin) and heparin cofactor II (HCII, which selectively inhibits thrombin). Dermatan Sulfate serpin family D member 1 Homo sapiens
3 Although AT and HCII are structural homologs, only heparin binds to AT, and HCII has different binding sites for heparin and dermatan sulfate. Dermatan Sulfate serpin family D member 1 Homo sapiens
4 Whereas the binding site of heparin for AT is a unique pentasaccharide sequence contained in only about one third of the chains of this GAG, HCII-binding sequences of heparin and dermatan sulfate are less specific and contained in practically all the GAG chains. Dermatan Sulfate serpin family D member 1 Homo sapiens
5 Whereas it inactivates the binding site for AT causing a drop of the anticoagulant activity, it enhances the HCII-associated activity of both heparin and dermatan sulfate. Dermatan Sulfate serpin family D member 1 Homo sapiens