Title : N-Acetylgalactosamine 4,6-O-sulfate residues mediate binding and activation of heparin cofactor II by porcine mucosal dermatan sulfate.

Pub. Date : 2006 Aug

PMID : 16624894






8 Functional Relationships(s)
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1 N-Acetylgalactosamine 4,6-O-sulfate residues mediate binding and activation of heparin cofactor II by porcine mucosal dermatan sulfate. Dermatan Sulfate serpin family D member 1 Homo sapiens
2 Dermatan sulfate (DS) accelerates the inhibition of thrombin by heparin cofactor II (HCII). Dermatan Sulfate serpin family D member 1 Homo sapiens
3 Dermatan sulfate (DS) accelerates the inhibition of thrombin by heparin cofactor II (HCII). Dermatan Sulfate serpin family D member 1 Homo sapiens
4 Dermatan sulfate (DS) accelerates the inhibition of thrombin by heparin cofactor II (HCII). Dermatan Sulfate serpin family D member 1 Homo sapiens
5 Dermatan sulfate (DS) accelerates the inhibition of thrombin by heparin cofactor II (HCII). Dermatan Sulfate serpin family D member 1 Homo sapiens
6 DS from porcine intestinal mucosa has a much lower content of this disaccharide but activates HCII with potency similar to that of porcine skin DS. Dermatan Sulfate serpin family D member 1 Homo sapiens
7 Therefore, we sought to characterize oligosaccharides from porcine mucosal DS that interact with HCII. Dermatan Sulfate serpin family D member 1 Homo sapiens
8 These data support the hypothesis that modification of IdoA-->GalNAc4SO3 subunits in the DS polymer by either 2-O-sulfation of IdoA or 6-O-sulfation of GalNAc can generate molecules with HCII-binding sites and anticoagulant activity. Dermatan Sulfate serpin family D member 1 Homo sapiens