The interaction of glycosaminoglycans with heparin cofactor II.

Abstract

The binding sites for dermatan sulfate and heparin in HCII overlap but are not identical. This may explain the observation that HCII binds nonspecifically to heparin oligosaccharides, but preferentially binds to a minor hexasaccharide isolated from dermatan sulfate. The tissue distribution of dermatan sulfate molecules containing the high-affinity HCII binding site may regulate HCII activity in vivo. Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic region of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction.