Anticoagulant heparan sulfate: structural specificity and biosynthesis.

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Liu J, Pedersen LC

Anticoagulant heparan sulfate: structural specificity and biosynthesis.

Appl Microbiol Biotechnol. 2007 Feb;74(2):263-72. doi: 10.1007/s00253-006-0722-x. Epub 2006 Nov 28.

PubMed ID

17131147 [ View in PubMed

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Abstract

Heparan sulfate (HS) is present on the surface of endothelial and surrounding tissues in large quantities. It plays important roles in regulating numerous functions of the blood vessel wall, including blood coagulation, inflammation response, and cell differentiation. HS is a highly sulfated polysaccharide containing glucosamine and glucuronic/iduronic acid repeating disaccharide units. The unique sulfated saccharide sequences of HS determine its specific functions. Heparin, an analog of HS, is the most commonly used anticoagulant drug. Because of its wide range of biological functions, HS has become an interesting molecule to biochemists, medicinal chemists, and developmental biologists. In this review, we summarize recent progress toward understanding the interaction between HS and blood-coagulating factors, the biosynthesis of anticoagulant HS and the mechanism of action of HS biosynthetic enzymes. Furthermore, knowledge of the biosynthesis of HS facilitates the development of novel enzymatic approaches to synthesize HS from bacterial capsular polysaccharides and to produce polysaccharide end products with high specificity for the biological target. These advancements provide the foundation for the development of polysaccharide-based therapeutic agents.

DrugBank Data that Cites this Article

Drugs

Danaparoid

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Danaparoid	Antithrombin-III	Protein	Humans	Yes	Positive allosteric modulator	Details