Heparan Sulfate D-Glucosaminyl 3-O-Sulfotransferase-1, -2, -3, and -4
Heparan sulfate D-glucosaminyl 3-O-sulfotransferase (HS3ST) is a class of sulfotransferase that transfers the sulfate from 3′-phosphoadenosine 5′-phosphosulfate (PAPS) to the 3-OH of the glucosamine residue. HS3ST was originally exclusively designated the key sulfotransferase to synthesize the antithrombin-binding site in heparan sulfate (HS) to confer its anticoagulant activity (Kusche et al. 1990; Shworak et al. 1996). However, recent studies suggest that HS3ST is present in at least five iso- forms (Shworak et al. 1999). Among these isoforms HS3ST-1, HS3ST-2, HS3ST-3A, and HS3ST-3B have been characterized, and the results allow us to distinguish these enzymes by their DNA/amino acid sequence, biochemical, and biological aspects. Although HS3ST isoforms have similar amino acid sequences at the C-terminus, they differ mainly in the following characteristics: (1) gene locations in the human genome; (2) mRNA expression levels in various human tissues; (3) substrate specificity; and (4) biological functions of enzyme-modified HS (Rosenberg et al. 1997).
KeywordsHeparan Sulfate Sulfated Glucosamine Pulmonary Artery Smooth Muscle Cell Glucosamine Residue Iduronic Acid
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