title: Is N-sulfation just a gateway modification during heparan sulfate biosynthesis?
abstract: Several biologically important growth factor-heparan sulfate (HS) interactions are regulated by HS sulfation patterns. However, the biogenesis of these combinatorial sulfation patterns is largely unknown. N-Deacetylase/N-sulfotrasferase (NDST) converts N-acetyl-d-glucosamine residues to N-sulfo-d-glucosamine residues. This enzyme is suggested to be a gateway enzyme because N-sulfation dictates the final HS sulfation pattern. It is known that O-sulfation blocks C5-epimerase, which acts immediately after NDST action. However, it is still unknown whether O-sulfation inhibits NDST action in a similar manner. In this article we radically change conventional assumptions regarding HS biosynthesis by providing in vitro evidence that N-sulfation is not necessarily just a gateway modification during HS biosynthesis.
authors: Department of Bioengineering, University of Utah, Salt Lake City, UT 84112, USA.
authors: Karthik
authors: K
authors: Raman
authors: Thao Kim Nu
authors: TK
authors: Nguyen
authors: Balagurunathan
authors: B
authors: Kuberan
mesh_terms: D000107:Acetylation; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D005417:Flavobacterium / Q000201:enzymology; D006497:Heparan Sulfate / Q000096:biosynthesis*; D013431:Sulfates / Q000378:metabolism*; D015238:Sulfotransferases / Q000737:chemistry / Q000378:metabolism
chemical_list: D006497:Heparan Sulfate; D013431:Sulfates; D015238:Sulfotransferases; C021350:heparitin sulfotransferase