Premium
Is N ‐sulfation just a gateway modification during heparan sulfate biosynthesis?
Author(s) -
Raman Karthik,
Nguyen Thao Kim Nu,
Kuberan Balagurunathan
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.09.030
Subject(s) - sulfation , biosynthesis , heparan sulfate , glucosamine , biochemistry , enzyme , biogenesis , chemistry , in vitro , glycosaminoglycan , gene
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.