Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities
J Liu, NW Shworak, P Sinay, JJ Schwartz… - Journal of Biological …, 1999 - ASBMB
The 3-O-sulfation of glucosamine residues is an important modification during the
biosynthesis of heparan sulfate (HS). Our previous studies have led us to purify and
molecularly clone the heparan sulfate d-glucosaminyl 3-O-sulfotransferase (3-OST-1), which
is the key enzyme converting nonanticoagulant heparan sulfate (HS inact) to anticoagulant
heparan sulfate (HS act). In this study, we expressed and characterized the full-length
cDNAs of 3-OST-1 homologous genes, designated as 3-OST-2, 3-OST-3 A, and 3-OST-3 B …
biosynthesis of heparan sulfate (HS). Our previous studies have led us to purify and
molecularly clone the heparan sulfate d-glucosaminyl 3-O-sulfotransferase (3-OST-1), which
is the key enzyme converting nonanticoagulant heparan sulfate (HS inact) to anticoagulant
heparan sulfate (HS act). In this study, we expressed and characterized the full-length
cDNAs of 3-OST-1 homologous genes, designated as 3-OST-2, 3-OST-3 A, and 3-OST-3 B …