Abstract
Interaction of bFGF with heparan sulfate (HS) is prerequisite for the binding of bFGF to its high-affinity receptor and for its mitogenic activity. HS possesses a complex polymeric structure in which the majority of N-sulfated glucosamine and various O-sulfated residues are clustered in a series of short domains separated by relatively long oligosaccharide sequences with low sulfate content. The formation of highly sulfated clusters in HS has been shown to be regulated by the activity of HS-N-deacetylase/N-sulfotransferase (HS-NdAc/NST), which catalyzes both N-deacetylation and N-sulfation reactions of glucosamine residues in HS. Recent studies showed that bFGF interacts with HS through large highly sulfated clusters that are enriched in 2-O-sulfated iduronic acid-N-sulfated glucosamine disaccharide sequence.
