Site-specific identification of heparan and chondroitin sulfate glycosaminoglycans in hybrid proteoglycans.

ABSTRACT: Heparan sulfate (HS) and chondroitin sulfate (CS) are complex polysaccharides that regulate important biological pathways in virtually all metazoan organisms. The polysaccharides often display opposite effects on cell functions with HS and CS structural motifs presenting unique binding sites for specific ligands. Still, the mechanisms by which glycan biosynthesis generates complex HS and CS polysaccharides required for the regulation of mammalian physiology remain elusive. Here we present a glycoproteomic approach that identifies and differentiates between HS and CS attachment sites and provides identity to the core proteins. Glycopeptides were prepared from perlecan, a complex proteoglycan known to be substituted with both HS and CS chains, further digested with heparinase or chondroitina

SUBMITTER: Noborn F 

PROVIDER: S-EPMC5046109 | biostudies-literature | 2016 Oct

REPOSITORIES: biostudies-literature