Site mapping and characterization of O-glycan structures on alpha-dystroglycan isolated from rabbit skeletal muscle.

ABSTRACT: The main extracellular matrix binding component of the dystrophin-glycoprotein complex, alpha-dystroglycan (alpha-DG), which was originally isolated from rabbit skeletal muscle, is an extensively O-glycosylated protein. Previous studies have shown alpha-DG to be modified by both O-GalNAc- and O-mannose-initiated glycan structures. O-Mannosylation, which accounts for up to 30% of the reported O-linked structures in certain tissues, has been rarely observed on mammalian proteins. Mutations in multiple genes encoding defined or putative glycosyltransferases involved in O-mannosylation are causal for various forms of congenital muscular dystrophy. Here, we explore the glycosylation of purified rabbit skeletal muscle alpha-DG in detail. Using tandem mass spectrometry approaches, we identify 4 O

SUBMITTER: Stalnaker SH 

PROVIDER: S-EPMC2915724 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature