Title : Characterization of site-specific O-glycan structures within the mucin-like
domain of alpha-dystroglycan from human skeletal muscle
Abstract :
- The glycosylation of the extracellular protein alpha-dystroglycan is important for its ligand-binding activity, and altered or blocked glycosylation is associated with several forms of congenital muscular dystrophies
- By immunoprecipitation and sialic acid capture-and-release enrichment strategies, we isolated tryptic glycopeptides of alpha-dystroglycan from human skeletal muscle
- Nano-liquid chromatography tandem mass spectrometry was used to identify both glycopeptides and peptides corresponding to the mucin-like and C-terminal domain of alpha-dystroglycan
- The O-glycans found had either Hex-O- Thr or HexNAc-O-Ser/Thr anchored structures, which were often elongated and frequently, but not always, terminated with sialic acid
- The HexNAc-O-Ser/Thr, but not Hex-O- Thr glycopeptides , displayed heterogeneity regarding glycan core structures and level of glycosylation site occupancy
- We demonstrate for the first time glycan attachment sites of the NeuAcHexHexNAcHex-O structure corresponding to the anticipated Neu5Acalpha3Galbeta4GlcNAcbeta2Man-O-glycan (sLacNAc-Man), within the mucin-like domain of human alpha-dystroglycan from human skeletal muscle
- Twenty-five glycopeptides were characterized from human alpha-dystroglycan, which provide insight to the complex in vivo O-glycosylation of alpha-dystroglycan
Output (sent_index, trigger,
protein,
sugar,
site):
- 1. glycosylation, , -, the extracellular protein alpha-dystroglycan, -
- 2. glycopeptides, , -, alpha-dystroglycan, glycopeptides
- 3. glycopeptides, , -, -, glycopeptides
- 5. glycopeptides, , -, -, Thr glycopeptides
- 5. glycosylation, , -, -, site
- 7. O-glycosylation, , -, alpha-dystroglycan, -
- 7. glycopeptides, , -, -, glycopeptides
Output(Part-Of) (sent_index,
protein,
site):
- 5. Hex, Thr glycopeptides
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):