期刊
GLYCOBIOLOGY
卷 22, 期 5, 页码 662-675出版社
OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cws002
关键词
alpha-dystroglycan; glycoproteomics; mass spectrometry; O-GalNAc; O-mannose
资金
- Biotechnology and Biological Research Council (BBSRC) [SF19107, B19088, BBF0083091]
- MRC
- Wellcome Trust [082915/B/07/Z]
- Biotechnology and Biological Sciences Research Council [SF19107, B19088] Funding Source: researchfish
- Medical Research Council [G0300145] Funding Source: researchfish
- MRC [G0300145] Funding Source: UKRI
alpha-Dystroglycan (DG) is a key component of the dystrophin-glycoprotein complex. Aberrant glycosylation of the protein has been linked to various forms of congenital muscular dystrophy. Unusually alpha-DG has previously been demonstrated to be modified with both O-N-acetylgalactosamine and O-mannose initiated glycans. In the present study, Fc-tagged recombinant mouse alpha-DG was expressed and purified from human embryonic kidney 293T cells. alpha-DG glycopeptides were characterized by glycoproteomic strategies using both nano-liquid chromatography matrix-assisted laser desorption ionization and electrospray tandem mass spectrometry. A total of 14 different peptide sequences glycosylation. These data provide new insights into the complex domain-specific and 38 glycopeptides were identified which displayed heterogeneous O-O-glycosylation of alpha-DG.
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