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Glycoproteomic characterization of recombinant mouse ?-dystroglycan.


ABSTRACT: ?-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 ?-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 ?-DG was expressed and purified from human embryonic kidney 293T cells. ?-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 and 38 glycopeptides were identified which displayed heterogeneous O-glycosylation. These data provide new insights into the complex domain-specific O-glycosylation of ?-DG.

SUBMITTER: Harrison R 

PROVIDER: S-EPMC3311285 | biostudies-literature | 2012 May

REPOSITORIES: biostudies-literature

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Glycoproteomic characterization of recombinant mouse α-dystroglycan.

Harrison Rebecca R   Hitchen Paul G PG   Panico Maria M   Morris Howard R HR   Mekhaiel David D   Pleass Richard J RJ   Dell Anne A   Hewitt Jane E JE   Haslam Stuart M SM  

Glycobiology 20120111 5


α-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 α-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 α-DG was expressed and purified from human embryonic kidney 293T cells. α-DG glycopeptides were characterized by glycoproteomic strategi  ...[more]

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