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Glycoproteomic characterization of recombinant mouse α-dystroglycan.

Harrison, Rebecca, Hitchen, Paul G, Panico, Maria, Morris, Howard R, Mekhaiel, David, Pleass, Richard ORCID:, Dell, Anne, Hewitt, Jane E and Haslam, Stuart M (2012) 'Glycoproteomic characterization of recombinant mouse α-dystroglycan.'. Glycobiology, Vol 22, Issue 5, pp. 662-675.

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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 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 α-DG.

Item Type: Article
Subjects: QU Biochemistry > Genetics > QU 470 Genetic structures
QU Biochemistry > Genetics > QU 500 Genetic phenomena
QU Biochemistry > Proteins. Amino Acids. Peptides > QU 58.5 DNA.
WE Musculoskeletal System > WE 140 Diseases (General)
Faculty: Department: Groups (2002 - 2012) > Molecular & Biochemical Parasitology Group
Digital Object Identifer (DOI):
Depositing User: Mary Creegan
Date Deposited: 27 Mar 2013 14:29
Last Modified: 06 Feb 2018 13:05


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