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Harrison, Rebecca, Hitchen, Paul G, Panico, Maria, Morris, Howard R, Mekhaiel, David, Pleass, Richard 
ORCID: https://orcid.org/0000-0001-7438-8296, 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.
Abstract
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): | https://doi.org/10.1093/glycob/cws002 |
| Depositing User: | Mary Creegan |
| Date Deposited: | 27 Mar 2013 14:29 |
| Last Modified: | 06 Feb 2018 13:05 |
| URI: | https://archive.lstmed.ac.uk/id/eprint/3232 |
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