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O-mannose and O-N-acetyl galactosamine glycosylation of mammalian α-dystroglycan is conserved in a region-specific manner

AuthorsGomez Toledo, Alejandro; Raducu, Madalina; Cruces, Jesús
Issue Date2012
PublisherOxford University Press
CitationGlycobiology 22(11): 1413-1423 (2012)
AbstractDefects in the O-linked glycosylation of the peripheral membrane protein α-dystroglycan (α-DG) are the main cause of several forms of congenital muscular dystrophies and thus the characterization of the glycosylation of α-DG is of great medical importance. A detailed investigation of the glycosylation pattern of the native α-DG protein is essential for the understanding of the biological processes related to human disease in which the protein is involved. To date, several studies have reported novel O-glycans and attachment sites on the mucin-like domain of mammalian α-DG with both similar and contradicting glycosylation patterns, indicating the species-specific O-glycosylation of mammalian α-DG. By applying a standardized purification scheme and subsequent glycoproteomic analysis of native α-DG from rabbit and human skeletal muscle biopsies and from cultured mouse C2C12 myotubes, we show that the O-glycosylation patterns of the mucin-like domain of native α-DG are conserved among mammalians in a region-specific manner. © 2012 The Author.
Identifiersdoi: 10.1093/glycob/cws109
issn: 0959-6658
e-issn: 1460-2423
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