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  • Toledo, Alejandro Gomez, et al. (author)
  • O-Mannose and O-N-acetyl galactosamine glycosylation of mammalian alpha-dystroglycan is conserved in a region-specific manner
  • 2012
  • In: Glycobiology. - : Oxford University Press (OUP). - 0959-6658 .- 1460-2423. ; 22:11, s. 1413-1423
  • Journal article (peer-reviewed)abstract
    • Defects in the O-linked glycosylation of the peripheral membrane protein alpha-dystroglycan (alpha-DG) are the main cause of several forms of congenital muscular dystrophies and thus the characterization of the glycosylation of alpha-DG is of great medical importance. A detailed investigation of the glycosylation pattern of the native alpha-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 alpha-DG with both similar and contradicting glycosylation patterns, indicating the species-specific O-glycosylation of mammalian alpha-DG. By applying a standardized purification scheme and subsequent glycoproteomic analysis of native alpha-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 alpha-DG are conserved among mammalians in a region-specific manner.
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