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

Glycobiology. 2012 Nov;22(11):1413-23. doi: 10.1093/glycob/cws109. Epub 2012 Jul 9.


Defects 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylgalactosamine / metabolism*
  • Animals
  • Dystroglycans / chemistry
  • Dystroglycans / metabolism*
  • Glycosylation
  • Humans
  • Mannose / metabolism*
  • Mice
  • Muscle, Skeletal / metabolism
  • Protein Structure, Tertiary
  • Rabbits
  • Species Specificity


  • Dystroglycans
  • Acetylgalactosamine
  • Mannose