O-Mannose and O-N-acetyl galactosamine glycosylation of mammalian α-dystroglycan is conserved in a region-specific manner.
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.
Department of Clinical Chemistry and Transfusion Medicine, Institute of Biomedicine, Sahlgrenska Academy at the University of Gothenburg, Sahlgrenska University Hospital, Göteborg, Sweden.
Alejandro
A
Gomez Toledo
Madalina
M
Raducu
Jesús
J
Cruces
Jonas
J
Nilsson
Adnan
A
Halim
Göran
G
Larson
Ulla
U
Rüetschi
Ammi
A
Grahn
D000116:Acetylgalactosamine / Q000378:metabolism*; D000818:Animals; D049030:Dystroglycans / Q000737:chemistry / Q000378:metabolism*; D006031:Glycosylation; D006801:Humans; D008358:Mannose / Q000378:metabolism*; D051379:Mice; D018482:Muscle, Skeletal / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011817:Rabbits; D013045:Species Specificity
D049030:Dystroglycans; D000116:Acetylgalactosamine; D008358:Mannose