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

• 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.

Ämnesord

NATURVETENSKAP  -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)

NATURAL SCIENCES  -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)

Nyckelord

alpha-dystroglycan

glycoproteomics

mammalian

mass spectrometry

O-glycosylation

girdle muscular-dystrophy

skeletal-muscle

laminin-binding

glycan

structures

peripheral-nerve

protein gene

fkrp gene

mannosylation

mutations

phenotype

Publikations- och innehållstyp

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