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

Journal article
Authors Alejandro Gomez Toledo
M. Raducu
J. Cruces
Jonas Nilsson
Adnan Halim
Göran Larson
Ulla Rüetschi
Ammi Grahn
Published in Glycobiology
Volume 22
Issue 11
Pages 1413-1423
ISSN 0959-6658
Publication year 2012
Published at Institute of Biomedicine, Department of Clinical Chemistry and Transfusion Medicine
Pages 1413-1423
Language en
Keywords 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
Subject categories Biochemistry


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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