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Characterization of site-specific O-glycan structures within the mucin-like domain of alpha-dystroglycan from human skeletal muscle.

Journal article
Authors Johanna Nilsson
Jonas Nilsson
Göran Larson
Ammi Grahn
Published in Glycobiology
Volume 20
Issue 9
Pages 1160-9
ISSN 1460-2423
Publication year 2010
Published at Institute of Biomedicine, Department of Pathology
Institute of Biomedicine, Department of Clinical Chemistry and Transfusion Medicine
Pages 1160-9
Language en
Links dx.doi.org/10.1093/glycob/cwq082
Keywords Amino Acid Sequence, Carbohydrate Sequence, Catalytic Domain, Dystroglycans, analysis, chemistry, metabolism, Glycosylation, Humans, Molecular Sequence Data, Mucins, chemistry, Muscle, Skeletal, chemistry, metabolism, N-Acetylneuraminic Acid, chemistry, metabolism, Peptide Mapping, Polysaccharides, chemistry, metabolism, Protein Processing, Post-Translational, Protein Structure, Tertiary, physiology, Structure-Activity Relationship, Substrate Specificity
Subject categories Neurochemistry, Clinical chemistry, Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)

Abstract

The glycosylation of the extracellular protein alpha-dystroglycan is important for its ligand-binding activity, and altered or blocked glycosylation is associated with several forms of congenital muscular dystrophies. By immunoprecipitation and sialic acid capture-and-release enrichment strategies, we isolated tryptic glycopeptides of alpha-dystroglycan from human skeletal muscle. Nano-liquid chromatography tandem mass spectrometry was used to identify both glycopeptides and peptides corresponding to the mucin-like and C-terminal domain of alpha-dystroglycan. The O-glycans found had either Hex-O-Thr or HexNAc-O-Ser/Thr anchored structures, which were often elongated and frequently, but not always, terminated with sialic acid. The HexNAc-O-Ser/Thr, but not Hex-O-Thr glycopeptides, displayed heterogeneity regarding glycan core structures and level of glycosylation site occupancy. We demonstrate for the first time glycan attachment sites of the NeuAcHexHexNAcHex-O structure corresponding to the anticipated Neu5Acalpha3Galbeta4GlcNAcbeta2Man-O-glycan (sLacNAc-Man), within the mucin-like domain of human alpha-dystroglycan from human skeletal muscle. Twenty-five glycopeptides were characterized from human alpha-dystroglycan, which provide insight to the complex in vivo O-glycosylation of alpha-dystroglycan.

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