Aberrant glycosylation of α-dystroglycan causes defective binding of laminin in the muscle of chicken muscular dystrophy

Fumiaki Saito; Martina Blank; Jörn Schröder; Hiroshi Manya; Teruo Shimizu; Kevin P Campbell; Tamao Endo; Makoto Mizutani; Stephan Kröger; Kiichiro Matsumura

doi:10.1016/j.febslet.2005.03.033

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Aberrant glycosylation of α-dystroglycan causes defective binding of laminin in the muscle of chicken muscular dystrophy

Journal article

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Aberrant glycosylation of α-dystroglycan causes defective binding of laminin in the muscle of chicken muscular dystrophy

Fumiaki Saito, Martina Blank, Jörn Schröder, Hiroshi Manya, Teruo Shimizu, Kevin P Campbell, Tamao Endo, Makoto Mizutani, Stephan Kröger and Kiichiro Matsumura

FEBS letters, Vol.579(11), pp.2359-2363

04/25/2005

DOI: 10.1016/j.febslet.2005.03.033

PMID: 15848172

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Abstract

Dystroglycan is a central component of dystrophin–glycoprotein complex that links extracellular matrix and cytoskeleton in skeletal muscle. Although dystrophic chicken is well established as an animal model of human muscular dystrophy, the pathomechanism leading to muscular degeneration remains unknown. We show here that glycosylation and laminin-binding activity of α-dystroglycan (α-DG) are defective in dystrophic chicken. Extensive glycan structural analysis reveals that Galβ1-3GalNAc and GalNAc residues are increased while Siaα2-3Gal structure is reduced in α-DG of dystrophic chicken. These results implicate aberrant glycosylation of α-DG in the pathogenesis of muscular degeneration in this model animal of muscular dystrophy.

Muscular Dystrophy

Dystroglycan

Glycosylation

Laminin

Dystrophic chicken

Details

Title: Subtitle: Aberrant glycosylation of α-dystroglycan causes defective binding of laminin in the muscle of chicken muscular dystrophy
Creators: Fumiaki Saito - Department of Neurology and Neuroscience, Teikyo University, 2-11-1 Kaga, Itabashi-ku, Tokyo 173-8605, Japan
Martina Blank - Institute for Physiological Chemistry, University of Mainz, Duesbergweg 6, D-55099 Mainz, Germany
Jörn Schröder - Institute for Physiological Chemistry, University of Mainz, Duesbergweg 6, D-55099 Mainz, Germany
Hiroshi Manya - Glycobiology Research Group, Tokyo Metropolitan Institute of Gerontology, 35-2 Sakae-chyo, Itabashi-ku, Tokyo 173-0015, Japan
Teruo Shimizu - Department of Neurology and Neuroscience, Teikyo University, 2-11-1 Kaga, Itabashi-ku, Tokyo 173-8605, Japan
Kevin P Campbell - Howard Hughes Medical Institute, Department of Physiology and Biophysics and Department of Neurology, The University of Iowa, Roy J. and Lucille A. Carver College of Medicine, 400 Eckstein medical research building, Iowa City, IA 52242-1101, USA
Tamao Endo - Glycobiology Research Group, Tokyo Metropolitan Institute of Gerontology, 35-2 Sakae-chyo, Itabashi-ku, Tokyo 173-0015, Japan
Makoto Mizutani - Nippon Institute for Biological Science, 3331-114 kamisasao, kobuchisawa-chyo, Yamanashi prefecture 408-0041, Japan
Stephan Kröger - Institute for Physiological Chemistry, University of Mainz, Duesbergweg 6, D-55099 Mainz, Germany
Kiichiro Matsumura - Department of Neurology and Neuroscience, Teikyo University, 2-11-1 Kaga, Itabashi-ku, Tokyo 173-8605, Japan
Resource Type: Journal article
Publication Details: FEBS letters, Vol.579(11), pp.2359-2363
DOI: 10.1016/j.febslet.2005.03.033
PMID: 15848172
NLM abbreviation: FEBS Lett
ISSN: 0014-5793
eISSN: 1873-3468
Publisher: Elsevier B.V
Language: English
Date published: 04/25/2005
Academic Unit: Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute
Record Identifier: 9984020993502771

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