Journal article
Aberrant glycosylation of α-dystroglycan causes defective binding of laminin in the muscle of chicken muscular dystrophy
FEBS letters, Vol.579(11), pp.2359-2363
04/25/2005
DOI: 10.1016/j.febslet.2005.03.033
PMID: 15848172
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.
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, JapanMartina Blank - Institute for Physiological Chemistry, University of Mainz, Duesbergweg 6, D-55099 Mainz, GermanyJörn Schröder - Institute for Physiological Chemistry, University of Mainz, Duesbergweg 6, D-55099 Mainz, GermanyHiroshi Manya - Glycobiology Research Group, Tokyo Metropolitan Institute of Gerontology, 35-2 Sakae-chyo, Itabashi-ku, Tokyo 173-0015, JapanTeruo Shimizu - Department of Neurology and Neuroscience, Teikyo University, 2-11-1 Kaga, Itabashi-ku, Tokyo 173-8605, JapanKevin 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, USATamao Endo - Glycobiology Research Group, Tokyo Metropolitan Institute of Gerontology, 35-2 Sakae-chyo, Itabashi-ku, Tokyo 173-0015, JapanMakoto Mizutani - Nippon Institute for Biological Science, 3331-114 kamisasao, kobuchisawa-chyo, Yamanashi prefecture 408-0041, JapanStephan Kröger - Institute for Physiological Chemistry, University of Mainz, Duesbergweg 6, D-55099 Mainz, GermanyKiichiro 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
- Publisher
- Elsevier B.V
- DOI
- 10.1016/j.febslet.2005.03.033
- PMID
- 15848172
- ISSN
- 0014-5793
- eISSN
- 1873-3468
- Language
- English
- Date published
- 04/25/2005
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute
- Record Identifier
- 9984020993502771
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