Premium
Aberrant glycosylation of α‐dystroglycan causes defective binding of laminin in the muscle of chicken muscular dystrophy
Author(s) -
Saito Fumiaki,
Blank Martina,
Schröder Jörn,
Manya Hiroshi,
Shimizu Teruo,
Campbell Kevin P.,
Endo Tamao,
Mizutani Makoto,
Kröger Stephan,
Matsumura Kiichiro
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.03.033
Subject(s) - dystroglycan , muscular dystrophy , laminin , itga7 , extracellular matrix , glycoprotein , dystrophin , skeletal muscle , congenital muscular dystrophy , glycosylation , duchenne muscular dystrophy , biology , microbiology and biotechnology , alpha (finance) , genetics , endocrinology , medicine , construct validity , nursing , patient satisfaction
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.