Aberrant glycosylation of alpha-dystroglycan causes defective binding of laminin in the muscle of chicken muscular dystrophy.
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 alpha-dystroglycan (alpha-DG) are defective in dystrophic chicken. Extensive glycan structural analysis reveals that Galbeta1-3GalNAc and GalNAc residues are increased while Siaalpha2-3Gal structure is reduced in alpha-DG of dystrophic chicken. These results implicate aberrant glycosylation of alpha-DG in the pathogenesis of muscular degeneration in this model animal of muscular dystrophy.
Saito
Fumiaki
F
Department of Neurology and Neuroscience, Teikyo University, Itabashi-ku, Tokyo, Japan. f-saito@med.teikyo-u.ac.jp
Blank
Martina
M
Schröder
Jörn
J
Manya
Hiroshi
H
Shimizu
Teruo
T
Campbell
Kevin P
KP
Endo
Tamao
T
Mizutani
Makoto
M
Kröger
Stephan
S
Matsumura
Kiichiro
K
D000818:Animals; D002645:Chickens; D002846:Chromatography, Affinity; D004195:Disease Models, Animal; D049030:Dystroglycans / Q000737:chemistry / Q000378:metabolism*; D006031:Glycosylation; D007797:Laminin / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000276:immunology / Q000378:metabolism* / Q000473:pathology; D009137:Muscular Dystrophy, Animal / Q000276:immunology / Q000378:metabolism* / Q000473:pathology; D037121:Plant Lectins / Q000378:metabolism; D011485:Protein Binding
D007797:Laminin; D037121:Plant Lectins; D049030:Dystroglycans