Journal
FEBS LETTERS
Volume 579, Issue 11, Pages 2359-2363Publisher
WILEY
DOI: 10.1016/j.febslet.2005.03.033
Keywords
dystroglycan; laminin; muscular dystrophy; glycosylation; dystrophic chicken
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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 Gal beta 1-3GalNAc and GalNAc residues are increased while Sia alpha 2-3Gal 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. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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