6533b826fe1ef96bd128535c

RESEARCH PRODUCT

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

Kiichiro MatsumuraFumiaki SaitoStephan KrögerMartina BlankTeruo ShimizuJörn E. SchröderTamao EndoMakoto MizutaniKevin P. CampbellHiroshi Manya

subject

musculoskeletal diseasesanimal structuresGlycosylationGlycosylationBiophysicsBiochemistryChromatography AffinityExtracellular matrixchemistry.chemical_compoundStructural BiologyLamininGeneticsDystroglycanmedicineAnimalsDystroglycanMuscular dystrophyDystrophic chickenDystroglycansMuscle SkeletalMolecular BiologybiologySkeletal muscleCell BiologyMuscular Dystrophy AnimalMuscular dystrophymedicine.diseaseMolecular biologycarbohydrates (lipids)Disease Models Animalmedicine.anatomical_structurechemistrybiology.proteinPikachurinLamininPlant LectinsITGA7ChickensProtein Binding

description

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.

yearjournalcountryeditionlanguage
2005-02-17FEBS letters
10.1016/j.febslet.2005.03.033https://pubmed.ncbi.nlm.nih.gov/15848172