title: Protein glycosylation in disease: new insights into the congenital muscular dystrophies.
abstract: Glycosylation is the most frequent modification of proteins and is important for many ligand-receptor interactions. Recently, defects in protein glycosylation have been linked to several forms of congenital muscular dystrophy that are frequently associated with brain abnormalities. Muscle-eye-brain disease and Walker-Warburg syndrome are caused by mutations in enzymes involved in O-mannosylation, whereas Fukuyama congenital muscular dystrophy and congenital muscular dystrophy type 1C are caused by mutations in genes that encode putative glycosyltransferases. The common factor in these disorders is defective processing and maturation of a protein called alpha-dystroglycan. This is thought to disrupt the link between alpha-dystroglycan and components of the extracellular matrix, and result in muscle disease and, in many cases, a neuronal-migration disorder.
authors.affiliation: Stem Cell Laboratory, National Blood Service, John Radcliffe Hospital, Headington, Oxford OX3 9DU, UK.
authors.forename: Enca
authors.initials: E
authors.lastname: Martin-Rendon
authors.forename: Derek J
authors.initials: DJ
authors.lastname: Blake
mesh_terms: D000818:Animals; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000378:metabolism; D049030:Dystroglycans; D015316:Genetic Therapy; D006031:Glycosylation; D016695:Glycosyltransferases / Q000235:genetics; D006801:Humans; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism; D009136:Muscular Dystrophies / Q000151:congenital* / Q000378:metabolism* / Q000628:therapy; D009154:Mutation
chemical_list: D003598:Cytoskeletal Proteins; C483081:DAG1 protein, human; D008562:Membrane Glycoproteins; D049030:Dystroglycans; D016695:Glycosyltransferases