title: Mouse adhalin: primary structure and expression during late stages of muscle differentiation in vitro.
abstract: Adhalin, or alpha-sarcoglycan, is a 50-kDa glycoprotein that was originally characterized as a muscle membrane protein. The importance of adhalin is suggested by the diseases associated with its absence, notably the limb-girdle muscular dystrophies. However, the function of adhalin is unknown. To analyze the biological roles of adhalin, we cloned the mouse adhalin cDNA, raised peptide-specific antibodies to its cytoplasmic domain, and examined its expression and localization in vivo and in vitro. The mouse adhalin sequence was 80% identical to that of human, rabbit, and hamster. Adhalin was specifically expressed in striated muscle cells and their immediate precursors, and absent in many other cell types. Adhalin expression in embryonic mouse muscle was coincident with primary myogenesis. Its expression was found to be up-regulated at mRNA and protein levels during myogenic differentiation in vitro. The proper localization of adhalin to the muscle cell membrane was observed only in late stages of myotube maturation, coincident with the re-distribution of caveolin-3 and dystrophin. These data suggest that adhalin is highly specific for striated muscle and that it is linked with the formation of a fully functional muscle fiber.
authors.affiliation: Department of Developmental Biology, The Wenner-Gren Institute, Stockholm University, Sweden.
authors.forename: L
authors.initials: L
authors.lastname: Liu
authors.forename: P H
authors.initials: PH
authors.lastname: Vachon
authors.forename: W
authors.initials: W
authors.lastname: Kuang
authors.forename: H
authors.initials: H
authors.lastname: Xu
authors.forename: U M
authors.initials: UM
authors.lastname: Wewer
authors.forename: P
authors.initials: P
authors.lastname: Kylsten
authors.forename: E
authors.initials: E
authors.lastname: Engvall
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D051244:Caveolin 3; D022461:Caveolins; D002454:Cell Differentiation; D003001:Cloning, Molecular; D003598:Cytoskeletal Proteins / Q000737:chemistry* / Q000235:genetics*; D018076:DNA, Complementary / Q000737:chemistry; D005455:Fluorescent Antibody Technique; D018507:Gene Expression Regulation, Developmental; D008562:Membrane Glycoproteins / Q000737:chemistry* / Q000235:genetics*; D008565:Membrane Proteins / Q000032:analysis; D051379:Mice; D008815:Mice, Inbred Strains; D008969:Molecular Sequence Data; D009124:Muscle Proteins / Q000737:chemistry / Q000378:metabolism; D018482:Muscle, Skeletal / Q000737:chemistry* / Q000166:cytology*; D009136:Muscular Dystrophies / Q000235:genetics; D012333:RNA, Messenger / Q000032:analysis; D049031:Sarcoglycans; D017386:Sequence Homology, Amino Acid; D014407:Tumor Cells, Cultured; D015854:Up-Regulation
chemical_list: C495548:Cav3 protein, mouse; D051244:Caveolin 3; D022461:Caveolins; D003598:Cytoskeletal Proteins; D018076:DNA, Complementary; D008562:Membrane Glycoproteins; D008565:Membrane Proteins; D009124:Muscle Proteins; D012333:RNA, Messenger; D049031:Sarcoglycans