title: The alpha7beta1 integrin mediates adhesion and migration of skeletal myoblasts on laminin.
abstract: Many aspects of myogenesis are believed to be regulated by myoblast interactions with specific components of the extracellular matrix. For example, laminin has been found to promote adhesion, migration, and proliferation of mammalian myoblasts. Based on affinity chromatography, the alpha7beta1 integrin has been presumed to be the major receptor mediating myoblast interactions with laminin. We have prepared a monoclonal antibody, O26, that specifically reacts with both the X1 and the X2 extracellular splice variants of the alpha7 integrin chain. This antibody completely and selectively blocks adhesion and migration of rat L8E63 myoblasts on laminin-1, but not on fibronectin. In contrast, a polyclonal antibody to the fibronectin receptor, alpha5beta1 integrin, blocks myoblast adhesion on fibronectin, but not on laminin-1. The alpha7beta1 integrin also binds to a mixture of laminin-2 and laminin-4, the major laminin isoforms in developing and adult skeletal muscle, but O26 is a much less potent inhibitor of myoblast adhesion on the laminin-2/4 mixture than on laminin-1. Based on affinity chromatography, we suggest that this may be due to higher affinity binding of alpha7X1 to laminin-2/4 than to laminin-1.
authors.affiliation: Center for Neurobiology and Psychiatry, University of California at San Francisco, San Francisco, California 94143-0984, USA.
authors.forename: S
authors.initials: S
authors.lastname: Crawley
authors.forename: E M
authors.initials: EM
authors.lastname: Farrell
authors.forename: W
authors.initials: W
authors.lastname: Wang
authors.forename: M
authors.initials: M
authors.lastname: Gu
authors.forename: H Y
authors.initials: HY
authors.lastname: Huang
authors.forename: V
authors.initials: V
authors.lastname: Huynh
authors.forename: B L
authors.initials: BL
authors.lastname: Hodges
authors.forename: D N
authors.initials: DN
authors.lastname: Cooper
authors.forename: S J
authors.initials: SJ
authors.lastname: Kaufman
mesh_terms: D017398:Alternative Splicing; D000818:Animals; D000911:Antibodies, Monoclonal / Q000494:pharmacology; D000918:Antibody Specificity; D016466:CHO Cells; D002448:Cell Adhesion; D002460:Cell Line; D002465:Cell Movement; D006224:Cricetinae; D005353:Fibronectins / Q000378:metabolism; D014644:Genetic Variation; D015151:Immunoblotting; D016023:Integrins / Q000096:biosynthesis / Q000276:immunology / Q000502:physiology*; D007700:Kinetics; D007797:Laminin / Q000378:metabolism*; D051379:Mice; D018482:Muscle, Skeletal / Q000166:cytology / Q000502:physiology*; D051381:Rats; D017469:Receptors, Fibronectin / Q000276:immunology / Q000502:physiology; D017474:Receptors, Laminin / Q000502:physiology*; D011994:Recombinant Proteins / Q000096:biosynthesis; D014162:Transfection
chemical_list: D000911:Antibodies, Monoclonal; D005353:Fibronectins; D016023:Integrins; D007797:Laminin; D017469:Receptors, Fibronectin; D017474:Receptors, Laminin; D011994:Recombinant Proteins; C082908:integrin alpha7beta1