title: Distinct alpha 7A beta 1 and alpha 7B beta 1 integrin expression patterns during mouse development: alpha 7A is restricted to skeletal muscle but alpha 7B is expressed in striated muscle, vasculature, and nervous system.
abstract: The laminin binding alpha 7 beta 1 integrin has been described as a major integrin in skeletal muscle. The RNA coding for the cytoplasmic domain of alpha 7 integrin undergoes alternative splicing to generate two major forms, denoted alpha 7A and alpha 7B. In the current paper, we have examined the developmental expression patterns of the alpha 7A and alpha 7B splice variants in the mouse. The alpha 7 integrin expression is compared to that of the nonintegrin laminin receptor dystroglycan and to that of laminin-alpha 1 and laminin-alpha 2 chains. Alpha 7A integrin was found by in situ hybridization to be specific to skeletal muscle. Antibodies specific for alpha 7B integrin and in situ hybridization revealed the presence of alpha 7 mRNA and alpha 7B protein in the E10 myotome and later in primary and secondary myotubes. In the heart, alpha 7B integrin was not detectable in the endocardium or myocardium during embryonic and fetal heart development. Northern blot analysis and immunohistochemistry revealed a postnatal induction of alpha 7B in the myocardium. In addition to striated muscle, alpha 7B integrin was localized to previously unreported nonmuscle locations such as a subset of vascular endothelia and restricted sites in the nervous system. Comparison of the alpha 7 integrin expression pattern with that of different laminin isoforms and dystroglycan revealed a coordinated temporal expression of dystroglycan, alpha 7 integrin, and laminin-alpha 2, but not laminin-alpha 1, in the forming skeletal muscle. We conclude that the alpha 7A and alpha 7B integrin variants are expressed in a developmentally regulated, tissue-specific pattern suggesting different functions for the two splice forms.
authors.affiliation: Department of Animal Physiology, Uppsala University, Sweden.
authors.forename: T
authors.initials: T
authors.lastname: Velling
authors.forename: G
authors.initials: G
authors.lastname: Collo
authors.forename: L
authors.initials: L
authors.lastname: Sorokin
authors.forename: M
authors.initials: M
authors.lastname: Durbeej
authors.forename: H
authors.initials: H
authors.lastname: Zhang
authors.forename: D
authors.initials: D
authors.lastname: Gullberg
mesh_terms: D000818:Animals; D015703:Antigens, CD / Q000378:metabolism*; D002319:Cardiovascular System / Q000196:embryology* / Q000378:metabolism*; D002478:Cells, Cultured; D003598:Cytoskeletal Proteins / Q000378:metabolism; D049030:Dystroglycans; D004622:Embryo, Mammalian / Q000378:metabolism; D004727:Endothelium / Q000378:metabolism; D004848:Epithelium / Q000378:metabolism; D005727:Ganglia, Spinal / Q000378:metabolism; D007150:Immunohistochemistry; D017403:In Situ Hybridization; D039001:Integrin alpha Chains; D016023:Integrins / Q000378:metabolism; D007797:Laminin / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000378:metabolism; D051379:Mice; D008815:Mice, Inbred Strains; D018482:Muscle, Skeletal / Q000196:embryology* / Q000378:metabolism*; D009420:Nervous System / Q000196:embryology* / Q000378:metabolism*; D009830:Olfactory Bulb / Q000378:metabolism; D012333:RNA, Messenger / Q000032:analysis; D017474:Receptors, Laminin / Q000378:metabolism; D014018:Tissue Distribution; D012668:Trigeminal Ganglion / Q000378:metabolism
chemical_list: D015703:Antigens, CD; D003598:Cytoskeletal Proteins; C483081:DAG1 protein, human; D039001:Integrin alpha Chains; D016023:Integrins; D007797:Laminin; D008562:Membrane Glycoproteins; D012333:RNA, Messenger; D017474:Receptors, Laminin; C085725:integrin alpha7; C102645:laminin alpha 2; D049030:Dystroglycans