title: Calponin and SM 22 as differentiation markers of smooth muscle: spatiotemporal distribution during avian embryonic development.
abstract: Calponin and SM 22 are two proteins related in sequence that are particularly abundant in smooth muscle cells. Here, the distribution patterns of calponin and SM 22 were compared with that of other smooth muscle contractile and cytoskeletal components in the avian embryo using immunofluorescence microscopy and immunoblotting. Like myosin-light-chain kinase and heavy caldesmon, both calponin and SM 22 were more or less exclusively found in smooth muscle cells, during embryonic development and in the adult. Labelling of other cell types including striated muscle was not observed. In contrast, tropomyosin, smooth muscle alpha-actin, filamin and desmin could also be detected in many other cell types in addition to smooth muscles, at least during part of embryonic life. Calponin and SM 22 appeared almost synchronously during the differentiation of all smooth muscle cell populations, though with a slight time difference in the case of the aorta. The appearance of calponin, SM 22 and heavy caldesmon was generally delayed in relation to desmin, tropomyosin, smooth muscle alpha-actin, myosin-light-chain kinase and filamin and a marked increase in abundance of these proteins was observed in the late embryo and in the adult. From these observations we can conclude that both calponin and SM 22 belong to a group of late differentiation determinants in smooth muscle and may constitute convenient and reliable markers to follow the differentiation of most, if not all, smooth muscle cell populations.
authors.affiliation: Laboratoire de Biologie Cellulaire du Developpement, Institut Jacques Monod, Universite Paris 7, France.
authors.forename: J L
authors.initials: JL
authors.lastname: Duband
authors.forename: M
authors.initials: M
authors.lastname: Gimona
authors.forename: M
authors.initials: M
authors.lastname: Scatena
authors.forename: S
authors.initials: S
authors.lastname: Sartore
authors.forename: J V
authors.initials: JV
authors.lastname: Small
mesh_terms: D000199:Actins / Q000032:analysis; D000818:Animals; D000911:Antibodies, Monoclonal; D000943:Antigens, Differentiation / Q000032:analysis* / Q000502:physiology; D002135:Calcium-Binding Proteins / Q000032:analysis* / Q000502:physiology; D002148:Calmodulin-Binding Proteins / Q000032:analysis; D002454:Cell Differentiation / Q000187:drug effects / Q000502:physiology; D002642:Chick Embryo; D003285:Contractile Proteins / Q000032:analysis; D003893:Desmin / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D004622:Embryo, Mammalian / Q000737:chemistry / Q000166:cytology; D004625:Embryo, Nonmammalian; D064448:Filamins; D005455:Fluorescent Antibody Technique; D015151:Immunoblotting; D008840:Microfilament Proteins / Q000032:analysis; D009124:Muscle Proteins / Q000032:analysis* / Q000502:physiology; D009131:Muscle, Smooth, Vascular / Q000737:chemistry* / Q000166:cytology / Q000196:embryology; D009219:Myosin-Light-Chain Kinase / Q000032:analysis; D014362:Trypsinogen / Q000032:analysis; D000096985:Calponins
chemical_list: D000199:Actins; D000911:Antibodies, Monoclonal; D000943:Antigens, Differentiation; D002135:Calcium-Binding Proteins; D002148:Calmodulin-Binding Proteins; D003285:Contractile Proteins; D003893:Desmin; D064448:Filamins; D008840:Microfilament Proteins; D009124:Muscle Proteins; D009219:Myosin-Light-Chain Kinase; D014362:Trypsinogen; D000096985:Calponins; C058992:Tagln protein, mouse; C051615:transgelin