title: Increased migration in late G(1) phase in cultured smooth muscle cells.
abstract: Migration and proliferation of smooth muscle cells (SMC) contribute to neointimal formation after arterial injury. However, the relation between migration and proliferation in these cells is obscure. To discriminate between migration and proliferation, we employed a migration assay of SMC at different phases of the cell cycle. Serum-deprived SMC were synchronized in different phases of the cell cycle by addition of serum for various periods of time. Migration induced by platelet-derived growth factor B-chain homodimer was maximal in SMC that were predominantly in the late G(1) (G(1b)) phase. In addition, in nonsynchronized SMC, 65-75% of SMC that had migrated were in the G(1b) phase. Phosphorylated myosin light chain was enriched around the cell periphery in SMC in the G(1b) phase compared with SMC in the other cell cycle phases. Interestingly, the Triton X-100-insoluble fraction of myosin was remarkably decreased in G(1b)-enriched SMC. These findings suggest that migratory activity of SMC may be coupled with the G(1b) phase. The phosphorylation and retention of myosin might explain some of the properties responsible for increased migration.
authors.affiliation: First Department of Internal Medicine, Osaka Medical College, Takatsuki-city, Osaka 569-8686, Japan. in1038@poh.osaka-med.ac.jp
authors.forename: R
authors.initials: R
authors.lastname: Fukui
authors.forename: M
authors.initials: M
authors.lastname: Amakawa
authors.forename: M
authors.initials: M
authors.lastname: Hoshiga
authors.forename: N
authors.initials: N
authors.lastname: Shibata
authors.forename: E
authors.initials: E
authors.lastname: Kohbayashi
authors.forename: M
authors.initials: M
authors.lastname: Seto
authors.forename: Y
authors.initials: Y
authors.lastname: Sasaki
authors.forename: T
authors.initials: T
authors.lastname: Ueno
authors.forename: N
authors.initials: N
authors.lastname: Negoro
authors.forename: T
authors.initials: T
authors.lastname: Nakakoji
authors.forename: M
authors.initials: M
authors.lastname: Ii
authors.forename: F
authors.initials: F
authors.lastname: Nishiguchi
authors.forename: T
authors.initials: T
authors.lastname: Ishihara
authors.forename: N
authors.initials: N
authors.lastname: Ohsawa
mesh_terms: D000199:Actins / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D000077214:Becaplermin; D002448:Cell Adhesion / Q000502:physiology; D002465:Cell Movement / Q000187:drug effects / Q000502:physiology*; D002478:Cells, Cultured; D003598:Cytoskeletal Proteins / Q000378:metabolism; D004247:DNA / Q000378:metabolism; D005353:Fibronectins / Q000378:metabolism; D005434:Flow Cytometry; D051417:Focal Adhesion Kinase 1; D051416:Focal Adhesion Protein-Tyrosine Kinases; D016193:G1 Phase / Q000502:physiology*; D006801:Humans; D007399:Interphase / Q000502:physiology; D009131:Muscle, Smooth, Vascular / Q000166:cytology* / Q000187:drug effects / Q000378:metabolism*; D018994:Myosin Light Chains / Q000737:chemistry / Q000378:metabolism; D017830:Octoxynol / Q000737:chemistry / Q000494:pharmacology; D051419:Paxillin; D010750:Phosphoproteins / Q000378:metabolism; D010766:Phosphorylation / Q000187:drug effects; D010982:Platelet-Derived Growth Factor / Q000494:pharmacology; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D020574:Proto-Oncogene Proteins c-sis; D012313:RNA / Q000378:metabolism; D011817:Rabbits; D012995:Solubility / Q000187:drug effects
chemical_list: D000199:Actins; D003598:Cytoskeletal Proteins; D005353:Fibronectins; D018994:Myosin Light Chains; C496061:PXN protein, human; D051419:Paxillin; D010750:Phosphoproteins; D010982:Platelet-Derived Growth Factor; D020574:Proto-Oncogene Proteins c-sis; D000077214:Becaplermin; D012313:RNA; D017830:Octoxynol; D004247:DNA; D011505:Protein-Tyrosine Kinases; D051417:Focal Adhesion Kinase 1; D051416:Focal Adhesion Protein-Tyrosine Kinases; C496050:PTK2 protein, human