Increased migration in late G(1) phase in cultured smooth muscle cells
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 differe...
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| Veröffentlicht in: | American Journal of Physiology: Cell Physiology 2000-10, Vol.279 (4), p.C999-1007 |
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| creator | Fukui, R Amakawa, M Hoshiga, M Shibata, N Kohbayashi, E Seto, M Sasaki, Y Ueno, T Negoro, N Nakakoji, T Ii, M Nishiguchi, F Ishihara, T Ohsawa, N |
| description | 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. |
| doi_str_mv | 10.1152/ajpcell.2000.279.4.C999 |
| format | Article |
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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.</description><identifier>ISSN: 0363-6143</identifier><identifier>DOI: 10.1152/ajpcell.2000.279.4.C999</identifier><identifier>PMID: 11003580</identifier><language>eng</language><publisher>United States</publisher><subject>Actins - chemistry ; Actins - metabolism ; Animals ; Cell Adhesion - physiology ; Cell Movement - drug effects ; Cell Movement - physiology ; Cells, Cultured ; Cytoskeletal Proteins - metabolism ; DNA - metabolism ; Fibronectins - metabolism ; Flow Cytometry ; Focal Adhesion Kinase 1 ; Focal Adhesion Protein-Tyrosine Kinases ; G1 Phase - physiology ; Humans ; Interphase - physiology ; Muscle, Smooth, Vascular - cytology ; Muscle, Smooth, Vascular - drug effects ; Muscle, Smooth, Vascular - metabolism ; Myosin Light Chains - chemistry ; Myosin Light Chains - metabolism ; Octoxynol - chemistry ; Octoxynol - pharmacology ; Paxillin ; Phosphoproteins - metabolism ; Phosphorylation - drug effects ; Platelet-Derived Growth Factor - pharmacology ; Protein-Tyrosine Kinases - metabolism ; Proto-Oncogene Proteins c-sis ; Rabbits ; RNA - metabolism ; Solubility - drug effects</subject><ispartof>American Journal of Physiology: Cell Physiology, 2000-10, Vol.279 (4), p.C999-1007</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11003580$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fukui, R</creatorcontrib><creatorcontrib>Amakawa, M</creatorcontrib><creatorcontrib>Hoshiga, M</creatorcontrib><creatorcontrib>Shibata, N</creatorcontrib><creatorcontrib>Kohbayashi, E</creatorcontrib><creatorcontrib>Seto, M</creatorcontrib><creatorcontrib>Sasaki, Y</creatorcontrib><creatorcontrib>Ueno, T</creatorcontrib><creatorcontrib>Negoro, N</creatorcontrib><creatorcontrib>Nakakoji, T</creatorcontrib><creatorcontrib>Ii, M</creatorcontrib><creatorcontrib>Nishiguchi, F</creatorcontrib><creatorcontrib>Ishihara, T</creatorcontrib><creatorcontrib>Ohsawa, N</creatorcontrib><title>Increased migration in late G(1) phase in cultured smooth muscle cells</title><title>American Journal of Physiology: Cell Physiology</title><addtitle>Am J Physiol Cell Physiol</addtitle><description>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.</description><subject>Actins - chemistry</subject><subject>Actins - metabolism</subject><subject>Animals</subject><subject>Cell Adhesion - physiology</subject><subject>Cell Movement - drug effects</subject><subject>Cell Movement - physiology</subject><subject>Cells, Cultured</subject><subject>Cytoskeletal Proteins - metabolism</subject><subject>DNA - metabolism</subject><subject>Fibronectins - metabolism</subject><subject>Flow Cytometry</subject><subject>Focal Adhesion Kinase 1</subject><subject>Focal Adhesion Protein-Tyrosine Kinases</subject><subject>G1 Phase - physiology</subject><subject>Humans</subject><subject>Interphase - physiology</subject><subject>Muscle, Smooth, Vascular - cytology</subject><subject>Muscle, Smooth, Vascular - drug effects</subject><subject>Muscle, Smooth, Vascular - metabolism</subject><subject>Myosin Light Chains - chemistry</subject><subject>Myosin Light Chains - metabolism</subject><subject>Octoxynol - chemistry</subject><subject>Octoxynol - pharmacology</subject><subject>Paxillin</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation - drug effects</subject><subject>Platelet-Derived Growth Factor - pharmacology</subject><subject>Protein-Tyrosine Kinases - metabolism</subject><subject>Proto-Oncogene Proteins c-sis</subject><subject>Rabbits</subject><subject>RNA - metabolism</subject><subject>Solubility - drug effects</subject><issn>0363-6143</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo1j8tOwzAQRb0A0VL4BfAKwSLBj_i1RBUtlSqxgXXkuGOaynkQOwv-nkSU1Uhzju7MReiekpxSwZ7tqXcQQs4IITlTJi_ytTHmAi0JlzyTtOALdB3jaeIFk-YKLSglhAtNlmiza90ANsIBN_XXYFPdtbhucbAJ8PaRPuH-ONF55caQxmESY9N16YibMboAeL4db9CltyHC7Xmu0Ofm9WP9lu3ft7v1yz7rKTcpcwDMi0oz6TVYkNZIRbVTlXDSeqI8rwSAkNzTikkBAigoYILJonBQKL5CD3-5_dB9jxBT2dRx_sC20I2xVIxppTWdxLuzOFYNHMp-qBs7_JT_zfkvmMRbMw</recordid><startdate>200010</startdate><enddate>200010</enddate><creator>Fukui, R</creator><creator>Amakawa, M</creator><creator>Hoshiga, M</creator><creator>Shibata, N</creator><creator>Kohbayashi, E</creator><creator>Seto, M</creator><creator>Sasaki, Y</creator><creator>Ueno, T</creator><creator>Negoro, N</creator><creator>Nakakoji, T</creator><creator>Ii, M</creator><creator>Nishiguchi, F</creator><creator>Ishihara, T</creator><creator>Ohsawa, N</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>200010</creationdate><title>Increased migration in late G(1) phase in cultured smooth muscle cells</title><author>Fukui, R ; Amakawa, M ; Hoshiga, M ; Shibata, N ; Kohbayashi, E ; Seto, M ; Sasaki, Y ; Ueno, T ; Negoro, N ; Nakakoji, T ; Ii, M ; Nishiguchi, F ; Ishihara, T ; Ohsawa, N</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p139t-cee2f5b826f8eae6a96718c7b5c6af07f3b5ee563f1b265e5e1e7e252644ce473</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Actins - chemistry</topic><topic>Actins - metabolism</topic><topic>Animals</topic><topic>Cell Adhesion - physiology</topic><topic>Cell Movement - drug effects</topic><topic>Cell Movement - physiology</topic><topic>Cells, Cultured</topic><topic>Cytoskeletal Proteins - metabolism</topic><topic>DNA - metabolism</topic><topic>Fibronectins - metabolism</topic><topic>Flow Cytometry</topic><topic>Focal Adhesion Kinase 1</topic><topic>Focal Adhesion Protein-Tyrosine Kinases</topic><topic>G1 Phase - physiology</topic><topic>Humans</topic><topic>Interphase - physiology</topic><topic>Muscle, Smooth, Vascular - cytology</topic><topic>Muscle, Smooth, Vascular - drug effects</topic><topic>Muscle, Smooth, Vascular - metabolism</topic><topic>Myosin Light Chains - chemistry</topic><topic>Myosin Light Chains - metabolism</topic><topic>Octoxynol - chemistry</topic><topic>Octoxynol - pharmacology</topic><topic>Paxillin</topic><topic>Phosphoproteins - metabolism</topic><topic>Phosphorylation - drug effects</topic><topic>Platelet-Derived Growth Factor - pharmacology</topic><topic>Protein-Tyrosine Kinases - metabolism</topic><topic>Proto-Oncogene Proteins c-sis</topic><topic>Rabbits</topic><topic>RNA - metabolism</topic><topic>Solubility - drug effects</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fukui, R</creatorcontrib><creatorcontrib>Amakawa, M</creatorcontrib><creatorcontrib>Hoshiga, M</creatorcontrib><creatorcontrib>Shibata, N</creatorcontrib><creatorcontrib>Kohbayashi, E</creatorcontrib><creatorcontrib>Seto, M</creatorcontrib><creatorcontrib>Sasaki, Y</creatorcontrib><creatorcontrib>Ueno, T</creatorcontrib><creatorcontrib>Negoro, N</creatorcontrib><creatorcontrib>Nakakoji, T</creatorcontrib><creatorcontrib>Ii, M</creatorcontrib><creatorcontrib>Nishiguchi, F</creatorcontrib><creatorcontrib>Ishihara, T</creatorcontrib><creatorcontrib>Ohsawa, N</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>American Journal of Physiology: Cell Physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fukui, R</au><au>Amakawa, M</au><au>Hoshiga, M</au><au>Shibata, N</au><au>Kohbayashi, E</au><au>Seto, M</au><au>Sasaki, Y</au><au>Ueno, T</au><au>Negoro, N</au><au>Nakakoji, T</au><au>Ii, M</au><au>Nishiguchi, F</au><au>Ishihara, T</au><au>Ohsawa, N</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Increased migration in late G(1) phase in cultured smooth muscle cells</atitle><jtitle>American Journal of Physiology: Cell Physiology</jtitle><addtitle>Am J Physiol Cell Physiol</addtitle><date>2000-10</date><risdate>2000</risdate><volume>279</volume><issue>4</issue><spage>C999</spage><epage>1007</epage><pages>C999-1007</pages><issn>0363-6143</issn><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.</abstract><cop>United States</cop><pmid>11003580</pmid><doi>10.1152/ajpcell.2000.279.4.C999</doi></addata></record> |
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| subjects | Actins - chemistry Actins - metabolism Animals Cell Adhesion - physiology Cell Movement - drug effects Cell Movement - physiology Cells, Cultured Cytoskeletal Proteins - metabolism DNA - metabolism Fibronectins - metabolism Flow Cytometry Focal Adhesion Kinase 1 Focal Adhesion Protein-Tyrosine Kinases G1 Phase - physiology Humans Interphase - physiology Muscle, Smooth, Vascular - cytology Muscle, Smooth, Vascular - drug effects Muscle, Smooth, Vascular - metabolism Myosin Light Chains - chemistry Myosin Light Chains - metabolism Octoxynol - chemistry Octoxynol - pharmacology Paxillin Phosphoproteins - metabolism Phosphorylation - drug effects Platelet-Derived Growth Factor - pharmacology Protein-Tyrosine Kinases - metabolism Proto-Oncogene Proteins c-sis Rabbits RNA - metabolism Solubility - drug effects |
| title | Increased migration in late G(1) phase in cultured smooth muscle cells |
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