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Am J Physiol Cell Physiol 279: C999-C1007, 2000;
0363-6143/00 $5.00
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Vol. 279, Issue 4, C999-C1007, October 2000

Increased migration in late G1 phase in cultured smooth muscle cells

Ryosuke Fukui1, Masahiro Amakawa2, Masaaki Hoshiga1, Nobuhiko Shibata1, Eiko Kohbayashi1, Minoru Seto3, Yasuharu Sasaki3, Teruo Ueno4, Nobuyuki Negoro1, Takahiro Nakakoji1, Masaaki Li1, Futoshi Nishiguchi1, Tadashi Ishihara1, and Nakaaki Ohsawa1

1 First Department of Internal Medicine and 4 Central Research Laboratory, Osaka Medical College, Takatsuki-city, Osaka 569-8686; 2 Department of Pharmacology, Development Research Laboratories, Kaken Pharmaceutical Company, Yamashina-ku, Kyoto 607; and 3 First Laboratory for Pharmacological Research Institute for Life Science Research, Asahi Chemical Industry Company, Tagata-gun, Shizuoka 416-0934, Japan

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 G1 (G1b) phase. In addition, in nonsynchronized SMC, 65-75% of SMC that had migrated were in the G1b phase. Phosphorylated myosin light chain was enriched around the cell periphery in SMC in the G1b phase compared with SMC in the other cell cycle phases. Interestingly, the Triton X-100-insoluble fraction of myosin was remarkably decreased in G1b-enriched SMC. These findings suggest that migratory activity of SMC may be coupled with the G1b phase. The phosphorylation and retention of myosin might explain some of the properties responsible for increased migration.

myosin; atherosclerosis


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