p38 mitogen-activated protein kinase contributes to angiotensin 2-stimulated migration of rat aortic smooth muscle cells

DOI Web Site PubMed 被引用文献2件 参考文献62件
  • Lee Hwan Myung
    Department of Medicine, College of Medicine, Konkuk University, Korea
  • Lee Chang-Kwon
    Department of Medicine, College of Medicine, Konkuk University, Korea
  • Lee So Hee
    Department of Medicine, College of Medicine, Konkuk University, Korea
  • Roh Hui Yul
    Department of Medicine, College of Medicine, Konkuk University, Korea
  • Bae Young Min
    Department of Medicine, College of Medicine, Konkuk University, Korea
  • Lee Kyung-Yung
    Department of Medicine, College of Medicine, Konkuk University, Korea
  • Lim Jaegeun
    Department of Biomedical Engineering, Keukdong College, Korea
  • Park Pyo-Jam
    Division of Life Science, College of Biomedical and Health Science, Konkuk University, Korea
  • Park Tae-Kyu
    Division of Life Science, College of Biomedical and Health Science, Konkuk University, Korea
  • Lee Yun Lyul
    Department of Physiology, College of Medicine, Hallym University, Korea
  • Won Kyung-Jong
    Department of Medicine, College of Medicine, Konkuk University, Korea
  • Kim Bokyung
    Department of Medicine, College of Medicine, Konkuk University, Korea

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タイトル別名
  • p38 Mitogen-Activated Protein Kinase Contributes to Angiotensin II-Stimulated Migration of Rat Aortic Smooth Muscle Cells

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In this study, we clarified the intracellular mechanism of angiotensin II (Ang II) in promoting migration in rat aortic smooth muscle cells (RASMCs). RASMC migration was measured with the Boyden chamber assay, and the result was confirmed with an aortic sprout assay. The activities of kinases were investigated by western blot analysis. Ang II enhanced RASMC migration, which was chemotaxis directed, and induced the phosphorylation of p38 mitogen-activated protein kinase (MAPK), extracellular signal-regulated kinase 1/2 (ERK1/2), and heat shock protein 27 (Hsp27). Ang II-enhanced cell migration was inhibited by SB203580 (a p38 MAPK inhibitor) and piceatannol (a spleen tyrosine kinase inhibitor), but only partially by PD98059 (an ERK inhibitor) and PP2 (a Src inhibitor). The Ang II-stimulated phosphorylation of p38 MAPK and Hsp27 in RASMCs was inhibited by piceatannol and SB203580. The phosphorylation of ERK1/2 stimulated by Ang II was suppressed by PD98059, piceatannol, and PP2. Ang II increased the sprout outgrowth from aortic rings and this response was attenuated by pretreatment with SB203580, PD98059, PP2, or piceatannol. These results suggest that p38 MAPK contributes to the regulation of the Ang II-induced chemotactic migration of vascular smooth muscle cells, which is mediated by Hsp27 phosphorylation.<br>

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