Inhibition of Angiogenesis by a Tenascin-C Peptide which Is Capable of Activating Beta1-Integrins(Molecular and Cell Biology)
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概要
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In addition to humoral angiogenic factors, including vascular endothelial growth factor (VEGF) and basic fibroblast growth factor (bFGF), integrin-mediated adhesion of vascular endothelial cells to the extracellular matrix plays an important role in neovascularization. We recently found that TNIIIA2, a peptide derived from tenascin-C, induces functional activation of β1 integrins. Here we investigated the effect of TNIIIA2 on vascular endothelial cell migration and proliferation, key processes for angiogenesis. TNIIIA2 was shown to activate β1-integrins on human dermal microvascular endothelial cells (HDMEC). HDMEC adhered to fibronectin mainly via integrin α5β1 and their haptotactic migration on that substrate was inhibited by TNIIIA2, in concomitant with a marked inhibition of Rac activation. TNIIIA2-treatment unaffected autophosphorylation of focal adhesion kinase (FAK), but induced its physical association with phospho-paxillin (Tyr118), suggesting the FAK/paxillin-dependent negative regulation of Rac activation. HDMEC proliferation on the fibronectin substrate was also inhibited by TNIIIA2-treatment, and this was accompanied either by an increase in the population of G_0/G_1 cells and, conversely, a decrease in the population of S and G_2/M cells or by dephosphorylation/inactivation of MAP-kinase (ERK1/2). Inhibited HDMEC migration and proliferation were both restored by pretreating the cells with a fibronectin peptide, FNIII14, which is capable of inactivating β1-integrins. The chorioallantoic membrane assay demonstrated an antiangiogenic effect of TNIIIA2 in vivo. Thus, TNIIIA2 appears to negatively regulate angiogenesis by inhibiting migration and proliferation of endothelial cells. The ability to activate β1-integrins may be responsible for the antiangiogenic effect of TNIIIA2, although it cannot be excluded the possibility that an additional mechanism(s) may play a role.
- 公益社団法人日本薬学会の論文
- 2008-05-01
著者
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Saito Yohei
Faculty Of Pharmaceutical Sciences Tokyo University Of Science
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SHIMAMURA Mariko
Medical R & D Center, Tokyo Metropolitan Institute of Medical Science
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Fukai F
Faculty Of Pharmaceutical Sciences Tokyo University Of Science
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深井 文雄
東京理大 薬
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深井 文雄
東理大 臨病
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FUKAI Fumio
Department of Patho-Physiology, Faculty of Pharmaceutical Science, Tokyo University of Science
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OWAKI Toshiyuki
Faculty of Pharmaceutical Sciences, Tokyo University of Science
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SAITO Yohei
Department of Molecular Patho-Physiology, Faculty of Pharmaceutical Sciences, Tokyo University of Sc
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Saito Yohei
Department Of Materials Science And Engineering Kyoto University
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Fukai Fumio
Faculty Of Pharmaceutical Sciences Tokyo University Of Science
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Fukai Fumio
Department Of Patho-physilogy Faculty Of Pharmaceutical Sciences Tokyo University Of Science
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Owaki Toshiyuki
Faculty Of Pharmaceutical Sciences Tokyo University Of Science
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SHIOTA Yasuhiro
Department of Molecular Patho-Physiology, Faculty of Pharmaceutical Sciences, Tokyo University of Sc
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NISHISAKA Mayuu
Department of Molecular Patho-Physiology, Faculty of Pharmaceutical Sciences, Tokyo University of Sc
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OWAKI Toshiyuki
Department of Molecular Patho-Physiology, Faculty of Pharmaceutical Sciences, Tokyo University of Sc
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Shimamura Mariko
Medical R&d Center Tokyo Metropolitan Institute Of Medical Science
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Nishisaka Mayuu
Department Of Molecular Patho-physiology Faculty Of Pharmaceutical Sciences Tokyo University Of Scie
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Shiota Yasuhiro
Department Of Molecular Patho-physiology Faculty Of Pharmaceutical Sciences Tokyo University Of Scie
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Saito Yohei
Department Of Computer Science Tokyo Institute Of Technology
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Fukai Fumio
Department Of Molecular Patho-physiology Faculty Of Pharmaceutical Science
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