2003 Fiscal Year Final Research Report Summary
Redox regulation of cell adhesion signals
| Project/Area Number |
13470491
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biological pharmacy
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| Research Institution | Showa University |
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Principal Investigator |
NOSE Kiyoshi SHOWA UNIV., SCH.PHARM.SCI., PROFESSOR, 薬学部, 教授 (70012747)
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| Co-Investigator(Kenkyū-buntansha) |
MORI Kazunori SHOWA UNIV., SCH.PHARM.SCI., RESEARCH ASSOCIATE, 薬学部, 助手 (60349040)
KIM-KANEYAMA Joori SHOWA UNIV., SCH.PHARM.SCI., RESEARCH ASSOCIATE, 薬学部, 助手 (10338535)
SHIBANUMA Makoto SHOWA UNIV., SCH.PHARM.SCI., ASSOCIATE PROFESSOR, 薬学部, 助教授 (60245876)
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| Project Period (FY) |
2001 – 2003
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| Keywords | Hic-5 / paxillin / nuclear lozalization / c-fos / focal adhesion / 核マトリクス / 核移行 |
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| Research Abstract |
Hic-5 (hydrogen peroxide-inducible clone-5) encodes a LIM protein which localizes in the focal adhesions and participates in the signal transduction from the cell surface. The Hic-5 protein translocates from the cell surface to the nucleus under oxidative condition, and regulates several target genes such as c-fos and p21. In case of c-fos genes, the transcriptional regulatory domain located at 5'-upstream region of approximately 1.5 kb from the cap site was responsible for transactivation by Hic-5. This domain contains several cis-acting sequences, but Sp1 elements was critical for the response to Hic-5. As for the mechanism of nuclear translocation of Hic-5, the LIM domains were found to be necessary. Overexpression of a cytoplasmic factor that interacts with the LIM domain 3 of Hic-5 (PTP-PEST) decreased nuclear accumulation of Hic-5 under oxidative condition. Hic-5 has an activity to oligomerize through the LIM 4 domain, and this domain functions to direct Hic-5 to the nuclear matrix fraction. Oxidative stress increased the association of Hic-5 with the nuclear matrix. These results indicate that the focal adhesion protein Hic-5 involves in cell surface signalings as well as transcriptional regulation under oxidative conditions.
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Research Products
(18 results)
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[Publications] Shibanuma, M., Kim-Kaneyama, J., Sato, S., Ishino, K., Sakamoto, N., Mashimo, J., Nose, K.: "Hic-5 communicates between focal adhesions and the nucleus through oxidant-sensitive nuclear export signal."Mol.Biol.Cell. 14. 1158-1171 (2003)
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[Publications] Hasebe, H., Egawa, K., Yamazaki, Y., Kunimoto, S., Hirai, Y., Ida, Y., Nose K.: "Specific Inhibition of HIIF-1? Activation and of VEGF Production by Flavonoids."Biol.Pharm.Bullet.. 26. 1379-1383 (2003)
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[Publications] Kawada, M., Usami, I., Ohba, S., Someno, T., Lim, J.W., Hayakawa, Y, Nose, K., Ishizuka, M.: "Hygrolidin induces p21 expression and abrogates cell cycle progression at G1 and S phases."Biochem.Biophys.Res.Commun.. 298. 178-183 (2002)
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[Publications] Jia, Y., Ranson, R.F., Shibanuma, M., Liu, C., Welsh, M.J., Smoyer, W.E.: "Identification and characterization of Hic-5/ARA55 as an Hsp27 binding protein."J.Biol.Chem.. 275. 39911-39918 (2001)
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「研究成果報告書概要(欧文)」より
