1999 Fiscal Year Final Research Report Summary
Study of the molecular mechanism of transactivation of PPAR
Project/Area Number |
10672039
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Biological pharmacy
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Research Institution | The University of Tokyo, Institute of Molecular and Cellular Biosciences |
Principal Investigator |
YANAGISAWA Junn The University of Tokyo, Institute of Molecular and Cellular Biosciences, Assistant Professor, 分子細胞生物学研究所, 助手 (50301114)
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Co-Investigator(Kenkyū-buntansha) |
KATO Shigeaki The University of Tokyo, Institute of Molecular and Cellular Biosciences, Assistant Professor, 分子細胞生物学研究所, 助手 (60204468)
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Project Period (FY) |
1998 – 1999
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Keywords | Nuclear Receptor / PPAR / ligand / Cooctivator |
Research Abstract |
Peroxisome proliferator-activated receptors (PPARs) are transcription factors belonging to the nuclear receptor super family. PPARa is predominantly expressed in tissues exhibiting high catabolic rates of fatty acids, while PPARg is adipose tissue selective where it triggers adipocyte differentiation' and lipid storage by regulating the expression of genes critical for adipogenesis. PPARS function as ligand-dependent transcription factors, which, upon heterodimerization with RXR, bind to specific response element termed PPRE, thus reguleting the expression of target genes. PPARs are activated by a number of ligands. These ligands exhibit the ligand-specific action through PPARs, suggesting that the liganded PPAR would reqruite a specific coacitator complex. Furthermore, the synthesis of ligands are thought to be strictly controled by ligand metabolic eazymes. Thus, we tried to identified coactivators for PPARs and ligand metabolic enzymes.
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[Publications] Kobayashi, Y., Kitamoto, T., Masuhiro, Y., Watanabe, M., Kase, T., Metzger, D., Yanagisawa J., Kato, S.: "p300 mediates functional synergism between AF-1 and AF-2 of estrogen receptor α and β by interacting directly with the N-terminal A/B domains."J. Biol. Chem.. (in press). (2000)
Description
「研究成果報告書概要(欧文)」より
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[Publications] Yanagisawa, J., Yanagi, Y., Masuhiro, Y., Suzawa, M., Toriyabe, T., Kashiwagi, K., Watanabe, M., Kawabata, M., Miyazono, K., Kato, S.: "Convergence of TGFβ and vitamin D signaling pathways on SMAD proteins acting as common transcriptional co-activators."Science. 283. 1317-1321 (1999)
Description
「研究成果報告書概要(欧文)」より
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[Publications] Takeyama, K., Masuhiro, Y., Fuse, H., Endoh, H., Murayama, A., Kitanaka, S., Suzawa, M., Yanagisawa, J., Kato, S.: "Selective interaction of vitamin D receptor with transcriptional coactivators by a vitamin D analog."Mol. Cell. Biol.. 19. 1049-1055 (1999)
Description
「研究成果報告書概要(欧文)」より
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[Publications] Endoh, H., Maruyama, K., Masuhiro, Y., Kobayashi, Y., Goto, M., Tai, H., Yanagisawa, J., Metzger, D., Hashimoto, S., Kato, S.: "Purification and identification of p68 RNA helicase acting as a transcriptional coactivator specific for the activation function 1 of human estrogen receptor α."Mol. Cell. Biol.. 19. 5363-5372 (1999)
Description
「研究成果報告書概要(欧文)」より
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[Publications] Kitanaka, S., Takeyama, K., Murayama, A., Sato, T., Okumura, K., Nogami, M., Hasegawa, Y., Niimi, H., Yanagisawa J., Tanaka, T., Kato, S.: "Inactivating mutations in the human 25-hydroxyvitamin DィイD23ィエD2 1α-hydroxylase gene in patients with pseudovitamin D-deficient rickets."N. Engl. J. Med.. 338. 653-661 (1998)
Description
「研究成果報告書概要(欧文)」より
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[Publications] Takeyama, K., Kitanaka, S., Sato, T., Kobori, M., Yanagisawa, J., Kato, S.: "25-Hydroxyvitamin DィイD23ィエD2 1α-hydroxylase and vitamin D synthesis."Science. 277. 1827-1830 (1997)
Description
「研究成果報告書概要(欧文)」より