A novel target receptor of tamoxifen on the breast cancer cell organellar membrane
| Project/Area Number |
15K00557
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Risk sciences of radiation and chemicals
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| Research Institution | Kyushu University |
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Principal Investigator |
LIU XIAOHUI 九州大学, 理学研究院, 助教 (60596849)
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| Co-Investigator(Renkei-kenkyūsha) |
SHIMOHIGASHI Yasuyuki 九州大学, 理学研究院, 名誉教授 (00211293)
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| Project Period (FY) |
2015-04-01 – 2018-03-31
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| Project Status |
Completed (Fiscal Year 2017)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2017: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2016: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2015: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | タモキシフェン受容体 / タモキシフェン / 抗エストロゲン作用 / オルガネラ膜 / 乳がん細胞 |
|---|
| Outline of Final Research Achievements |
We have recently found a novel tamoxifen-specific receptor in the endoplasmic reticulum membrane or nuclear envelope in various cells. The purpose of the present study is to identify this tamoxifen receptor substance in a breast cancer cell and also to develop the new anti-estrogen with its inability to bind to such a tamoxifen-receptor. Despite our efforts, we failed in the isolation of any receptor substances present on endoplasmic reticulum membrane this time. On the other hand, we succeeded in identifying several different kinds of candidate receptor proteins, the siRNA knockdown of which attenuated significantly the maximum binding of tamoxifen. Furthermore, we achieved in the design-synthesis of a novel series of compounds that strongly bind to the estrogen receptor, but not to the tamoxifen receptor.
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Report
(4 results)
Research Products
(19 results)
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[Journal Article] Homodimer function of human nuclear receptor ERRα evidenced using α-helix peptides in the dimer interface2018
Author(s)
Liu, X., Nakagawa, H., Sugiyama, M., Matsushima, A., Shimohigashi, M., and Shimohigashi, Y.
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Journal Title
Peptide Science 2017
Volume: -
Pages: 190-191
Related Report
Peer Reviewed
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[Journal Article] Phe2715.39 of thrombin receptor PAR-1 is a specific target of Phe-2-Phenyl group of its tethered ligand2018
Author(s)
Sugiyama, M., Fujita, T., Liu, X., Matsuyama, Y., Matsushima, A., Shimohigashi, M., and Shimohigashi, Y.
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Journal Title
Peptide Science 2017
Volume: -
Pages: 94-95
Related Report
Peer Reviewed
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[Journal Article] α-Helix-peptides composing the human nuclear receptor ERRγ competitively provoke inhibition of functional homomeric dimerization. ― Bisphenol A receptor ERRγ physiologically functions as homodimer.2017
Author(s)
Liu, X., Nishimura, H., Fujiyama, A., Matsushima, A. Shimohigashi, M., and Shimohigashi, Y.
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Journal Title
Biomedical Advances
Volume: -
Related Report
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