| Project/Area Number |
26460079
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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 |
Biological pharmacy
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| Research Institution | Hoshi University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
今井 正彦 星薬科大学, 薬学部, 助教 (40507670)
高橋 勝彦 星薬科大学, 薬学部, 准教授 (80307066)
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| Project Period (FY) |
2014-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2016: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2015: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2014: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | レチノイン酸 / レチノイル化 / 遺伝子発現制御 / 蛋白質修飾 / プロテインキナーゼA / シグナル伝達 / 癌 / 細胞分化 / 遺伝子発現調節 / タンパク質修飾 |
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| Outline of Final Research Achievements |
Retinoic acid (RA) elicits a wide variety of biological actions that are important for the living body. It has attracted considerable attention from the viewpoint of prevention and treatment of cancers and lifestyle-related diseases. Using human promyelocytic leukemia cells, this study identified retinoylation (protein modification by RA) as a new mechanism of RA action that is distinct from its actions through the nuclear receptor. A new retinoylated protein was identified as RhoGDI, which controls actin polymerization. In addition, the physiological role of retinoylated protein kinase A (PKA) was elucidated. It was found that PKA is stabilized and transferred into nuclei by RA treatment, where the movement of nuclear histones is also changed. This suggests that RA influences histone modification and effects epigenetic regulation. Novel RA mechanisms were analyzed by identifying nuclear phosphorylated proteins and by clarifying its association with protein modification.
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