| Project/Area Number |
26670159
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Pathological medical chemistry
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| Research Institution | Okayama University |
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Principal Investigator |
Katayama Hiroshi 岡山大学, 医歯(薬)学総合研究科, 准教授 (90713975)
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| Co-Investigator(Kenkyū-buntansha) |
Kaori Sasai 岡山大学, 大学院医歯薬学総合研究科, 助教 (50722162)
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| Project Period (FY) |
2014-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥3,770,000 (Direct Cost: ¥2,900,000、Indirect Cost: ¥870,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥2,210,000 (Direct Cost: ¥1,700,000、Indirect Cost: ¥510,000)
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| Keywords | オーロラキナーゼ / p53 / EMT / glycolysis / Aurora kinase / Glucose Metabolism / オーロラA / ミトコンドリア |
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| Outline of Final Research Achievements |
In this research project, we examined whether Aurora-A oncoprotein involves in EMT and glycolysis which are crucial process for transformation of cells. We revealed that Aurora-A overexpression results in induction of EMT and loss of cell polarity in 3D culture, and enhanced glycolysis during mitosis. Aurora-A phosphorylation of p53 but not p73 also showed similar increase glycolysis. Analysis of proteins specifically interacting to phosphory-mimetic mutant of p53 by Mass-spectrometry revealed the existence of proteins known to involve in the process of glycolysis. Our study suggests that Aurora-A plays an essential role in the tumorigene throuhg dereguation of EMT and glycolyssis which are parlty mediated through p53 phosphorlyation.
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