| Project/Area Number |
23659188
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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 |
Human pathology
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| Research Institution | Nara Medical University |
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Principal Investigator |
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| Co-Investigator(Kenkyū-buntansha) |
OHMORI Hitoshi 奈良県立医科大学, 医学科, 博士研究員 (80213875)
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| Project Period (FY) |
2011 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥3,770,000 (Direct Cost: ¥2,900,000、Indirect Cost: ¥870,000)
Fiscal Year 2012: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2011: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
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| Keywords | 塩基性アミノ酸 / リン酸化アミノ酸 / がん幹細胞 / 大腸癌 / リン酸化酵素 / リン酸化アルギニン / 解糖系 / 酸化的リン酸化 / 癌幹細胞 |
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| Research Abstract |
Phosphorylation of basic amino acids were an old knowledge; however, it was hardly examined from their marked lability. We found the free phosphorylated basic amino acids were increased in stem cell-enriched cancer population. Especially, phosphoarginine inhibited pyruvate kinase activity, which induced aerobic glycolysis. Inhibition of the aerobic glycolysis and induction of oxidative phosphorylation decreased stemness of cancer cells. Thus, phosphoarginine might be associated with the energy production of cancer stem cells and stemness maintenance. We also examined the effect of phosphorylation of histone lysine residue on the epigenetics. Histone lysine phosphorylation did not show a simple inhibition of acetylation or methylation of the lysine residue. Histone lysine phosphorylation might induce a transitional status to acetylation or methylation of the lysine residue.
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