| Project/Area Number |
23590374
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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 |
Pathological medical chemistry
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| Research Institution | Himeji Dokkyo University |
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Principal Investigator |
TOHYAMA Yumi 姫路獨協大学, 薬学部, 教授 (70362770)
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| Co-Investigator(Renkei-kenkyūsha) |
KAJI Hiroaki 姫路獨協大学, 薬学部, 講師 (10368706)
TANAKA Chisato 姫路獨協大学, 薬学部, 助手 (30461122)
MORITA Hiroyuki 姫路獨協大学, 薬学部, 助手 (90648594)
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥5,200,000 (Direct Cost: ¥4,000,000、Indirect Cost: ¥1,200,000)
Fiscal Year 2013: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2012: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2011: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | 破骨細胞 / ATP / アクチン / P2X7受容体 / Syk / F-アクチン |
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| Research Abstract |
To determine the molecular mechanism of osteoclast activation, human monocytes and human leukemic cell line, HL60 were used after differentiation into ostelclast-like cells. To analyze the role of target molecules on osteoclast function, knocked down cells of PKC-delta, KIF20A, Vimentin, or SMN, were established by lentiviral transfection containing each shRNA. Knockdown of PKC-delta or Vimentin led to decreased podosome (F-actin structure) formation. Knockdown of both KIF20A and SMN increased multinuclear cells resulting from cell to cell fusion. In addition, SMN-knockdown promoted alpha-tubulin acetylation (K40), which is essential for lysosomal trasnport, suggesting that SMN is a regulator of osteoclast activation.
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