| Project/Area Number |
20590999
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Neurology
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| Research Institution | Tottori University |
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Principal Investigator |
NAKASO Kazuhiro Tottori University, 医学部, 講師 (30379648)
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| Co-Investigator(Renkei-kenkyūsha) |
ITO Satoru 鳥取大学, 医学部附属病院, 助教 (20448195)
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| Project Period (FY) |
2008 – 2010
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| Project Status |
Completed (Fiscal Year 2010)
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| Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2010: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2009: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2008: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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| Keywords | p62(A170) / Lewy小体 / 凝集体 / sequestration / オートファジー / パーキンソン病 / 蛋白分解 / 細胞内凝集体 / SQSTM1 / ユビキチン-プロテアソーム系 / ストレス応答 / ユビキチンープロテアソーム系 / 封入体 |
|---|
| Research Abstract |
Most neurodegenerative diseases such as Parkinson's disease (PD) show neuronal inclusion body in the patient's brain. p62(A170) is one of the component proteins of the inclusion body, and it is believed that it plays an important role in the step of protein sequestration and induces unfolded proteins to the proteolysis by autophagy. In the present study, we clarified that p62(A170) was induced in the transcription level by proteasome inhibition or overexpression of alpha-synuclein. Furthermore, autophagy-related molecules, such as LC3, were colocalized with p62(A170) existing inclusion body.
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