The analysis of regulatory mechanisms of degradation/aggregation of abnormally accumulated protein in fontotemporal dementia brain.
| Project/Area Number |
24390283
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Partial Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Psychiatric science
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| Research Institution | Osaka University |
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Principal Investigator |
TAKEDA Masatoshi 大阪大学, 医学(系)研究科(研究院), 教授 (00179649)
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| Co-Investigator(Kenkyū-buntansha) |
TANAKA Toshihisa 大阪大学, 医学(系)・研究科(研究院), 准教授 (10294068)
KUDO Takashi 大阪大学, 保健センター, 教授 (10273632)
MORIHARA Takashi 大阪大学, 医学(系)・研究科(研究院), 助教 (90403196)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥18,070,000 (Direct Cost: ¥13,900,000、Indirect Cost: ¥4,170,000)
Fiscal Year 2014: ¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2013: ¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2012: ¥8,580,000 (Direct Cost: ¥6,600,000、Indirect Cost: ¥1,980,000)
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| Keywords | タウ蛋白 / XIAP / アポトーシス / ＸＩＡＰ |
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| Outline of Final Research Achievements |
The effects of phosphorylation on interaction of tau with ubiquitin conjyugating enzyme XIAP (X-linked Inhibitor to apoptosis protein) were analayzed. Wild typed tau and Met-deleted tau were prepared and pull-down assay was caried out using XIAP after phophorylation of both tau and both tau proteins were incubated with ubiquitination enzyme sources togather with XIAP, and the effects of phosphorylation on ubiquitinaation were evaluated. No signifivcant difference was observed between non-phosphorylated samples and phosphorylated ones. Then binding partner to phosphorylated TDP-43 was invesytigated employing phosphorylated and non-phosphorylated peptides coresponding to Ser409/Ser410 of TDP-43. Then specigfic binding proteins were purified.
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Report
(4 results)
Research Products
(10 results)
