| Project/Area Number |
25670153
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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 |
General medical chemistry
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| Research Institution | Tokyo Metropolitan Institute of Medical Science |
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Principal Investigator |
HARA Takahiko 公益財団法人東京都医学総合研究所, 生体分子先端研究分野, プロジェクトリーダー(参事研究員) (80280949)
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| Co-Investigator(Kenkyū-buntansha) |
SUZUKI Teruhiko 公益財団法人東京都医学総合研究所, 生体分子先端研究分野, 主席研究員 (70621027)
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| Project Period (FY) |
2013-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥3,770,000 (Direct Cost: ¥2,900,000、Indirect Cost: ¥870,000)
Fiscal Year 2014: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
Fiscal Year 2013: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
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| Keywords | プロテアソーム / ハダカデバネズミ / 老化 / ユビキチン化 / アンチエイジング / タンパク質品質管理 |
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| Outline of Final Research Achievements |
Naked mole rat (NMR) is an extraordinarily long-lived rodent. It was previously shown that age-dependent increase of ubiquitinated proteins in the liver does not occur in NMRs. We hypothesized that the ubiquitin-proteasome system of NMRs is different from that of mice. To test that possibility, we isolated 26S proteasome complex from NMR-derived dermal fibroblasts and mouse dermal fibroblasts and compared their proteasome activities. We found that chymotrypsin-like activity of NMR-fibroblasts was 2.5 times higher than that of mouse fibroblasts. Quantitative comparison of major proteasome subunits between two species by qRT-PCR and western blotting revealed that β1i, one of the immunoproteasome components, is abundantly expressed in NMR fibroblasts. We also confirmed the incorporation of β1i protein in the 26S proteasome of NMR fibroblasts. These results collectively indicate the presence of NMR-specific proteasome complex with a higher degradation capacity of ubiquitinated proteins.
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