A mechanism regulating the copper acquisition by intracellular proteins
| Project/Area Number |
25291028
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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 |
Functional biochemistry
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| Research Institution | Keio University |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
NOMURA Takao 慶應義塾大学, 理工学部, 助教 (90597840)
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥17,940,000 (Direct Cost: ¥13,800,000、Indirect Cost: ¥4,140,000)
Fiscal Year 2015: ¥5,070,000 (Direct Cost: ¥3,900,000、Indirect Cost: ¥1,170,000)
Fiscal Year 2014: ¥5,850,000 (Direct Cost: ¥4,500,000、Indirect Cost: ¥1,350,000)
Fiscal Year 2013: ¥7,020,000 (Direct Cost: ¥5,400,000、Indirect Cost: ¥1,620,000)
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| Keywords | 銅シャペロン / 神経変性疾患 / タンパク質フォールディング / SOD1 / タンパク質凝集 / 筋萎縮性側索硬化症 / 金属タンパク質 / タンパク質 / 銅イオン / 金属シャペロン / ジスルフィド結合 |
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| Outline of Final Research Achievements |
Copper ion is essential to various physiologies. Most of the copper ions in our bodies exist as the protein-bound form and function as active sites for enzymatic reactions. Also, the level of copper ions in our bodies is strictly controlled, and even slight deviation of the copper ions in physiological conditions will lead to pathological conditions and sometimes fatal diseases. Here, we investigated the mechanism regulating the acquisition of copper ions by intracellular proteins and also examined the molecular pathomechanism of the disease caused by the mis-regulation of copper metabolism in the cell. More precisely, we have noted the activation mechanism of Cu,Zn-superoxide dismutase (SOD1), which requires a copper ion for its enzymatic activity. Also, conformational changes of SOD1 upon dissociation of metal ions have been examined and discussed in relation to the pathogenesis of amyotrophic lateral sclerosis.
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Report
(4 results)
Research Products
(34 results)
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[Journal Article] Intranuclear aggregation of mutant FUS/TLS as a molecular pathomechanism of amyotrophic lateral sclerosis2014
Author(s)
Nomura, T., Watanabe, S., Kaneko, K., Yamanaka, K., Nukina, N. & Furukawa, Y.
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Journal Title
J. Biol. Chem.
Volume: 289
Issue: 2
Pages: 1192-1202
DOI
Related Report
Peer Reviewed / Open Access
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