Understanding a mechanism regulating intracellular dynamics of metal ions
| Project/Area Number |
16H04768
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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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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| Project Period (FY) |
2016-04-01 – 2020-03-31
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| Project Status |
Completed (Fiscal Year 2019)
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| Budget Amount *help |
¥17,810,000 (Direct Cost: ¥13,700,000、Indirect Cost: ¥4,110,000)
Fiscal Year 2019: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
Fiscal Year 2018: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
Fiscal Year 2017: ¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2016: ¥8,840,000 (Direct Cost: ¥6,800,000、Indirect Cost: ¥2,040,000)
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| Keywords | 銅タンパク質 / SOD1 / 筋萎縮性側索硬化症 / 金属タンパク質 |
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| Outline of Final Research Achievements |
To understand intracellular dynamics of metal ions (copper ions, in particular), I have focused upon Cu/Zn-superoxide dismutase (SOD1), which is one of the most important copper proteins, as well as the copper chaperone protein CCS that supplies copper ions to SOD1. This study has suggested a new mechanistic action of CCS on SOD1 upon the copper supply and also newly identified a protein interacting with CCS. Furthermore, the breakdown of a copper supplying step to SOD1 was evaluated as a possible pathological change occurring in a neurodegenerative disease, amyotrophic lateral sclerosis (ALS). Misfolded SOD1 that is unable to bind copper ions has been proposed as a pathogenic species causing ALS.
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| Academic Significance and Societal Importance of the Research Achievements |
生体における金属イオンの重要性・危険性は広く認識されている一方で、金属イオンの基本的な細胞内動態・挙動については多くのことが明らかとなっていない。本研究で扱う銅タンパク質SOD1は、活性酸素であるスーパーオキシドを不均化し、酸化ストレスの軽減を担う重要なタンパク質である。よって、SOD1を中心に、細胞内銅イオンの質的・量的恒常性を維持するメカニズムに迫る本研究は、基礎科学のみならず医学的にも意義のある研究で、神経変性疾患や各種の加齢性疾患などに対する分子標的治療薬の開発に貢献できると期待される。
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Report
(5 results)
Research Products
(57 results)
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[Journal Article] Immunochemical characterization on pathological oligomers of mutant Cu/Zn-superoxide dismutase in amyotrophic lateral sclerosis2017
Author(s)
Eiichi Tokuda, Itsuki Anzai, Takao Nomura, Keisuke Toichi, Masahiko Watanabe, Shinji Ohara, Seiji Watanabe, Koji Yamanaka, Yuta Morisaki, Hidemi Misawa, and Yoshiaki Furukawa
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Journal Title
Molecular Neurodegeneration
Volume: 12
Issue: 1
Pages: 2-2
DOI
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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