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KAKEN_16H04768seika.pdf
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Download
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:473.2 KB
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:Mar 5, 2021 |
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Total downloads since Mar 5, 2021 : 349
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| Title |
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定量的メタロプロテオミクスが明らかにする細胞内金属イオンの恒常性維持メカニズム
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テイリョウテキ メタロプロテオミクス ガ アキラカニ スル サイボウナイ キンゾク イオン ノ コウジョウセイ イジ メカニズム
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Teiryōteki metaropuroteomikusu ga akirakani suru saibōnai kinzoku ion no kōjōsei iji mekanizumu
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Understanding a mechanism regulating intracellular dynamics of metal ions
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古川, 良明
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フルカワ, ヨシアキ
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Furukawa, Yoshiaki
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慶應義塾大学・理工学部 (矢上) ・准教授
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Research team head
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科研費研究者番号 : 40415287
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2020
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科学研究費補助金研究成果報告書
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2019
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| Abstract |
細胞内における金属イオン (特に、銅イオン) の動態を理解するために、最も主要な銅タンパク質SOD1と、SOD1に銅イオンを供給する銅シャペロンCCSに着目し、その作用機序について検討を行なった。また、CCSと相互作用する新規タンパク質を網羅的に同定し、新たな細胞内金属イオン輸送経路を明らかにした。さらに、神経変性疾患ALSにおけるSOD1への銅イオン供給の破綻について検証し、金属イオン動態の制御が生命現象を維持するために重要であることを示した。
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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研究種目 : 基盤研究 (B) (一般)
研究期間 : 2016～2019
課題番号 : 16H04768
研究分野 : 生物無機化学
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