Characterization of human glutathione S-transferase P1-1-catalyzed glutathionylation of proteins: as a clue to understand the inter-individual difference in drug-induced toxicity

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Author: Zhang, Yongjie

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Publication date: 2021-05-27

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Note (General)：: 金沢大学ナノ生命科学研究所グルタチオン転移酵素GSTP1は、グルタチオン付加を触媒し生体内のタンパク質の機能を変化させうる。Keap1は通常Nrf2と相互作用し、その核内への移行を抑制しているが、酸化ストレス時にはNrf2はKeap1から離れ核内に移行し、解毒遺伝子を発現誘導する。この系における酸化...

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Material Type: 文書・図像類
Title: Characterization of human glutathione S-transferase P1-1-catalyzed glutathionylation of proteins: as a clue to understand the inter-individual difference in drug-induced toxicity
Author/Editor: Zhang, Yongjie
Author Heading: Zhang, Yongjie
Publication Date: 2021-05-27
Publication Date (W3CDTF): 2021-05-27
Alternative Title: Characterization of human glutathione S-transferase P1-1-catalyzed glutathionylation of proteins: as a clue to understand the inter-individual difference in drug-induced toxicity
Periodical title: 令和2(2020)年度科学研究費補助金若手研究研究成果報告書 = 2020 Fiscal Year Final Research Report
No. or year of volume/issue: 2019-04-01 – 2021-03-31
Volume: 2019-04-01 – 2021-03-31
Pages: 5p.-
Text Language Code: eng
Subject Heading: Glutathionylation
Keap1
GSTP1
drug-induced toxicity
Target Audience: 一般
Note (General): 金沢大学ナノ生命科学研究所
グルタチオン転移酵素GSTP1は、グルタチオン付加を触媒し生体内のタンパク質の機能を変化させうる。Keap1は通常Nrf2と相互作用し、その核内への移行を抑制しているが、酸化ストレス時にはNrf2はKeap1から離れ核内に移行し、解毒遺伝子を発現誘導する。この系における酸化ストレス時のGSTP1の役割を明らかにすることを目的とした。Keap1は実際にグルタチオン付加を受けることを明らかにし、さらに、Keap1とGSTP1がタンパク間相互作用することを高速電子間力顕微鏡(HS-AFM)で近接・解離をリアルタイムで観察することにより初めて明らかにした。Nrf2もHS-AFMで初めて観察成功した。
GSTP1 catalyzes glutathionylation of proteins to alter their functions. Under normal condition, Keap1 protein interacts with Nrf2 protein, which induces detoxification-related genes, to interfere the translocation into nucleus. Upon oxidative stress, Keap1 is suggested to be glutathionylated, which may affect the interaction with Nrf2 protein. Several experiments were conducted to understand molecular mechanisms, and the following results were obtained. 1. Purified human GSTP1, Keap1, and Nrf2 were successfully obtained from E.coli heterologous expression system. 2. HS-AFM imaging conditions for these proteins were established and optimized. This is the first observation of these dynamic structure at single molecule level. 3. Clear oxidants-dependent glutathionylation of Keap1 were observed, which also indicating an oxidative status-dependency of Keap1 molecular structure. With application of this method, glutathionylated protein concentrations were determined from in vitro samples.
研究課題/領域番号:19K16348, 研究期間(年度):2019-04-01 – 2021-03-31
出典：「Characterization of human glutathione S-transferase P1-1-catalyzed glutathionylation of proteins: as a clue to understand the inter-individual difference in drug-induced toxicity」研究成果報告書　課題番号19K16348（KAKEN：科学研究費助成事業データベース（国立情報学研究所））（https://kaken.nii.ac.jp/ja/report/KAKENHI-PROJECT-19K16348/19K16348seika/）を加工して作成
DOI: 10.24517/00059069
Access Restrictions: 限定公開
Related Material: https://kaken.nii.ac.jp/ja/search/?kw=80836180
https://kaken.nii.ac.jp/ja/grant/KAKENHI-PROJECT-19K16348/
https://kaken.nii.ac.jp/ja/report/KAKENHI-PROJECT-19K16348/19K16348seika/
Data Provider (Database): 国立情報学研究所 : 学術機関リポジトリデータベース（IRDB）（機関リポジトリ）
https://irdb.nii.ac.jp
Original Data Provider (Database): 金沢大学 : 金沢大学学術情報リポジトリKURA