Metal Response Element-binding Transcription Factor-1 Is Activated by Degradation of Metallothionein
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- Kimura Tomoki
- Department of Toxicology, Faculty of Pharmaceutical Sciences, Setsunan University
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- Okumura Fumika
- Department of Toxicology, Faculty of Pharmaceutical Sciences, Setsunan University
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- Oguro Ikuyo
- Department of Toxicology, Graduate School of Pharmaceutical Sciences, Osaka University
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- Nakanishi Tsuyoshi
- Department of Toxicology, Graduate School of Pharmaceutical Sciences, Osaka University Present address: Laboratory of Hygienics, Gifu Pharmaceutical University
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- Sone Tomomichi
- Department of Toxicology, Faculty of Pharmaceutical Sciences, Setsunan University
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- Isobe Masakazu
- Department of Toxicology, Faculty of Pharmaceutical Sciences, Setsunan University
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- Tanaka Keiichi
- Department of Toxicology, Graduate School of Pharmaceutical Sciences, Osaka University Present address: Laboratory of Toxicology, Faculty of Pharmacy, Osaka Ohtani University
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- Itoh Norio
- Department of Toxicology, Graduate School of Pharmaceutical Sciences, Osaka University
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抄録
Cytosolic zinc-binding protein, metallothionein (MT), is normally saturated with Zn. It is thought that Zn-saturated MT (Zn-MT) acts as a major intracellular Zn pool. Metal-response element-binding transcription factor-1 (MTF-1) plays an important role in Zn-mediated MT transcription. Here, we showed that degradation of Zn-MT activates MTF-1. We measured activated MTF-1 using an electrophoretic mobility shift assay. Interleukin-6 induced MT expression and increased MTF-1 activity. MTF-1 activation was not observed in MT-overexpressing cells. MT-dependent MTF-1 activation was observed only after treating MT-overexpressing cells with cycloheximide (CHX), a protein synthesis inhibitor. CHX-treatment increased the degradation/synthesis ratio of protein. An increase in the degradation/synthesis ratio for the MT protein is expected to increase the level of labile Zn and activate MTF-1. Recombinant MTF-1 was activated by H2O2 only in the presence of Zn-MT. Oxidative stress activated MTF-1 DNA-binding activity in primary cultured hepatocytes but not in MT-deficient hepatocytes. These findings suggest that degradation of Zn-MT activates MTF-1, and that MT plays an important role in zinc-mediated signal transduction.
収録刊行物
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- JOURNAL OF HEALTH SCIENCE
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JOURNAL OF HEALTH SCIENCE 55 (1), 72-76, 2009
公益社団法人 日本薬学会
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詳細情報 詳細情報について
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- CRID
- 1390282679475562368
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- NII論文ID
- 110007055930
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- NII書誌ID
- AA11316464
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- ISSN
- 13475207
- 13449702
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- NDL書誌ID
- 9782118
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- NDL
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