Mild Electrical Stimulation Increases Ubiquitinated Proteins and Hsp72 in A549 Cells via Attenuation of Proteasomal Degradation
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- Morino Saori
- Department of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Global COE “Cell Fate Regulation Research and Education Unit”, Kumamoto University, Japan
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- Suico Mary Ann
- Department of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Global COE “Cell Fate Regulation Research and Education Unit”, Kumamoto University, Japan
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- Kondo Tatsuya
- Department of Metabolic Medicine, Faculty of Medical and Pharmaceutical Sciences, Kumamoto University, Japan
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- Sekimoto Erika
- Department of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Global COE “Cell Fate Regulation Research and Education Unit”, Kumamoto University, Japan
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- Yano Shuichiro
- Department of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Global COE “Cell Fate Regulation Research and Education Unit”, Kumamoto University, Japan
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- Matsuda Tomoko
- Department of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Global COE “Cell Fate Regulation Research and Education Unit”, Kumamoto University, Japan
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- Matsuno Takashi
- Department of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Global COE “Cell Fate Regulation Research and Education Unit”, Kumamoto University, Japan
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- Shuto Tsuyoshi
- Department of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Global COE “Cell Fate Regulation Research and Education Unit”, Kumamoto University, Japan
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- Araki Eiichi
- Department of Metabolic Medicine, Faculty of Medical and Pharmaceutical Sciences, Kumamoto University, Japan
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- Kai Hirofumi
- Department of Molecular Medicine, Graduate School of Pharmaceutical Sciences, Global COE “Cell Fate Regulation Research and Education Unit”, Kumamoto University, Japan
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抄録
To explore the cellular effects of mild electrical stimulation (MES), we treated A549 cells with low-intensity direct current at 5 V applied for 10 min. MES did not induce cell cytotoxicity or the unfolded protein response (UPR). Interestingly, the expression of ubiquitinated proteins and heat shock protein (Hsp) 72 was increased but not that of other Hsps. MES attenuated the degradation of Hsp72, which is a substrate of the proteasome-ubiquitin system. These results, along with the observed increase in expression of ubiquitinated proteins, imply that MES may affect the proteasome system, which regulates the fate of many proteins.<br>
収録刊行物
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- Journal of Pharmacological Sciences
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Journal of Pharmacological Sciences 108 (2), 222-226, 2008
公益社団法人 日本薬理学会
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詳細情報 詳細情報について
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- CRID
- 1390001205178083072
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- NII論文ID
- 10024385095
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- NII書誌ID
- AA11806667
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- ISSN
- 13478648
- 13478613
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- NDL書誌ID
- 9684894
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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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- 使用不可