Hyper-O-GlcNAcylation Inhibits the Induction of Heat Shock Protein 70 (Hsp 70) by Sodium Arsenite in HeLa Cells
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- Miura Yuri
- Research Team for Mechanism of Aging, Tokyo Metropolitan Institute of Gerontology
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- Sato Takatoshi
- Research Team for Mechanism of Aging, Tokyo Metropolitan Institute of Gerontology Department of Physics, School of Science and Technology, Meiji University
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- Sakurai Yoko
- Research Team for Mechanism of Aging, Tokyo Metropolitan Institute of Gerontology
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- Sakai Ryo
- Research Team for Mechanism of Aging, Tokyo Metropolitan Institute of Gerontology Department of Physics, School of Science and Technology, Meiji University
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- Hiraoka Wakako
- Department of Physics, School of Science and Technology, Meiji University
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- Endo Tamao
- Research Team for Mechanism of Aging, Tokyo Metropolitan Institute of Gerontology
書誌事項
- タイトル別名
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- Hyper-<i>O</i>-GlcNAcylation Inhibits the Induction of Heat Shock Protein 70 (Hsp 70) by Sodium Arsenite in HeLa Cells
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O-Linked β-N-acetylglucosamine-modification (O-GlcNAcylation) is a reversible, post-translational, and regulatory modification of nuclear, mitochondrial, and cytoplasmic proteins that is responsive to cellular stress. However, the role of O-GlcNAcylation in the induction of heat shock proteins (Hsps) by arsenite remains unclear. We used O-(2-acetamido-2-deoxy-D-glucopyranosylidene) amino N-phenyl carbamate (PUGNAc), an inhibitor of O-GlcNAcase, and glucosamine (GlcN), an enhancer of the hexosamine biosynthesis pathway, or O-GlcNAc transferase (OGT) short interfering RNA (siRNA) to enhance or suppress cellular O-GlcNAcylation levels, respectively, in HeLa cells. The exposure to arsenite increased O-GlcNAcylation and Hsp 70 levels in HeLa cells. However, the pre-treatment with PUGNAc or GlcN, which enhanced O-GlcNAcylation levels, decreased the arsenite-induced expression of Hsp 70. The pre-treatment with OGT siRNA, which suppressed O-GlcNAcylation levels, did not affect the induction of Hsp 70. We then examined the effects of O-GlcNAcylation on the nuclear translocation and phosphorylation of heat shock factor 1 (HSF1), and found that neither the nuclear translocation nor phosphorylation of HSF1 was regulated by O-GlcNAcylation. Finally, Hsp 70 mRNA expression was induced by arsenite, whereas the addition of PUGNAc slightly suppressed its induction. These results indicate that O-GlcNAcylation is related to arsenite-induced Hsp 70 expression, and demonstrated that hyper-O-GlcNAcylation inhibited the induction of Hsp 70 via transcriptional factors instead of HSF1.
収録刊行物
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- Biological & Pharmaceutical Bulletin
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Biological & Pharmaceutical Bulletin 37 (8), 1308-1314, 2014
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
- 1390282679608919552
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- NII論文ID
- 130004677539
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- NII書誌ID
- AA10885497
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- COI
- 1:STN:280:DC%2BC2cbos1KisA%3D%3D
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- ISSN
- 13475215
- 09186158
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- NDL書誌ID
- 025609944
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- PubMed
- 25087952
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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
- Crossref
- PubMed
- CiNii Articles
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- 使用不可