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Copper chaperone antioxidant-1, Atox-1, is involved in the induction of SOD3 in THP-1 cells.
https://gifu-pu.repo.nii.ac.jp/records/13183
https://gifu-pu.repo.nii.ac.jp/records/13183ded1a812-48cd-49e9-a790-3473e5bcee32
Item type | 研究室原著論文(1) | |||||
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公開日 | 2018-06-14 | |||||
タイトル | ||||||
タイトル | Copper chaperone antioxidant-1, Atox-1, is involved in the induction of SOD3 in THP-1 cells. | |||||
言語 | ||||||
言語 | eng | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | journal article | |||||
アクセス権 | ||||||
アクセス権 | metadata only access | |||||
アクセス権URI | http://purl.org/coar/access_right/c_14cb | |||||
抄録 | ||||||
値 | Superoxide dismutase (SOD) 3, a copper (Cu)-containing anti-oxidative enzyme, plays a key role in extracellular redox homeostasis. Cu chaperone antioxidant-1 (Atox-1) not only delivers Cu ions to SOD3 at the trans-Golgi network, it also functions as a transcription factor of SOD3; however, the role of Atox-1 in the regulation of SOD3 during the monocytic differentiation of THP-1 cells has not yet been elucidated. A treatment with 12-O-tetradecanoylphorbol-13-acetate (TPA) induced the expression of the Cu transport protein ATP7A in THP-1 cells. On the other hand, the nuclear translocation of Atox-1 was detected in TPA-treated THP-1 cells, and was suppressed in the presence of the Cu chelator, bathocuproinedisulfonic acid. Furthermore, Atox-1 bound to the SOD3 promoter region in TPA-treated THP-1 cells. The overexpression of Atox-1 in THP-1 cells significantly enhanced TPA-elicited SOD3 expression, whereas its knockdown suppressed this induction. The present results demonstrate that Atox-1 functions as a key molecule in TPA-elicited SOD3 expression. | |||||
書誌情報 |
en : Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine 巻 31, 号 1, p. 61-68, 発行日 2018 |
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DOI | ||||||
値 | 10.1007/s10534-017-0067-1 |