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  1. 教員研究業績
  2. 臨床薬剤学研究室
  3. 原著論文

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/13183
ded1a812-48cd-49e9-a790-3473e5bcee32
Item type 研究室原著論文(1)
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
DOI
値 10.1007/s10534-017-0067-1
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