1. Academic Validation
  2. Epo-C12 inhibits peroxiredoxin 1 peroxidase activity

Epo-C12 inhibits peroxiredoxin 1 peroxidase activity

  • Bioorg Med Chem. 2021 Jul 1:41:116203. doi: 10.1016/j.bmc.2021.116203.
Tomoka Yoda 1 Masateru Furuta 1 Tomohiko Tsutsumi 1 Seiki Ikeda 1 Shunsuke Yukizawa 1 Satoshi Arai 1 Akinori Morita 2 Kenji Yamatoya 3 Kazuya Nakata 4 Shusuke Tomoshige 5 Kenji Ohgane 1 Yuuki Furuyama 1 Kengo Sakaguchi 1 Fumio Sugawara 1 Susumu Kobayashi 6 Masahiko Ikekita 1 Kouji Kuramochi 7
Affiliations

Affiliations

  • 1 Department of Applied Biological Science, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan.
  • 2 Department of Applied Biological Science, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan; Department of Biomedical Science and Technology, Graduate School of Biomedical Sciences, Tokushima University, 3-18-15 Kuramoto-cho, Tokushima 770-8503, Japan.
  • 3 Department of Applied Biological Science, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan; Institute for Environmental and Gender-Specific Medicine, Juntendo University Graduate School of Medicine, 2-1-1 Tomioka, Urayasu-City, Chiba, 279-0021, Japan.
  • 4 Department of Applied Biological Science, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan; Graduate School of Bio-Applications and Systems Engineering, Tokyo University of Agriculture and Technology, 2-24-16 Nakacho, Koganei, Tokyo, 184-0012, Japan.
  • 5 Department of Applied Biological Science, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan; Graduate School of Life Sciences, Tohoku University, 2-1-1 Katahira, Aoba-ku, Sendai 980-8577, Japan.
  • 6 Department of Pharmacy, Faculty of Pharmaceutical Sciences, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan.
  • 7 Department of Applied Biological Science, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan. Electronic address: kuramoch@rs.tus.ac.jp.
Abstract

Epo-C12 is a synthetic derivative of epolactaene, isolated from Penicillium sp. BM 1689-P. Epo-C12 induces Apoptosis in human acute lymphoblastoid leukemia BALL-1 cells. In our previous studies, seven proteins that bind to Epo-C12 were identified by a combination of pull-down experiments using biotinylated Epo-C12 (Bio-Epo-C12) and mass spectrometry. In the present study, the effect of Epo-C12 on peroxiredoxin 1 (Prx 1), one of the proteins that binds to Epo-C12, was investigated. Epo-C12 inhibited Prx 1 peroxidase activity. However, it did not suppress its chaperone activity. Binding experiments between Bio-Epo-C12 and point-mutated Prx 1s suggest that Epo-C12 binds to Cys52 and Cys83 in Prx 1. The present study revealed that Prx 1 is one of the target proteins through which Epo-C12 exerts an apoptotic effect in BALL-1 cells.

Keywords

Chaperone; Epolactaene; Peroxidase; Peroxiredoxin 1; Reactive oxygen species.

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