Epo-C12 inhibits peroxiredoxin 1 peroxidase activity

Tomoka Yoda, Masateru Furuta, Tomohiko Tsutsumi, Seiki Ikeda, Shunsuke Yukizawa, Satoshi Arai, Akinori Morita, Kenji Yamatoya, Kazuya Nakata, Shusuke Tomoshige, Kenji Ohgane, Yuuki Furuyama, Kengo Sakaguchi, Fumio Sugawara, Susumu Kobayashi, Masahiko Ikekita, Kouji Kuramochi

Research output: Contribution to journalArticlepeer-review

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.

Original languageEnglish
Article number116203
JournalBioorganic and Medicinal Chemistry
Volume41
DOIs
Publication statusPublished - 2021 Jul 1

Keywords

  • Chaperone
  • Epolactaene
  • Peroxidase
  • Peroxiredoxin 1
  • Reactive oxygen species

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

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