Epo-C12 inhibits peroxiredoxin 1 peroxidase activity

[Display omitted] 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 exper...

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Published in:Bioorganic & medicinal chemistry 2021-07, Vol.41, p.116203-116203, Article 116203
Main Authors: Yoda, Tomoka, Furuta, Masateru, Tsutsumi, Tomohiko, Ikeda, Seiki, Yukizawa, Shunsuke, Arai, Satoshi, Morita, Akinori, Yamatoya, Kenji, Nakata, Kazuya, Tomoshige, Shusuke, Ohgane, Kenji, Furuyama, Yuuki, Sakaguchi, Kengo, Sugawara, Fumio, Kobayashi, Susumu, Ikekita, Masahiko, Kuramochi, Kouji
Format: Article
Language:English
Subjects:
Chaperone
Epolactaene
Peroxidase
Peroxiredoxin 1
Reactive oxygen species
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Summary:[Display omitted] 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.
ISSN:0968-0896
1464-3391
DOI:10.1016/j.bmc.2021.116203