Cysteine perthiosulfenic acid (Cys-SSOH): A novel intermediate in thiol-based redox signaling?

David E. Heppner, Milena Hristova, Tomoaki Ida, Ana Mijuskovic, Christopher M. Dustin, Virág Bogdándi, Jon M. Fukuto, Tobias P. Dick, Péter Nagy, Jianing Li, Takaaki Akaike, Albert van der Vliet

研究成果: Article査読

37 被引用数 (Scopus)

抄録

The reversible oxidation of protein cysteine residues (Cys-SH) is a key reaction in cellular redox signaling involving initial formation of sulfenic acids (Cys-SOH), which are commonly detected using selective dimedone-based probes. Here, we report that significant portions of dimedone-tagged proteins are susceptible to cleavage by DTT reflecting the presence of perthiosulfenic acid species (Cys-SSOH) due to similar oxidation of hydropersulfides (Cys-SSH), since Cys-S-dimedone adducts are stable toward DTT. Combined studies using molecular modeling, mass spectrometry, and cell-based experiments indicate that Cys-SSH are readily oxidized to Cys-SSOH, which forms stable adducts with dimedone-based probes. We additionally confirm the presence of Cys-SSH within protein tyrosine kinases such as EGFR, and their apparent oxidation to Cys-SSOH in response NADPH oxidase activation, suggesting that such Cys-SSH oxidation may represent a novel, as yet uncharacterized, event in redox-based signaling.

本文言語English
ページ(範囲)379-385
ページ数7
ジャーナルRedox Biology
14
DOI
出版ステータスPublished - 2018 4

ASJC Scopus subject areas

  • 有機化学
  • 臨床生化学

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