| Autor: |
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 |
| Jazyk: |
angličtina |
| Rok vydání: |
2018 |
| Předmět: |
|
| Zdroj: |
Redox Biology, Vol 14, Iss , Pp 379-385 (2018) |
| Druh dokumentu: |
article |
| ISSN: |
2213-2317 |
| DOI: |
10.1016/j.redox.2017.10.006 |
| Popis: |
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. Keywords: Thiol oxidation, Sulfenic acid, Dimedone, Hydrogen peroxide, NADPH oxidase, Redox signaling |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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