Cysteine perthiosulfenic acid (Cys-SSOH): A novel intermediate in thiol-based redox signaling?
Redox Biol
; 14: 379-385, 2018 04.
Article
em En
| MEDLINE
| ID: mdl-29054072
ABSTRACT
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.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Ácidos Sulfênicos
/
Compostos de Sulfidrila
/
Proteínas
/
Cisteína
Limite:
Humans
Idioma:
En
Revista:
Redox Biol
Ano de publicação:
2018
Tipo de documento:
Article
País de afiliação:
Estados Unidos