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• W3010350167 abstract "Rationale Oxidative stress is an imbalance between reactive free radical oxygen species and antioxidant defenses. Its consequences can lead to numerous pathologies. Regulating oxidative stress is the complex interplay between antioxidant recycling and thiol‐containing regulatory proteins. Understanding these regulatory mechanisms is important for preventing onset of oxidative stress. The aim of this study was to investigae S‐thiol protein chemistry associated with oxidized vitamin C (dehydroascorbate, DHA), homocysteine (HcySH) and glutathione (GSH) using mass spectrometry. Methods Glutaredoxin‐1 (Grx‐1) was incubated with DHA, with and without GSH and HcySH. Disulfide formation was followed by electrospray ionization mass spectrometry (ESI‐MS) of intact proteins and by LC/ESI‐MS/MS of peptides from protein tryptic digestions. The mechanism of DHA‐mediated S‐thiolation was investigated using two synthetic peptides: AcFHACAAK and AcFHACE. Three proteins, i.e. human hemoglobin (HHb), recombinant peroxiredoxin 2 (Prdx2) and Grx‐1, were S‐homocysteinylated followed by S‐transthiolyation with GSH and investigated by ESI‐MS and ESI‐MS/MS. Results ESI‐MS analysis reveals that DHA mediates disulfide formation and S‐thiolation by HcySH as well as GSH of Grx‐1. LC/ESI‐MS/MS analysis allows identification of Grx‐1 S‐thiolated cysteine adducts. The mechanism by which DHA mediates S‐thiolation of heptapeptide AcFHACAAK is shown to be via initial formation of a thiohemiketal adduct. In addition, ESI‐MS of intact proteins shows that GSH can S‐transthiolate S‐homocysteinylated Grx‐1_ HHb and Prdx2. The GS‐S‐protein adducts over time dominate the ESI‐MS spectrum profile. Conclusions Mass spectrometry is a unique analytical technique for probing complex reaction mechanisms associated with oxidative stress. Using model proteins, ESI‐MS reveals the mechanism of DHA‐facilitated S‐thiolation, which consists of thiohemiketal formation, disulfide formation or S‐thiolation. Furthermore, protein S‐thiolation by HcySH can be reversed by reversible GSH thiol exchange. The use of mass spectrometry with in vitro models of protein S‐thiolation in oxidative stress may provide significant insight into possible mechanisms of action occurring in vivo." @default.
• W3010350167 created "2020-03-13" @default.
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• W3010350167 date "2020-04-23" @default.
• W3010350167 modified "2023-09-27" @default.
• W3010350167 title "Investigating protein thiol chemistry associated with dehydroascorbate, homocysteine and glutathione using mass spectrometry" @default.
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• W3010350167 doi "https://doi.org/10.1002/rcm.8774" @default.
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