Cysteine trisulfide oxidizes protein thiols and induces electrophilic stress in human cells.

ABSTRACT: The cellular effects of hydrogen sulfide (H₂S) signaling may be partially mediated by the formation of alkyl persulfides from thiols, such as glutathione and protein cysteine residues. Persulfides are potent nucleophiles and reductants and therefore potentially an important endogenous antioxidant or protein post-translational modification. To directly study the cellular effects of persulfides, cysteine trisulfide (Cys-S₃) has been proposed as an in situ persulfide donor, as it reacts with cellular thiols to generate cysteine persulfide (Cys-S-S^-). Numerous pathways sense and respond to electrophilic cellular stressors to inhibit cellular proliferation and induce apoptosis, however the effect of Cys-S₃ on the cellular stress response has not been

SUBMITTER: Switzer CH 

PROVIDER: S-EPMC8497997 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature