The Eye Lens Protein, γS Crystallin, Undergoes Glutathionylation-Induced Disulfide Bonding Between Cysteines 22 and 26.

ABSTRACT: The oxidation of cysteines in crystallins is a major age-related modification associated with cataract formation. The purpose of this research was to determine the susceptibility of γS-crystallin to glutathionylation-induced oxidation and disulfide bond formation. Recombinantly expressed wild-type human γS-crystallin and four cysteine-to-serine mutants were reduced and incubated for up to 2 days with oxidized glutathione. Following incubation and alkylation, the overall degree of glutathionylation and disulfide bond formation were determined by whole-mass measurement. Tryptic digests were also analyzed by LC-MS/MS to identify specific sites of S-glutathionylation and disulfide linkages. We determined that C22, C24, and C26 undergo glutathione-mediated disulfide interchange with each other,

SUBMITTER: Halverson-Kolkind K 

PROVIDER: S-EPMC11940727 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature