PRDX5 (peroxiredoxin 5) is a thiol-specific peroxidase that serves as a critical antioxidant enzyme, catalyzing the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols 1. The protein exhibits dual subcellular localization: a full-length mitochondrial form (24 kDa) targeted by its N-terminal 50 amino acids, and a shorter cytoplasmic/nuclear form (17 kDa) translated from the second AUG codon 1. PRDX5's antioxidant activity is regulated by S-palmitoylation at its nucleophilic active site residue Cys100, which is controlled by the mitochondrial depalmitoylase ABHD10 23. The gene's high basal expression is coordinated with mitochondrial biogenesis through nuclear respiratory factors NFR-1 and GABPA 1. Disease relevance includes roles in dilated cardiomyopathy, where NDUFS2 exon skipping competitively inhibits PRDX5's antioxidant activity 4, alopecia areata susceptibility 5, and castration-resistant prostate cancer progression through promoting drug-tolerant persister cell survival 67. In chr11 prostatitis, PRDX5 promotes M1 macrophage polarization via the TLR4/NF-κB pathway, contributing to prostate epithelial cell apoptosis 8. Therapeutically, PRDX5 represents a promising target for cancer treatment, with inhibitors like stachyose showing efficacy in suppressing castration-resistant prostate cancer 7.