Peroxiredoxin-4 (PRDX4)

Peroxiredoxin-4 (PRDX4) is an endoplasmic reticulum-localized antioxidant enzyme of the peroxiredoxin family, classified as a typical 2-Cys peroxiredoxin and oxidoreductase[1][3][4]. It functions by reducing hydrogen peroxide and other hydroperoxides to water and alcohol, using reducing equivalents from thiol-containing donors such as thioredoxin, thereby protecting cells from oxidative damage and modulating redox signaling. PRDX4 also couples hydrogen peroxide catabolism with the formation of disulfide bonds during the oxidative folding of nascent proteins in the ER, thereby ensuring protein quality control and maintenance of ER homeostasis[2][4]. It can regulate the activation of the transcription factor NF-kappaB and plays roles in cell survival, apoptosis, and signal transduction. Dysregulation or altered expression of PRDX4 is linked to various disease processes, notably cancer, metabolic and inflammatory diseases, and reproductive aging[4][5]. PRDX4 is being investigated as a diagnostic and prognostic biomarker in multiple pathological contexts, but currently there are no drugs that specifically and directly target this enzyme in clinical use.

Other names

Peroxiredoxin IVPrx-IVAOE37-2Antioxidant enzyme AOE372Thioredoxin peroxidase AO372Thioredoxin-dependent peroxide reductase A0372Thioredoxin-dependent peroxiredoxin 4HEL-S-97nPRX-4epididymis secretory sperm binding protein Li 97nprx-IV

Drugs targeting PRDX4 would theoretically act by modulating its peroxidase activity, influencing redox balance, or affecting protein folding and stress responses; specific approved drugs modulating PRDX4 directly are not currently established.