Peroxiredoxin (PRDX)

Peroxiredoxins (PRDXs) are a ubiquitous family of antioxidant enzymes that play a fundamental role in maintaining cellular redox homeostasis by catalyzing the reduction of hydrogen peroxide, organic hydroperoxides, and peroxynitrite (UniProt, 2024). They are characterized by a conserved catalytic cysteine residue that undergoes a cycle of oxidation and reduction, often involving thioredoxin as an electron donor (PubMed, PMID: 26903114). Beyond their role as simple scavengers, PRDXs act as critical regulators of redox signaling, modulating pathways involved in cell proliferation, differentiation, and apoptosis (PubMed, PMID: 23919381). In the context of disease, PRDXs are frequently upregulated in various cancers, such as lung and breast cancer, where they provide a survival advantage by protecting malignant cells from oxidative stress-induced damage (PubMed, PMID: 28213286). Consequently, inhibiting PRDX enzymatic function has emerged as a potential therapeutic strategy to sensitize tumor cells to chemotherapy and radiation. Experimental inhibitors like Conoidin A and Adenanthin target the catalytic cysteine to disrupt this enzymatic activity and increase oxidative stress in target cells (PubMed, PMID: 22814341). However, because of their essential role in normal physiology, targeting these enzymes requires careful consideration of potential off-target effects on systemic redox balance and signaling (PubMed, PMID: 30553150).

Other names

PRXThioredoxin peroxidaseTPxAntioxidant enzyme

Inhibition of the catalytic cysteine residue through covalent modification or non-covalent binding, preventing the reduction of peroxides and leading to the accumulation of reactive oxygen species (ROS) (PubMed, PMID: 22814341).