{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPeroxiredoxin‐2 (PRDX2) is a highly abundant, thiol‐dependent peroxidase that rapidly reduces hydrogen peroxide and organic hydroperoxides, thereby protecting cells from oxidative damage. Its exceptional kinetic reactivity, documented in erythrocytes and other cell types, enables efficient peroxide scavenging while its oligomeric organization (dimer/decamer equilibrium) is crucial for its rapid peroxidase activity. PRDX2 also participates in reversible post‐translational modifications such as glutathionylation—which can be reversed by glutaredoxin—and its sensitivity to hyperoxidation is regulated by specific molecular determinants. These characteristics collectively underscore its fundamental role in antioxidant defense and maintenance of redox homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its peroxidase function, PRDX2 plays an important role in redox signaling and cell‐regulatory processes. Under conditions of oxidative stress, its catalytic cysteine residues can become hyperoxidized or modified through S‐nitrosylation and acetylation—thereby altering its activity and participation in signal transduction pathways. For example, modified extracellular or nuclear forms of PRDX2 help modulate inflammatory responses (by stimulating cytokine release) or protect vulnerable signaling receptors (such as VEGFR2) and DNA repair systems in cancer cells. Moreover, in certain myeloid and glioma cells, proper maintenance of PRDX2 activity is implicated in cell cycle regulation and survival, while its targeted inhibition (by agents such as Celastrol) can trigger redox‐dependent apoptosis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nClinically, alterations in PRDX2 expression and regulation have been linked to a broad spectrum of human diseases. In neurodegenerative disorders such as Alzheimer’s and Parkinson’s disease—as well as in Down syndrome—the dysregulated levels or post‐translational modifications of PRDX2 appear to contribute to neuronal vulnerability. In inflammatory conditions (e.g. psoriasis) and a variety of cancers (including gastric, colorectal, breast, and acute myeloid leukemia), aberrant PRDX2 expression correlates with tumor progression, metastasis, and therapy resistance. In erythrocytes, PRDX2 not only protects hemoglobin and membrane proteins from oxidative denaturation but also plays a structural role through interactions with Band 3, while in placental trophoblasts its loss is associated with increased apoptosis linked to recurrent miscarriage. Intriguingly, even pathogens such as Plasmodium falciparum exploit host PRDX2 to bolster their own antioxidant defenses. 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