{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nPeroxiredoxin‐3 (PRDX3) is a mitochondrion‐localized thiol peroxidase that plays a central role in detoxifying hydrogen peroxide and maintaining redox homeostasis. Detailed kinetic analyses have shown that PRDX3 reacts rapidly with H₂O₂—its active‐site features (including conserved arginine residues) and higher‐order oligomerization together enhance its peroxidase activity. Together with mitochondrial thioredoxin (and even glutaredoxin) systems, PRDX3 ensures efficient elimination of reactive oxygen species, while its resistance to hyperoxidation and subsequent reactivation by sulfiredoxin preserves mitochondrial integrity even under conditions of oxidative stress."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "12"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn various cancer models, PRDX3 has been implicated as a key mediator of mitochondrial function and cell proliferation. It is transcriptionally regulated by oncogenes such as c‐Myc and factors including FOXM1, and its expression is modulated by microRNAs and post‐translational mechanisms (for example, via ubiquitin ligase–mediated degradation). In cancers ranging from hepatocellular and cervical to breast and prostate malignancies—and even in renal cell carcinoma via a circRNA/miRNA axis—elevated or deregulated PRDX3 expression contributes to the maintenance of mitochondrial mass, supports bioenergetic homeostasis, and can promote chemoresistance."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in proliferation, PRDX3 is critical for cellular resilience against oxidative and apoptotic stress. In cardiac fibroblasts, neuronal cells, and various in vitro or in vivo models, proper PRDX3 activity safeguards mitochondrial integrity, helps regulate ATP production, and prevents the activation of pro‐apoptotic signaling pathways. Conversely, diminished or dysfunctional PRDX3—whether due to genetic silencing, interference by dominant‐negative proteins, or post‐translational modifications—leads to enhanced mitochondrial damage, cell cycle arrest, and even accelerated aging phenotypes, as evidenced in models of osteoarthritis and muscle degeneration. Such findings underscore the importance of PRDX3 in coupling mitochondrial dynamics with redox-sensitive cell signaling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "27", "end_ref": "39"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nAltered expression of PRDX3 is also observed in other pathophysiological contexts, including ocular and autoimmune conditions. Changes in PRDX3 levels in the corneal endothelium and in patients with certain retinal or inflammatory syndromes highlight the broad physiological relevance of PRDX3 in protecting diverse tissues from oxidative injury."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "40"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Thierry Rabilloud, Manfred Heller, Francoise Gasnier, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Proteomics analysis of cellular response to oxidative stress. 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