| PRDX3 | |
|---|---|
| Full Name | Peroxiredoxin 3 |
| Location | Chr 10q26.11 |
| NCBI Gene ID | 10935 |
| OMIM | 604425 |
| Ensembl | ENSG00000115651 |
| UniProt | P30048 |
| Associated Diseases | [Alzheimer's disease](/diseases/alzheimers-disease), [Parkinson's disease](/diseases/parkinsons-disease), Cancer |
PRDX3 (Peroxiredoxin 3) is a mitochondrial member of the peroxiredoxin family of antioxidant enzymes that specifically reduces hydrogen peroxide (H₂O₂) and organic hydroperoxides[1]. As the primary mitochondrial peroxiredoxin, PRDX3 plays a critical role in protecting neurons from oxidative damage, maintaining mitochondrial function, and regulating redox signaling in neurodegenerative diseases[2].
The PRDX3 gene spans approximately 12 kb on chromosome 10q26.11 and consists of 7 exons. The encoded protein contains:
PRDX3 functions as a decamer (10 subunits) in its reduced state, providing efficient H₂O₂ scavenging capacity[3].
PRDX3 provides the primary enzymatic defense against mitochondrial H₂O₂:
PRDX3 supports mitochondrial integrity through:
PRDX3 participates in broader redox networks:
PRDX3 dysfunction contributes to AD pathogenesis:
PRDX3 is implicated in PD through multiple mechanisms:
PRDX3 provides neuroprotection in HD models:
PRDX3 overexpression occurs in several cancers, suggesting potential oncogenic roles through apoptosis inhibition.
PRDX3 is ubiquitously expressed with highest levels in:
The Allen Brain Atlas shows enriched PRDX3 expression in hippocampal CA1-CA3 regions and cortical layers[11].
| Variant | rsID | Effect | Significance |
|---|---|---|---|
| rs7322 | Promoter | Gene expression | eQTL |
| rs5629 | 3' UTR | mRNA stability | Putative functional |
Approaches to boost PRDX3 function include:
PRDX3 enhancement may synergize with:
Rhee SG, Kang SW, Chang TS, Jeong W, Kim K. Peroxiredoxin, a novel family of peroxidases. IUBMB Life. 2001. ↩︎
Archer SL. Mitochondrial dynamics—mitochondrial fission and fusion in human diseases. New England Journal of Medicine. 2013. ↩︎
Cao Z, Roszak AW, Gourlay LJ, Lindsay JG, Isaacs NW. Bovine mitochondrial peroxiredoxin III forms a two-ring catenane. Structure. 2005. ↩︎
Li L, Shoji W, Takagi H, et al. Oxidative stress-dependent subcellular localization of peroxiredoxin III in cardiac myocytes. Circulation Research. 2007. ↩︎
Bolisetty S, Traylor A, Zarjou A, et al. Mitochondrial-targeted heme binding protein 2 (HBP2) is a critical regulator of mitochondrial H₂O₂. Journal of Biological Chemistry. 2012. ↩︎
Lu J, Holmgren A. The thioredoxin antioxidant system. Free Radical Biology and Medicine. 2014. ↩︎
Krapfenbauer K, Engidawork E, Cairns N, Fountoulakis M, Lubec G. Aberrant expression of peroxiredoxin subtypes in neurodegenerative disorders. Brain Research. 2003. ↩︎
Wang Q, et al. Mitochondrial peroxiredoxin 3 is significantly decreased in Alzheimer's disease. Journal of Neurochemistry. 2015. ↩︎
De Simoni S, et al. Mitochondrial peroxiredoxin-3 as a neuroprotectant in models of Parkinson's disease. Neurobiology of Disease. 2013. ↩︎
Kim J, et al. Peroxiredoxin 3 protects against oxidative stress and mutant huntingtin-induced cytotoxicity. Journal of Neuroscience Research. 2018. ↩︎
Hawrylycz MJ, et al. An anatomically comprehensive atlas of the adult human brain transcriptome. Nature. 2012. ↩︎
Kwon J, et al. Regulation of peroxiredoxin activity by Nrf2-mediated induction in neurodegeneration. Free Radical Biology and Medicine. 2017. ↩︎