The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

PRDX3  -  peroxiredoxin 3

Homo sapiens

Synonyms: AOP-1, AOP1, Antioxidant protein 1, HBC189, MER5, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of PRDX3


Psychiatry related information on PRDX3


High impact information on PRDX3


Chemical compound and disease context of PRDX3


Biological context of PRDX3


Anatomical context of PRDX3


Associations of PRDX3 with chemical compounds


Physical interactions of PRDX3

  • In KD clones, but not in RD-clones, formation of etoposide-induced gamma-H2AX was increased, indicating that PrxV inhibits conversion of topoisomerase II cleavage complexes into double-strand DNA breaks but this inhibition is not caused by its antioxidant activity [26].
  • We also provided evidence that LZK was associated directly with the IKK complex through the kinase domain, and that AOP-1 was recruited to the IKK complex through the binding to LZK [31].
  • Haptoglobin polymorphisms result in proteins with altered haemoglobin-binding capacity and different antioxidant, iron-recycling, and immune functions [32].
  • Wild-type but not G546R mutant FANCG physically interacts with the mitochondrial peroxidase peroxiredoxin-3 (PRDX3) [33].
  • HAH1 is a copper-binding protein with distinct amino acid residues mediating copper homeostasis and antioxidant defense [34].

Enzymatic interactions of PRDX3


Co-localisations of PRDX3


Regulatory relationships of PRDX3


Other interactions of PRDX3

  • The DNA microarray data for PRDX1 and PRDX3 were reproduced by reverse transcription-PCR analysis [45].
  • Antioxidant proteins in fetal brain: superoxide dismutase-1 (SOD-1) protein is not overexpressed in fetal Down syndrome [46].
  • RPK118, a PX domain-containing protein, interacts with peroxiredoxin-3 through pseudo-kinase domains [23].
  • Together, these data strongly suggest that AOP2 is a novel thiol-dependent antioxidant that functions to scavenge particular hydroperoxides in the cell and mediate specific signals [47].
  • This review discusses Srx as a novel antioxidant, and focuses on its potential role in the regulation of glutathionylation/deglutathionylation pathways, that have been implicated in a growing number of disease states [48].

Analytical, diagnostic and therapeutic context of PRDX3

  • To examine this view, we investigated the expression of thirteen different proteins involved in the cellular antioxidant defense system in brains of control and DS fetuses by two-dimensional electrophoresis (2-DE) coupled with matrix-assisted laser desorption/ionization mass spectroscopy (MALDI-MS) [46].
  • Peroxiredoxins (Prx) have recently moved into the focus of plant and animal research in the context of development, adaptation, and disease, as they function both in antioxidant defense by reducing a broad range of toxic peroxides and in redox signaling relating to the adjustment of cell redox and antioxidant metabolism [49].
  • These results demonstrate that the NKEF-B is an antioxidant that protects cells from oxidative stress, chemotherapy agents, and inflammation-induced monocyte adhesion [50].
  • Immunohistochemistry of placental tissues showed that the levels of peroxiredoxin III/SP-22 protein were increased in the trophoblasts of floating villi, stromal cells of stem villi, and decidual cells in pre-eclamptic placentae [51].
  • In this study, we examined the expression of an antioxidant defense gene, nkef, in human tissue and isolated populations of rat brain cells using Western and Northern blot analysis [52].


  1. Peroxiredoxin 2 (PRDX2), an antioxidant enzyme, is under-expressed in Down syndrome fetal brains. Sánchez-Font, M.F., Sebastià, J., Sanfeliu, C., Cristòfol, R., Marfany, G., Gonzàlez-Duarte, R. Cell. Mol. Life Sci. (2003) [Pubmed]
  2. Nonredundant antioxidant defense by multiple two-cysteine peroxiredoxins in human prostate cancer cells. Shen, C., Nathan, C. Mol. Med. (2002) [Pubmed]
  3. Thioredoxin reductase in human hepatoma cells is transcriptionally regulated by sulforaphane and other electrophiles via an antioxidant response element. Hintze, K.J., Wald, K.A., Zeng, H., Jeffery, E.H., Finley, J.W. J. Nutr. (2003) [Pubmed]
  4. Neutrophil tolerance to oxidative stress induced by hypoxia/reoxygenation. Sureda, A., Batle, J.M., Tauler, P., Cases, N., Aguiló, A., Tur, J.A., Pons, A. Free Radic. Res. (2004) [Pubmed]
  5. Tagging single-nucleotide polymorphisms in antioxidant defense enzymes and susceptibility to breast cancer. Cebrian, A., Pharoah, P.D., Ahmed, S., Smith, P.L., Luccarini, C., Luben, R., Redman, K., Munday, H., Easton, D.F., Dunning, A.M., Ponder, B.A. Cancer Res. (2006) [Pubmed]
  6. Enzyme-linked immunospot assay for detection of thioredoxin and thioredoxin reductase secretion from cells. Sahaf, B., Söderberg, A., Ekerfelt, C., Paulie, S., Rosén, A. Meth. Enzymol. (2002) [Pubmed]
  7. Modification of brain aging and neurodegenerative disorders by genes, diet, and behavior. Mattson, M.P., Chan, S.L., Duan, W. Physiol. Rev. (2002) [Pubmed]
  8. Dietary habits and their relations to insulin resistance and postprandial lipemia in nonalcoholic steatohepatitis. Musso, G., Gambino, R., De Michieli, F., Cassader, M., Rizzetto, M., Durazzo, M., Fagà, E., Silli, B., Pagano, G. Hepatology (2003) [Pubmed]
  9. Evidence of oxidative stress and in vivo neurotoxicity of beta-amyloid in a transgenic mouse model of Alzheimer's disease: a chronic oxidative paradigm for testing antioxidant therapies in vivo. Pappolla, M.A., Chyan, Y.J., Omar, R.A., Hsiao, K., Perry, G., Smith, M.A., Bozner, P. Am. J. Pathol. (1998) [Pubmed]
  10. HIV-dementia, Tat-induced oxidative stress, and antioxidant therapeutic considerations. Pocernich, C.B., Sultana, R., Mohmmad-Abdul, H., Nath, A., Butterfield, D.A. Brain Res. Brain Res. Rev. (2005) [Pubmed]
  11. Reactive oxygen species promote TNFalpha-induced death and sustained JNK activation by inhibiting MAP kinase phosphatases. Kamata, H., Honda, S., Maeda, S., Chang, L., Hirata, H., Karin, M. Cell (2005) [Pubmed]
  12. Simvastatin and niacin, antioxidant vitamins, or the combination for the prevention of coronary disease. Brown, B.G., Zhao, X.Q., Chait, A., Fisher, L.D., Cheung, M.C., Morse, J.S., Dowdy, A.A., Marino, E.K., Bolson, E.L., Alaupovic, P., Frohlich, J., Albers, J.J. N. Engl. J. Med. (2001) [Pubmed]
  13. Prevention of radiographic-contrast-agent-induced reductions in renal function by acetylcysteine. Tepel, M., van der Giet, M., Schwarzfeld, C., Laufer, U., Liermann, D., Zidek, W. N. Engl. J. Med. (2000) [Pubmed]
  14. Additive apoptotic effect of STI571 with the cytoprotective agent amifostine in K-562 cell line. Vellón, L., González-Cid, M., Nebel, M.d.e. .C., Larripa, I. Cancer Chemother. Pharmacol. (2005) [Pubmed]
  15. Oxidants downstream from superoxide inhibit nitric oxide production by vascular endothelium--a key role for selenium-dependent enzymes in vascular health. McCarty, M.F. Med. Hypotheses (1999) [Pubmed]
  16. A novel copper complex induces ROS generation in doxorubicin resistant Ehrlich ascitis carcinoma cells and increases activity of antioxidant enzymes in vital organs in vivo. Mookerjee, A., Basu, J.M., Majumder, S., Chatterjee, S., Panda, G.S., Dutta, P., Pal, S., Mukherjee, P., Efferth, T., Roy, S., Choudhuri, S.K. BMC Cancer (2006) [Pubmed]
  17. Vitamin E consumption and the risk of coronary disease in women. Stampfer, M.J., Hennekens, C.H., Manson, J.E., Colditz, G.A., Rosner, B., Willett, W.C. N. Engl. J. Med. (1993) [Pubmed]
  18. Impairment of endothelial functions by acute hyperhomocysteinemia and reversal by antioxidant vitamins. Nappo, F., De Rosa, N., Marfella, R., De Lucia, D., Ingrosso, D., Perna, A.F., Farzati, B., Giugliano, D. JAMA (1999) [Pubmed]
  19. The c-Myc target gene PRDX3 is required for mitochondrial homeostasis and neoplastic transformation. Wonsey, D.R., Zeller, K.I., Dang, C.V. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  20. Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family. Knoops, B., Clippe, A., Bogard, C., Arsalane, K., Wattiez, R., Hermans, C., Duconseille, E., Falmagne, P., Bernard, A. J. Biol. Chem. (1999) [Pubmed]
  21. Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 A resolution. Declercq, J.P., Evrard, C., Clippe, A., Stricht, D.V., Bernard, A., Knoops, B. J. Mol. Biol. (2001) [Pubmed]
  22. PRDX4, a member of the peroxiredoxin family, is fused to AML1 (RUNX1) in an acute myeloid leukemia patient with a t(X;21)(p22;q22). Zhang, Y., Emmanuel, N., Kamboj, G., Chen, J., Shurafa, M., Van Dyke, D.L., Wiktor, A., Rowley, J.D. Genes Chromosomes Cancer (2004) [Pubmed]
  23. RPK118, a PX domain-containing protein, interacts with peroxiredoxin-3 through pseudo-kinase domains. Liu, L., Yang, C., Yuan, J., Chen, X., Xu, J., Wei, Y., Yang, J., Lin, G., Yu, L. Mol. Cells (2005) [Pubmed]
  24. Peroxiredoxin V is essential for protection against apoptosis in human lung carcinoma cells. Kropotov, A., Gogvadze, V., Shupliakov, O., Tomilin, N., Serikov, V.B., Tomilin, N.V., Zhivotovsky, B. Exp. Cell Res. (2006) [Pubmed]
  25. Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism. Manevich, Y., Fisher, A.B. Free Radic. Biol. Med. (2005) [Pubmed]
  26. Downregulation of peroxiredoxin V stimulates formation of etoposide-induced double-strand DNA breaks. Kropotov, A.V., Grudinkin, P.S., Pleskach, N.M., Gavrilov, B.A., Tomilin, N.V., Zhivotovsky, B. FEBS Lett. (2004) [Pubmed]
  27. Purification and characterization of thiol-specific antioxidant protein from human red blood cell: a new type of antioxidant protein. Lim, Y.S., Cha, M.K., Yun, C.H., Kim, H.K., Kim, K., Kim, I.H. Biochem. Biophys. Res. Commun. (1994) [Pubmed]
  28. Cloning and sequencing of thiol-specific antioxidant from mammalian brain: alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Chae, H.Z., Robison, K., Poole, L.B., Church, G., Storz, G., Rhee, S.G. Proc. Natl. Acad. Sci. U.S.A. (1994) [Pubmed]
  29. Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Rhee, S.G., Chae, H.Z., Kim, K. Free Radic. Biol. Med. (2005) [Pubmed]
  30. SP-22 is a thioredoxin-dependent peroxide reductase in mitochondria. Watabe, S., Hiroi, T., Yamamoto, Y., Fujioka, Y., Hasegawa, H., Yago, N., Takahashi, S.Y. Eur. J. Biochem. (1997) [Pubmed]
  31. Mixed lineage kinase LZK and antioxidant protein-1 activate NF-kappaB synergistically. Masaki, M., Ikeda, A., Shiraki, E., Oka, S., Kawasaki, T. Eur. J. Biochem. (2003) [Pubmed]
  32. Seasonal childhood anaemia in West Africa is associated with the haptoglobin 2-2 genotype. Atkinson, S.H., Rockett, K., Sirugo, G., Bejon, P.A., Fulford, A., O'Connell, M.A., Bailey, R., Kwiatkowski, D.P., Prentice, A.M. PLoS Med. (2006) [Pubmed]
  33. Defective mitochondrial peroxiredoxin-3 results in sensitivity to oxidative stress in Fanconi anemia. Mukhopadhyay, S.S., Leung, K.S., Hicks, M.J., Hastings, P.J., Youssoufian, H., Plon, S.E. J. Cell Biol. (2006) [Pubmed]
  34. HAH1 is a copper-binding protein with distinct amino acid residues mediating copper homeostasis and antioxidant defense. Hung, I.H., Casareno, R.L., Labesse, G., Mathews, F.S., Gitlin, J.D. J. Biol. Chem. (1998) [Pubmed]
  35. Efficient reduction of lipoamide and lipoic acid by mammalian thioredoxin reductase. Arnér, E.S., Nordberg, J., Holmgren, A. Biochem. Biophys. Res. Commun. (1996) [Pubmed]
  36. Noncovalent Interaction Between Amyloid-beta-Peptide (1-40) and Oleuropein Studied by Electrospray Ionization Mass Spectrometry. Bazoti, F.N., Bergquist, J., Markides, K.E., Tsarbopoulos, A. J. Am. Soc. Mass Spectrom. (2006) [Pubmed]
  37. Kinetic and mechanistic studies of the reactions of nitrogen monoxide and nitrite with ferryl myoglobin. Herold, S., Rehmann, F.J. J. Biol. Inorg. Chem. (2001) [Pubmed]
  38. A second look into the oxidant mechanisms in Alzheimer's disease. Moreira, P.I., Oliveira, C.R., Santos, M.S., Nunomura, A., Honda, K., Zhu, X., Smith, M.A., Perry, G. Current neurovascular research. (2005) [Pubmed]
  39. Oxidation of plasma alpha 1-antitrypsin in smokers and nonsmokers and by an oxidizing agent. Cox, D.W., Billingsley, G.D. Am. Rev. Respir. Dis. (1984) [Pubmed]
  40. Regional NAD(P)H:quinone oxidoreductase activity in Alzheimer's disease. SantaCruz, K.S., Yazlovitskaya, E., Collins, J., Johnson, J., DeCarli, C. Neurobiol. Aging (2004) [Pubmed]
  41. Thioredoxin induced antioxidant gene expressions in human lens epithelial cells. Yegorova, S., Yegorov, O., Lou, M.F. Exp. Eye Res. (2006) [Pubmed]
  42. Peroxiredoxin 5 expression in the human thyroid gland. Gérard, A.C., Many, M.C., Daumerie, C.h., Knoops, B., Colin, I.M. Thyroid (2005) [Pubmed]
  43. Antioxidant enzymes in renal cell carcinoma. Soini, Y., Kallio, J.P., Hirvikoski, P., Helin, H., Kellokumpu-Lehtinen, P., Tammela, T.L., Peltoniemi, M., Martikainen, P.M., Kinnula, L.V. Histol. Histopathol. (2006) [Pubmed]
  44. Vascular cell adhesion molecule-1 (VCAM-1) gene transcription and expression are regulated through an antioxidant-sensitive mechanism in human vascular endothelial cells. Marui, N., Offermann, M.K., Swerlick, R., Kunsch, C., Rosen, C.A., Ahmad, M., Alexander, R.W., Medford, R.M. J. Clin. Invest. (1993) [Pubmed]
  45. Sex-based molecular profiling of hepatitis C virus-related hepatocellular carcinoma. Takemoto, N., Iizuka, N., Yamada-Okabe, H., Hamada, K., Tamesa, T., Okada, T., Hashimoto, K., Sakamoto, K., Takashima, M., Miyamoto, T., Uchimura, S., Hamamoto, Y., Oka, M. Int. J. Oncol. (2005) [Pubmed]
  46. Antioxidant proteins in fetal brain: superoxide dismutase-1 (SOD-1) protein is not overexpressed in fetal Down syndrome. Gulesserian, T., Engidawork, E., Fountoulakis, M., Lubec, G. J. Neural Transm. Suppl. (2001) [Pubmed]
  47. AOP2 (antioxidant protein 2): structure and function of a unique thiol-specific antioxidant. Phelan, S.A. Antioxid. Redox Signal. (1999) [Pubmed]
  48. Sulfiredoxin: a potential therapeutic agent? Findlay, V.J., Tapiero, H., Townsend, D.M. Biomed. Pharmacother. (2005) [Pubmed]
  49. The mitochondrial type II peroxiredoxin F is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress. Finkemeier, I., Goodman, M., Lamkemeyer, P., Kandlbinder, A., Sweetlove, L.J., Dietz, K.J. J. Biol. Chem. (2005) [Pubmed]
  50. Endogenous natural killer enhancing factor-B increases cellular resistance to oxidative stresses. Shau, H., Kim, A.T., Hedrick, C.C., Lusis, A.J., Tompkins, C., Finney, R., Leung, D.W., Paglia, D.E. Free Radic. Biol. Med. (1997) [Pubmed]
  51. Enhancement of mitochondrial oxidative stress and up-regulation of antioxidant protein peroxiredoxin III/SP-22 in the mitochondria of human pre-eclamptic placentae. Shibata, E., Nanri, H., Ejima, K., Araki, M., Fukuda, J., Yoshimura, K., Toki, N., Ikeda, M., Kashimura, M. Placenta (2003) [Pubmed]
  52. Expression of the antioxidant gene NKEF in the central nervous system. Sarafian, T.A., Huang, C., Kim, A., de Vellis, J., Shau, H. Mol. Chem. Neuropathol. (1998) [Pubmed]
WikiGenes - Universities