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

PRDX5  -  peroxiredoxin 5

Homo sapiens

Synonyms: ACR1, AOEB166, Alu corepressor 1, Antioxidant enzyme B166, B166, ...
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 PRDX5


Psychiatry related information on PRDX5


High impact information on PRDX5

  • Recent studies with a human adenocarcinoma cell line led to the unexpected discovery that selenocysteine occurs in mammalian thioredoxin reductase [7].
  • Defective metabolism of pyridoxal 5'-phosphate (PLP), characterized by elevated serum PLP levels, results in reduced levels of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) in the brain [8].
  • The accumulating P6C inactivates pyridoxal 5'-phosphate (PLP) by forming a Knoevenagel condensation product [9].
  • MAIN OUTCOME MEASURES--Plasma homocysteine concentration correlated with plasma folate, vitamin B12, pyridoxal-5'-phosphate (PLP), and oral intakes of these vitamins, and the contribution of these vitamins to the prevalence of elevated homocysteine in the population [10].
  • Homocysteine demonstrated weaker, inverse associations with plasma vitamin B12 and PLP [10].

Chemical compound and disease context of PRDX5


Biological context of PRDX5


Anatomical context of PRDX5


Associations of PRDX5 with chemical compounds

  • In the reduced form of PRDX5, Cys47 and Cys151 are distant of 13.8 A although these two cysteine residues are thought to be involved in peroxide reductase activity by forming an intramolecular disulfide intermediate in the oxidized enzyme [15].
  • Systemically administered recombinant PRDX5 provided protection against ibotenate-induced excitotoxic stress [20].
  • Two classical antioxidants, N-acetylcysteine and catalase-PEG, provided the same neuroprotective effect as PRDX5 [20].
  • The possible role of benzoate in the antioxidant activity of PRDX5 is discussed [15].
  • Recombinant PRDX5 plus dithiothreitol displayed a synergistic neuroprotective effect on NMDA-induced neuronal death [20].

Physical interactions of PRDX5

  • 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 [21].

Regulatory relationships of PRDX5

  • In conclusion, our data show that PRDX5 is expressed in the thyroid gland where it could act as antioxidant [1].
  • Bacterially expressed ACR1 is demonstrated to inhibit RNA polymerase III (Pol III)-dependent Alu transcription in vitro but showed no repression of transcription of a tRNA gene or of a reporter gene under control of a Pol II promoter [22].

Other interactions of PRDX5


Analytical, diagnostic and therapeutic context of PRDX5


  1. 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]
  2. 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]
  3. Expression and regulation of peroxiredoxin 5 in human osteoarthritis. Wang, M.X., Wei, A., Yuan, J., Trickett, A., Knoops, B., Murrell, G.A. FEBS Lett. (2002) [Pubmed]
  4. New aspects in the pathophysiology of cutaneous melanoma: a review of the role of thioproteins and the effect of nitrosoureas. Schallreuter, K.U., Wood, J.M. Melanoma Res. (1991) [Pubmed]
  5. Decreased thioredoxin and increased thioredoxin reductase levels in Alzheimer's disease brain. Lovell, M.A., Xie, C., Gabbita, S.P., Markesbery, W.R. Free Radic. Biol. Med. (2000) [Pubmed]
  6. Influence of lifestyle on vitamin bioavailability. van den Berg, H., van der Gaag, M., Hendriks, H. International journal for vitamin and nutrition research. Internationale Zeitschrift für Vitamin- und Ernährungsforschung. Journal international de vitaminologie et de nutrition. (2002) [Pubmed]
  7. Discoveries of vitamin B12 and selenium enzymes. Stadtman, T.C. Annu. Rev. Biochem. (2002) [Pubmed]
  8. Mice lacking tissue non-specific alkaline phosphatase die from seizures due to defective metabolism of vitamin B-6. Waymire, K.G., Mahuren, J.D., Jaje, J.M., Guilarte, T.R., Coburn, S.P., MacGregor, G.R. Nat. Genet. (1995) [Pubmed]
  9. Mutations in antiquitin in individuals with pyridoxine-dependent seizures. Mills, P.B., Struys, E., Jakobs, C., Plecko, B., Baxter, P., Baumgartner, M., Willemsen, M.A., Omran, H., Tacke, U., Uhlenberg, B., Weschke, B., Clayton, P.T. Nat. Med. (2006) [Pubmed]
  10. Vitamin status and intake as primary determinants of homocysteinemia in an elderly population. Selhub, J., Jacques, P.F., Wilson, P.W., Rush, D., Rosenberg, I.H. JAMA (1993) [Pubmed]
  11. Expression of antioxidant enzymes in astrocytic brain tumors. Haapasalo, H., Kyläniemi, M., Paunul, N., Kinnula, V.L., Soini, Y. Brain Pathol. (2003) [Pubmed]
  12. Thioredoxin reductase is the major selenoprotein expressed in human umbilical-vein endothelial cells and is regulated by protein kinase C. Anema, S.M., Walker, S.W., Howie, A.F., Arthur, J.R., Nicol, F., Beckett, G.J. Biochem. J. (1999) [Pubmed]
  13. 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]
  14. The stereospecific suicide inhibition of human melanoma thioredoxin reductase by 13-cis-retinoic acid. Schallreuter, K.U., Wood, J.M. Biochem. Biophys. Res. Commun. (1989) [Pubmed]
  15. 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]
  16. Overexpression of antioxidant enzyme peroxiredoxin 5 protects human tendon cells against apoptosis and loss of cellular function during oxidative stress. Yuan, J., Murrell, G.A., Trickett, A., Landtmeters, M., Knoops, B., Wang, M.X. Biochim. Biophys. Acta (2004) [Pubmed]
  17. Thioredoxin reductase - its role in epidermal redox status. Schallreuter, K.U., Wood, J.M. J. Photochem. Photobiol. B, Biol. (2001) [Pubmed]
  18. Antioxidant enzyme peroxiredoxin 5 is upregulated in degenerative human tendon. Wang, M.X., Wei, A., Yuan, J., Clippe, A., Bernard, A., Knoops, B., Murrell, G.A. Biochem. Biophys. Res. Commun. (2001) [Pubmed]
  19. Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate. Seo, M.S., Kang, S.W., Kim, K., Baines, I.C., Lee, T.H., Rhee, S.G. J. Biol. Chem. (2000) [Pubmed]
  20. Recombinant peroxiredoxin 5 protects against excitotoxic brain lesions in newborn mice. Plaisant, F., Clippe, A., Vander Stricht, D., Knoops, B., Gressens, P. Free Radic. Biol. Med. (2003) [Pubmed]
  21. 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]
  22. A novel human DNA-binding protein with sequence similarity to a subfamily of redox proteins which is able to repress RNA-polymerase-III-driven transcription of the Alu-family retroposons in vitro. Kropotov, A., Sedova, V., Ivanov, V., Sazeeva, N., Tomilin, A., Krutilina, R., Oei, S.L., Griesenbeck, J., Buchlow, G., Tomilin, N. Eur. J. Biochem. (1999) [Pubmed]
  23. Immunogenicity without immunoselection: a mutant but functional antioxidant enzyme retained in a human metastatic melanoma and targeted by CD8(+) T cells with a memory phenotype. Sensi, M., Nicolini, G., Zanon, M., Colombo, C., Molla, A., Bersani, I., Lupetti, R., Parmiani, G., Anichini, A. Cancer Res. (2005) [Pubmed]
  24. Inverse mRNA expression of the selenocysteine-containing proteins GI-GPx and SeP in colorectal adenomas compared with adjacent normal mucosa. Mörk, H., al-Taie, O.H., Bähr, K., Zierer, A., Beck, C., Scheurlen, M., Jakob, F., Köhrle, J. Nutrition and cancer. (2000) [Pubmed]
  25. Human peroxiredoxin 5 is a peroxynitrite reductase. Dubuisson, M., Vander Stricht, D., Clippe, A., Etienne, F., Nauser, T., Kissner, R., Koppenol, W.H., Rees, J.F., Knoops, B. FEBS Lett. (2004) [Pubmed]
  26. Cigarette smoke extract inhibits expression of peroxiredoxin v and increases airway epithelial permeability. Serikov, V.B., Leutenegger, C., Krutilina, R., Kropotov, A., Pleskach, N., Suh, J.H., Tomilin, N.V. Inhalation toxicology. (2006) [Pubmed]
  27. Antioxidant function of thioredoxin and glutaredoxin systems. Holmgren, A. Antioxid. Redox Signal. (2000) [Pubmed]
WikiGenes - Universities