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Gene Review

PRDX3  -  peroxiredoxin 3

Homo sapiens

Synonyms: AOP-1, AOP1, Antioxidant protein 1, HBC189, MER5, ...
 
 
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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].

References

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  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]
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  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]
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  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]
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