Peroxiredoxin 1

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Peroxiredoxin 1
PDB rendering based on 1qq2.
Available structures: 1qq2
Identifiers
Symbol(s) PRDX1; MSP23; NKEFA; PAG; PAGA; PAGB; TDPX2
External IDs OMIM: 176763 MGI: 99523 HomoloGene: 21685
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 5052 18477
Ensembl ENSG00000117450 ENSMUSG00000028691
Uniprot Q06830 Q3U9J9
Refseq NM_002574 (mRNA)
NP_002565 (protein)		 NM_011034 (mRNA)
NP_035164 (protein)
Location Chr 1: 45.75 - 45.76 Mb Chr 4: 116.18 - 116.2 Mb
Pubmed search [1] [2]

Peroxiredoxin 1, also known as PRDX1, is a human gene.[1]

This gene encodes a member of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. The encoded protein may play an antioxidant protective role in cells, and may contribute to the antiviral activity of CD8(+) T-cells. This protein may have a proliferative effect and play a role in cancer development or progression. Three transcript variants encoding the same protein have been identified for this gene.[1]

[edit] References

  1. ^ a b Entrez Gene: PRDX1 peroxiredoxin 1.

[edit] Further reading

  • Wood ZA, Schröder E, Robin Harris J, Poole LB (2003). "Structure, mechanism and regulation of peroxiredoxins.". Trends Biochem. Sci. 28 (1): 32–40. PMID 12517450. 
  • Sauri H, Butterfield L, Kim A, Shau H (1995). "Antioxidant function of recombinant human natural killer enhancing factor.". Biochem. Biophys. Res. Commun. 208 (3): 964–9. PMID 7702627. 
  • Shau H, Butterfield LH, Chiu R, Kim A (1994). "Cloning and sequence analysis of candidate human natural killer-enhancing factor genes.". Immunogenetics 40 (2): 129–34. PMID 8026862. 
  • Kawai S, Takeshita S, Okazaki M, et al. (1994). "Cloning and characterization of OSF-3, a new member of the MER5 family, expressed in mouse osteoblastic cells.". J. Biochem. 115 (4): 641–3. PMID 8089076. 
  • Shau H, Kim A (1994). "Identification of natural killer enhancing factor as a major antioxidant in human red blood cells.". Biochem. Biophys. Res. Commun. 199 (1): 83–8. PMID 8123050. 
  • Prospéri MT, Apiou F, Dutrillaux B, Goubin G (1994). "Organization and chromosomal assignment of two human PAG gene loci: PAGA encoding a functional gene and PAGB a processed pseudogene.". Genomics 19 (2): 236–41. doi:10.1006/geno.1994.1053. PMID 8188254. 
  • Prospéri MT, Ferbus D, Karczinski I, Goubin G (1993). "A human cDNA corresponding to a gene overexpressed during cell proliferation encodes a product sharing homology with amoebic and bacterial proteins.". J. Biol. Chem. 268 (15): 11050–6. PMID 8496166. 
  • Wen ST, Van Etten RA (1997). "The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity.". Genes Dev. 11 (19): 2456–67. PMID 9334312. 
  • Jin DY, Chae HZ, Rhee SG, Jeang KT (1998). "Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation.". J. Biol. Chem. 272 (49): 30952–61. PMID 9388242. 
  • Outinen PA, Sood SK, Pfeifer SI, et al. (1999). "Homocysteine-induced endoplasmic reticulum stress and growth arrest leads to specific changes in gene expression in human vascular endothelial cells.". Blood 94 (3): 959–67. PMID 10419887. 
  • Yanagawa T, Ishikawa T, Ishii T, et al. (1999). "Peroxiredoxin I expression in human thyroid tumors.". Cancer Lett. 145 (1-2): 127–32. PMID 10530780. 
  • Noh DY, Ahn SJ, Lee RA, et al. (2001). "Overexpression of peroxiredoxin in human breast cancer.". Anticancer Res. 21 (3B): 2085–90. PMID 11497302. 
  • Xu XR, Huang J, Xu ZG, et al. (2002). "Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver.". Proc. Natl. Acad. Sci. U.S.A. 98 (26): 15089–94. doi:10.1073/pnas.241522398. PMID 11752456. 
  • Kim SH, Fountoulakis M, Cairns N, Lubec G (2002). "Protein levels of human peroxiredoxin subtypes in brains of patients with Alzheimer's disease and Down syndrome.". J. Neural Transm. Suppl. (61): 223–35. PMID 11771746. 
  • Rabilloud T, Heller M, Gasnier F, et al. (2002). "Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site.". J. Biol. Chem. 277 (22): 19396–401. doi:10.1074/jbc.M106585200. PMID 11904290. 
  • Chang TS, Jeong W, Choi SY, et al. (2002). "Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation.". J. Biol. Chem. 277 (28): 25370–6. doi:10.1074/jbc.M110432200. PMID 11986303. 
  • Wagner E, Luche S, Penna L, et al. (2002). "A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress.". Biochem. J. 366 (Pt 3): 777–85. doi:10.1042/BJ20020525. PMID 12059788. 
  • Shen C, Nathan C (2002). "Nonredundant antioxidant defense by multiple two-cysteine peroxiredoxins in human prostate cancer cells.". Mol. Med. 8 (2): 95–102. PMID 12080185. 
  • Yang KS, Kang SW, Woo HA, et al. (2002). "Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid.". J. Biol. Chem. 277 (41): 38029–36. doi:10.1074/jbc.M206626200. PMID 12161445. 
  • Geiben-Lynn R, Kursar M, Brown NV, et al. (2003). "HIV-1 antiviral activity of recombinant natural killer cell enhancing factors, NKEF-A and NKEF-B, members of the peroxiredoxin family.". J. Biol. Chem. 278 (3): 1569–74. doi:10.1074/jbc.M209964200. PMID 12421812. 
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