PRDX6

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Peroxiredoxin 6
File:PBB Protein PRDX6 image.jpg
PDB rendering based on 1prx.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols PRDX6 ; 1-Cys; AOP2; KIAA0106; MGC46173; NSGPx; PRX; aiPLA2; p29
External IDs Template:OMIM5 Template:MGI HomoloGene3606
RNA expression pattern
File:PBB GE PRDX6 200845 s at tn.png
File:PBB GE PRDX6 200844 s at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Peroxiredoxin 6, also known as PRDX6, is a human gene.[1]

The protein encoded by this gene is a member of the thiol-specific antioxidant protein family. This protein is a bifunctional enzyme with two distinct active sites. It is involved in redox regulation of the cell; it can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. It may play a role in the regulation of phospholipid turnover as well as in protection against oxidative injury.[1]

References

  1. 1.0 1.1 "Entrez Gene: PRDX6 peroxiredoxin 6".

Further reading

  • Phelan SA (2001). "AOP2 (antioxidant protein 2): structure and function of a unique thiol-specific antioxidant". Antioxid. Redox Signal. 1 (4): 571–84. PMID 11233154.
  • Manevich Y, Fisher AB (2005). "Peroxiredoxin 6, a 1-Cys peroxiredoxin, functions in antioxidant defense and lung phospholipid metabolism". Free Radic. Biol. Med. 38 (11): 1422–32. doi:10.1016/j.freeradbiomed.2005.02.011. PMID 15890616.
  • Akesson B (1975). "Work in progress. Occurrence of phospholipase A1 and A2 in human decidua". Prostaglandins. 9 (5): 667–73. PMID 240188.
  • Hochstrasser DF, Frutiger S, Paquet N; et al. (1993). "Human liver protein map: a reference database established by microsequencing and gel comparison". Electrophoresis. 13 (12): 992–1001. PMID 1286669.
  • Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. PMID 1602151.
  • Yeats DA, Bakhle YS (1989). "Phospholipases A2 and C of human lung; subcellular distribution and substrate selectivity". Biochim. Biophys. Acta. 1003 (2): 189–95. PMID 2730891.
  • Nagase T, Miyajima N, Tanaka A; et al. (1995). "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1". DNA Res. 2 (1): 37–43. PMID 7788527.
  • Golaz O, Hughes GJ, Frutiger S; et al. (1994). "Plasma and red blood cell protein maps: update 1993". Electrophoresis. 14 (11): 1223–31. PMID 8313871.
  • Kim TS, Sundaresh CS, Feinstein SI; et al. (1997). "Identification of a human cDNA clone for lysosomal type Ca2+-independent phospholipase A2 and properties of the expressed protein". J. Biol. Chem. 272 (4): 2542–50. PMID 8999971.
  • Frank S, Munz B, Werner S (1997). "The human homologue of a bovine non-selenium glutathione peroxidase is a novel keratinocyte growth factor-regulated gene". Oncogene. 14 (8): 915–21. doi:10.1038/sj.onc.1200905. PMID 9050990.
  • Kang SW, Baines IC, Rhee SG (1998). "Characterization of a mammalian peroxiredoxin that contains one conserved cysteine". J. Biol. Chem. 273 (11): 6303–11. PMID 9497358.
  • Choi HJ, Kang SW, Yang CH; et al. (1998). "Crystal structure of a novel human peroxidase enzyme at 2.0 A resolution". Nat. Struct. Biol. 5 (5): 400–6. PMID 9587003.
  • Chen JW, Dodia C, Feinstein SI; et al. (2000). "1-Cys peroxiredoxin, a bifunctional enzyme with glutathione peroxidase and phospholipase A2 activities". J. Biol. Chem. 275 (37): 28421–7. doi:10.1074/jbc.M005073200. PMID 10893423.
  • Fatma N, Singh DP, Shinohara T, Chylack LT (2002). "Transcriptional regulation of the antioxidant protein 2 gene, a thiol-specific antioxidant, by lens epithelium-derived growth factor to protect cells from oxidative stress". J. Biol. Chem. 276 (52): 48899–907. doi:10.1074/jbc.M100733200. PMID 11677226.
  • 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.
  • Leavey PJ, Gonzalez-Aller C, Thurman G; et al. (2003). "A 29-kDa protein associated with p67phox expresses both peroxiredoxin and phospholipase A2 activity and enhances superoxide anion production by a cell-free system of NADPH oxidase activity". J. Biol. Chem. 277 (47): 45181–7. doi:10.1074/jbc.M202869200. PMID 12121978.
  • Manevich Y, Sweitzer T, Pak JH; et al. (2002). "1-Cys peroxiredoxin overexpression protects cells against phospholipid peroxidation-mediated membrane damage". Proc. Natl. Acad. Sci. U.S.A. 99 (18): 11599–604. doi:10.1073/pnas.182384499. PMID 12193653.
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
  • Krapfenbauer K, Engidawork E, Cairns N; et al. (2003). "Aberrant expression of peroxiredoxin subtypes in neurodegenerative disorders". Brain Res. 967 (1–2): 152–60. PMID 12650976.

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