PRDX6
Peroxiredoxin-6 is a protein that in humans is encoded by the PRDX6 gene.[1][2]
Function
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.[2]
Model organisms
Model organisms have been used in the study of PRDX6 function. A conditional knockout mouse line, called Prdx6tm1a(EUCOMM)Wtsi[7][8] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the Wellcome Trust Sanger Institute.[9][10][11]
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[5][12] Twenty five tests were carried out on mutant mice but no significant abnormalities were observed.[5]
References
- ^ Phelan SA (Mar 2001). "AOP2 (antioxidant protein 2): structure and function of a unique thiol-specific antioxidant". Antioxid Redox Signal 1 (4): 571–84. PMID 11233154.
- ^ a b "Entrez Gene: PRDX6 peroxiredoxin 6". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=9588.
- ^ "Salmonella infection data for Prdx6". Wellcome Trust Sanger Institute. http://www.sanger.ac.uk/mouseportal/phenotyping/MBMD/salmonella-challenge/.
- ^ "Citrobacter infection data for Prdx6". Wellcome Trust Sanger Institute. http://www.sanger.ac.uk/mouseportal/phenotyping/MBMD/citrobacter-challenge/.
- ^ a b c Gerdin AK (2010). "The Sanger Mouse Genetics Programme: high throughput characterisation of knockout mice". Acta Opthalmologica 88: 925-7.doi:10.1111/j.1755-3768.2010.4142.x: Wiley. http://onlinelibrary.wiley.com/doi/10.1111/j.1755-3768.2010.4142.x/abstract.
- ^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
- ^ "International Knockout Mouse Consortium". http://www.knockoutmouse.org/martsearch/search?query=Prdx6.
- ^ "Mouse Genome Informatics". http://www.informatics.jax.org/searchtool/Search.do?query=MGI:4431891.
- ^ Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M. et al. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature 474 (7351): 337–342. doi:10.1038/nature10163. PMID 21677750. edit
- ^ Dolgin E (June 2011). "Mouse library set to be knockout". Nature 474: 262-263. doi:10.1038/474262a. http://www.nature.com/news/2011/110615/full/474262a.html.
- ^ Collins FS, Rossant J, Wurst W (January 2007). A mouse for all reasons. Cell 128(1): 9-13. doi:10.1016/j.cell.2006.12.018 PMID 17218247.
- ^ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism.". Genome Biol 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMID 21722353. http://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=21722353.
Further reading
- 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; Gustavii, B (1975). "Work in progress. Occurrence of phospholipase A1 and A2 in human decidua". Prostaglandins 9 (5): 667–73. doi:10.1016/0090-6980(75)90106-9. 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. doi:10.1002/elps.11501301201. PMID 1286669.
- Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. 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. doi:10.1093/dnares/2.1.37. 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. doi:10.1002/elps.11501401183. 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. doi:10.1074/jbc.272.4.2542. 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. doi:10.1074/jbc.273.11.6303. 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. doi:10.1038/nsb0598-400. 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. PMC 1222825. PMID 12059788. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222825.
- 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. PMC 129315. PMID 12193653. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=129315.
- 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Krapfenbauer K; Engidawork E; Cairns N et al. (2003). "Aberrant expression of peroxiredoxin subtypes in neurodegenerative disorders". Brain Res. 967 (1–2): 152–60. doi:10.1016/S0006-8993(02)04243-9. PMID 12650976.
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PDB gallery
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1prx: HORF6 A NOVEL HUMAN PEROXIDASE ENZYME
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| 1.11.1.1-14 |
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| 1.11.1.15 (peroxiredoxin) |
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B enzm: 1.1/2/3/4/5/6/7/8/10/11/13/14/15-18, 2.1/2/3/4/5/6/7/8, 2.7.10, 2.7.11-12, 3.1/2/3/4/5/6/7, 3.1.3.48, 3.4.21/22/23/24, 4.1/2/3/4/5/6, 5.1/2/3/4/99, 6.1-3/4/5-6
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