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{{Infobox_gene}}'''Peroxiredoxin-5 (PRDX5), mitochondrial''' is a [[protein]] that in humans is encoded by the ''PRDX5'' [[gene]], located on chromosome 11.<ref>{{Cite web|url=https://www.ncbi.nlm.nih.gov/gene/25824|title=PRDX5 peroxiredoxin 5 [Homo sapiens (human)] |publisher=NCBI |access-date=2016-07-19}}</ref>
{{PBB_Controls
This gene encodes a member of the six-member [[peroxiredoxin]] family of [[antioxidant]] enzymes. Like the other five members, PRDX5 is widely expressed in tissues but differs by its large subcellular distribution.<ref name="Zhou_2000">{{cite journal | vauthors = Zhou Y, Kok KH, Chun AC, Wong CM, Wu HW, Lin MC, Fung PC, Kung H, Jin DY | title = Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis | journal = Biochemical and Biophysical Research Communications | volume = 268 | issue = 3 | pages = 921–7 | date = February 2000 | pmid = 10679306 | doi = 10.1006/bbrc.2000.2231 }}</ref> In human cells, it has been shown that PRDX5 can be localized to [[Mitochondrion|mitochondria]], [[peroxisome]]s, the [[cytosol]], and the [[Cell nucleus|nucleus]].<ref name="Knoops_2011">{{cite journal | vauthors = Knoops B, Goemaere J, Van der Eecken V, Declercq JP | title = Peroxiredoxin 5: structure, mechanism, and function of the mammalian atypical 2-Cys peroxiredoxin | journal = Antioxidants & Redox Signaling | volume = 15 | issue = 3 | pages = 817–29 | date = August 2011 | pmid = 20977338 | doi = 10.1089/ars.2010.3584 }}</ref> Human PRDX5 is identified by virtue of the sequence homologies to yeast peroxisomal antioxidant enzyme PMP20.<ref name="Zhou_2000" /><ref>{{cite journal | vauthors = Yamashita H, Avraham S, Jiang S, London R, Van Veldhoven PP, Subramani S, Rogers RA, Avraham H | title = Characterization of human and murine PMP20 peroxisomal proteins that exhibit antioxidant activity in vitro | journal = The Journal of Biological Chemistry | volume = 274 | issue = 42 | pages = 29897–904 | date = October 1999 | pmid = 10514471 | doi = 10.1074/jbc.274.42.29897 }}</ref>
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Biochemically, PRDX5 is a peroxidase that can use cytosolic or mitochondrial thioredoxins to reduce [[Organic peroxide|alkyl hydroperoxides]] or [[peroxynitrite]] with high rate constants in the 10<sup>6</sup> to 10<sup>7</sup> M<sup>−1</sup>s<sup>−1</sup> range, whereas its reaction with hydrogen peroxide is more modest, in the 10<sup>5</sup> M<sup>−1</sup>s<sup>−1</sup> range.<ref name="Knoops_2011" /> So far, PRDX5 has been shown to be a cytoprotective antioxidant enzyme that inhibits endogenous or exogenous [[peroxide]] accumulation.<ref name="Knoops_2011" />
{{GNF_Protein_box
| image = PBB_Protein_PRDX5_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1h4o.
| PDB = {{PDB2|1h4o}}, {{PDB2|1hd2}}, {{PDB2|1oc3}}, {{PDB2|1urm}}
| Name = Peroxiredoxin 5
| HGNCid = 9355
| Symbol = PRDX5
| AltSymbols =; PLP; PRDX6; ACR1; AOEB166; B166; MGC117264; MGC142283; MGC142285; PMP20; PRXV; SBBI10
| OMIM = 606583
| ECnumber = 
| Homologene = 8076
| MGIid = 1859821
| Function = {{GNF_GO|id=GO:0016209 |text = antioxidant activity}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0051920 |text = peroxiredoxin activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005777 |text = peroxisome}}
| Process = {{GNF_GO|id=GO:0006954 |text = inflammatory response}} {{GNF_GO|id=GO:0006979 |text = response to oxidative stress}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 25824
    | Hs_Ensembl = ENSG00000126432
    | Hs_RefseqProtein = NP_036226
    | Hs_RefseqmRNA = NM_012094
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 63842145
    | Hs_GenLoc_end = 63845858
    | Hs_Uniprot = P30044
    | Mm_EntrezGene = 54683
    | Mm_Ensembl = ENSMUSG00000024953
    | Mm_RefseqmRNA = NM_012021
    | Mm_RefseqProtein = NP_036151
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 19
    | Mm_GenLoc_start = 6973751
    | Mm_GenLoc_end = 6977120
    | Mm_Uniprot = Q3U7H9
  }}
}}
'''Peroxiredoxin 5''', also known as '''PRDX5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRDX5 peroxiredoxin 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=25824| accessdate = }}</ref>


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==Structure==
{{PBB_Summary
| section_title =  
| summary_text = 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 different tissues under normal conditions and during inflammatory processes. This protein interacts with peroxisome receptor 1. The crystal structure of this protein in its reduced form has been resolved to 1.5 angstrom resolution. This gene uses alternate in-frame translation initiation sites to generate mitochondrial or peroxisomal/cytoplasmic forms. Three transcript variants encoding distinct isoforms have been identified for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: PRDX5 peroxiredoxin 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=25824| accessdate = }}</ref>
}}


==References==
According to its amino acid sequence, this 2-Cys peroxiredoxin, PRDX5, is the most divergent isoform among mammalian peroxiredoxins, processing only 28% to 30% sequence identity with typical 2-Cys and 1-Cys peroxiredoxins.<ref>{{cite journal | vauthors = Leyens G, Donnay I, Knoops B | title = Cloning of bovine peroxiredoxins-gene expression in bovine tissues and amino acid sequence comparison with rat, mouse and primate peroxiredoxins | journal = Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology | volume = 136 | issue = 4 | pages = 943–55 | date = December 2003 | pmid = 14662316 | doi = 10.1016/S1096-4959(03)00290-2 }}</ref> The divergent amino acid sequence of this atypical peroxiredoxin is reflected in its unique crystal structure. The typical peroxiredoxin is composed of a [[thioredoxin]] domain and a C-terminal, whereas PRDX5 has an N-terminal domain and a unique [[alpha helix]] replaces a loop structure in the typical thioredoxin domain.<ref name="Knoops_2011" /> In addition, typical 2-Cys or 1-Cys peroxiredoxins are associated as [[Protein dimer|anti-parallel dimers]] via linkage of two beta-7-strands, whereas a PRDX5 dimer is formed by close contact between an alpha-3-helix of one molecule and an alpha-5-helix from the other molecule.<ref name="Knoops_2011" />
{{reflist|2}}
 
==Further reading==
== Function ==
{{refbegin | 2}}
As a peroxiredoxin, PRDX5 has antioxidative and cytoprotective functions during oxidative stress. Overexpression of human PRDX5 has been shown to inhibit peroxide accumulation induced by [[TNF-alpha]], [[Platelet-derived growth factor|PDGF]], and [[p53]] in [[3T3 cells|NIH3T3]] and [[HeLa]] cells and reduce cell death by exogenous peroxide in multiple organelles of [[Chinese hamster ovary cell|CHO]], HT-22, and human tendon cells.<ref name="Zhou_2000" /><ref name="Zitzler_2004"/><ref>{{cite journal | vauthors = Zitzler J, Link D, Schäfer R, Liebetrau W, Kazinski M, Bonin-Debs A, Behl C, Buckel P, Brinkmann U | title = High-throughput functional genomics identifies genes that ameliorate toxicity due to oxidative stress in neuronal HT-22 cells: GFPT2 protects cells against peroxide | journal = Molecular & Cellular Proteomics | volume = 3 | issue = 8 | pages = 834–40 | date = August 2004 | pmid = 15181156 | doi = 10.1074/mcp.M400054-MCP200 }}</ref><ref>{{cite journal | vauthors = Banmeyer I, Marchand C, Verhaeghe C, Vucic B, Rees JF, Knoops B | title = Overexpression of human peroxiredoxin 5 in subcellular compartments of Chinese hamster ovary cells: effects on cytotoxicity and DNA damage caused by peroxides | journal = Free Radical Biology & Medicine | volume = 36 | issue = 1 | pages = 65–77 | date = January 2004 | pmid = 14732291 | doi = 10.1016/j.freeradbiomed.2003.10.019 }}</ref><ref>{{cite journal | vauthors = Yuan J, Murrell GA, Trickett A, Landtmeters M, Knoops B, Wang MX | title = Overexpression of antioxidant enzyme peroxiredoxin 5 protects human tendon cells against apoptosis and loss of cellular function during oxidative stress | journal = Biochimica et Biophysica Acta | volume = 1693 | issue = 1 | pages = 37–45 | date = July 2004 | pmid = 15276323 | doi = 10.1016/j.bbamcr.2004.04.006 }}</ref> Meanwhile, reduced expression of PRDX5 induces cell susceptibility to oxidative damage and [[etoposide]], [[doxorubicin]], [[MPP+|MPP<sup>+</sup>]], and peroxide-induced [[apoptosis]].<ref>{{cite journal | vauthors = Avila PC, Kropotov AV, Krutilina R, Krasnodembskay A, Tomilin NV, Serikov VB | title = Peroxiredoxin V contributes to antioxidant defense of lung epithelial cells | journal = Lung | volume = 186 | issue = 2 | pages = 103–14 | year = 2008 | pmid = 18219526 | doi = 10.1007/s00408-007-9066-2 }}</ref><ref>{{cite journal | vauthors = De Simoni S, Goemaere J, Knoops B | title = Silencing of peroxiredoxin 3 and peroxiredoxin 5 reveals the role of mitochondrial peroxiredoxins in the protection of human neuroblastoma SH-SY5Y cells toward MPP+ | journal = Neuroscience Letters | volume = 433 | issue = 3 | pages = 219–24 | date = March 2008 | pmid = 18262354 | doi = 10.1016/j.neulet.2007.12.068 }}</ref><ref>{{cite journal | vauthors = Kropotov A, Gogvadze V, Shupliakov O, Tomilin N, Serikov VB, Tomilin NV, Zhivotovsky B | title = Peroxiredoxin V is essential for protection against apoptosis in human lung carcinoma cells | journal = Experimental Cell Research | volume = 312 | issue = 15 | pages = 2806–15 | date = September 2006 | pmid = 16781710 | doi = 10.1016/j.yexcr.2006.05.006 }}</ref><ref>{{cite journal | vauthors = Serikov VB, Leutenegger C, Krutilina R, Kropotov A, Pleskach N, Suh JH, Tomilin NV | title = Cigarette smoke extract inhibits expression of peroxiredoxin V and increases airway epithelial permeability | journal = Inhalation Toxicology | volume = 18 | issue = 1 | pages = 79–92 | date = January 2006 | pmid = 16326404 | doi = 10.1080/08958370500282506 }}</ref> In addition, expressing human PRDX5 in other organisms or tissues such as yeast, mouse brain, and Xenopus embryos also leads to protection against oxidative stress.<ref>{{cite journal | vauthors = Tiên Nguyên-nhu N, Knoops B | title = Mitochondrial and cytosolic expression of human peroxiredoxin 5 in Saccharomyces cerevisiae protect yeast cells from oxidative stress induced by paraquat | journal = FEBS Letters | volume = 544 | issue = 1-3 | pages = 148–52 | date = June 2003 | pmid = 12782306 | doi=10.1016/s0014-5793(03)00493-9}}</ref><ref>{{cite journal | vauthors = Plaisant F, Clippe A, Vander Stricht D, Knoops B, Gressens P | title = Recombinant peroxiredoxin 5 protects against excitotoxic brain lesions in newborn mice | journal = Free Radical Biology & Medicine | volume = 34 | issue = 7 | pages = 862–72 | date = April 2003 | pmid = 12654475 | doi = 10.1016/s0891-5849(02)01440-5 }}</ref><ref>{{cite journal | vauthors = Peng Y, Yang PH, Guo Y, Ng SS, Liu J, Fung PC, Tay D, Ge J, He ML, Kung HF, Lin MC | title = Catalase and peroxiredoxin 5 protect Xenopus embryos against alcohol-induced ocular anomalies | journal = Investigative Ophthalmology & Visual Science | volume = 45 | issue = 1 | pages = 23–9 | date = January 2004 | pmid = 14691149 | doi = 10.1167/iovs.03-0550 }}</ref> Interestingly, PRDX5 in Drosophila melanogaster has been shown to promote longevity in addition to antioxidant activity.<ref>{{cite journal | vauthors = Radyuk SN, Michalak K, Klichko VI, Benes J, Rebrin I, Sohal RS, Orr WC | title = Peroxiredoxin 5 confers protection against oxidative stress and apoptosis and also promotes longevity in Drosophila | journal = The Biochemical Journal | volume = 419 | issue = 2 | pages = 437–45 | date = April 2009 | pmid = 19128239  | pmc = 2842572 | doi = 10.1042/BJ20082003 }}</ref>
{{PBB_Further_reading
 
| citations =
==Clinical significance==
*{{cite journal | author=Wood ZA, Schröder E, Robin Harris J, Poole LB |title=Structure, mechanism and regulation of peroxiredoxins. |journal=Trends Biochem. Sci. |volume=28 |issue= 1 |pages= 32-40 |year= 2003 |pmid= 12517450 |doi= }}
By examining 98 [[stroke]] patients, Kunze et al. showed an inverse correlation between stroke progression and PRDX5 concentration, suggesting that plasma PRDX5 can be a potential biomarker of [[inflammation]] in acute stroke.<ref>{{cite journal | vauthors = Kunze A, Zierath D, Tanzi P, Cain K, Becker K | title = Peroxiredoxin 5 (PRX5) is correlated inversely to systemic markers of inflammation in acute stroke | journal = Stroke | volume = 45 | issue = 2 | pages = 608–10 | date = February 2014 | pmid = 24385276 | pmc = 3946812 | doi = 10.1161/STROKEAHA.113.003813 }}</ref> In human [[breast cancer]] cells, knockdown of transcription factor, [[GATA1]], led to increased expression of PRDX5 and inhibition of apoptosis.<ref name="Zitzler_2004">{{cite journal | vauthors = Seo MS, Kang SW, Kim K, Baines IC, Lee TH, Rhee SG | title = Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate | journal = The Journal of Biological Chemistry | volume = 275 | issue = 27 | pages = 20346–54 | date = July 2000 | pmid = 10751410 | doi = 10.1074/jbc.M001943200 }}</ref> A substantial increase in PRDX5 expression has been observed in [[astrocyte]]s in [[Multiple sclerosis lesions|multiple sclerosis lesion]].<ref>{{cite journal | vauthors = Holley JE, Newcombe J, Winyard PG, Gutowski NJ | title = Peroxiredoxin V in multiple sclerosis lesions: predominant expression by astrocytes | journal = Multiple Sclerosis | volume = 13 | issue = 8 | pages = 955–61 | date = September 2007 | pmid = 17623739 | doi = 10.1177/1352458507078064 }}</ref> PRDX5 has also been identified as a candidate risk gene for the inflammatory disease, [[sarcoidosis]].<ref>{{cite journal | vauthors = Fischer A, Schmid B, Ellinghaus D, Nothnagel M, Gaede KI, Schürmann M, Lipinski S, Rosenstiel P, Zissel G, Höhne K, Petrek M, Kolek V, Pabst S, Grohé C, Grunewald J, Ronninger M, Eklund A, Padyukov L, Gieger C, Wichmann HE, Nebel A, Franke A, Müller-Quernheim J, Hofmann S, Schreiber S | title = A novel sarcoidosis risk locus for Europeans on chromosome 11q13.1 | journal = American Journal of Respiratory and Critical Care Medicine | volume = 186 | issue = 9 | pages = 877–85 | date = November 2012 | pmid = 22837380 | doi = 10.1164/rccm.201204-0708OC }}</ref>
*{{cite journal  | author=Hochstrasser DF, Frutiger S, Paquet N, ''et al.'' |title=Human liver protein map: a reference database established by microsequencing and gel comparison. |journal=Electrophoresis |volume=13 |issue= 12 |pages= 992-1001 |year= 1993 |pmid= 1286669 |doi=  }}
 
*{{cite journal  | author=Kropotov A, Sedova V, Ivanov V, ''et al.'' |title=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. |journal=Eur. J. Biochem. |volume=260 |issue= 2 |pages= 336-46 |year= 1999 |pmid= 10095767 |doi= }}
== Interactions ==
*{{cite journal | author=Wattiez R, Hermans C, Bernard A, ''et al.'' |title=Human bronchoalveolar lavage fluid: two-dimensional gel electrophoresis, amino acid microsequencing and identification of major proteins. |journal=Electrophoresis |volume=20 |issue= 7 |pages= 1634-45 |year= 1999 |pmid= 10424490 |doi= 10.1002/(SICI)1522-2683(19990601)20:7<1634::AID-ELPS1634>3.0.CO;2-J }}
 
*{{cite journal | author=Yamashita H, Avraham S, Jiang S, ''et al.'' |title=Characterization of human and murine PMP20 peroxisomal proteins that exhibit antioxidant activity in vitro. |journal=J. Biol. Chem. |volume=274 |issue= 42 |pages= 29897-904 |year= 1999 |pmid= 10514471 |doi= }}
Transcription factor GATA-binding protein 1 can bind to the PRDX5 gene and lead to increased expression of PRDX5.<ref name="Zitzler_2004" /> PRDX5 has been shown to physically interact with PRDX1, PRDX2, PRDX6, SOD1, and PARK7 in at least two independent high-throughput proteomic analyses.<ref>{{Cite web|url=http://thebiogrid.org/117352/summary/homo-sapiens/prdx5.html|title=PRDX5 (SBBI10) Result Summary {{!}} BioGRID|last=Lab|first=Mike Tyers|website=thebiogrid.org|access-date=2016-07-19}}</ref>
*{{cite journal  | author=Knoops B, Clippe A, Bogard C, ''et al.'' |title=Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family. |journal=J. Biol. Chem. |volume=274 |issue= 43 |pages= 30451-8 |year= 1999 |pmid= 10521424 |doi= }}
 
*{{cite journal | author=Zhou Y, Kok KH, Chun AC, ''et al.'' |title=Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis. |journal=Biochem. Biophys. Res. Commun. |volume=268 |issue= 3 |pages= 921-7 |year= 2000 |pmid= 10679306 |doi= 10.1006/bbrc.2000.2231 }}
== References ==
*{{cite journal | author=Seo MS, Kang SW, Kim K, ''et al.'' |title=Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate. |journal=J. Biol. Chem. |volume=275 |issue= 27 |pages= 20346-54 |year= 2000 |pmid= 10751410 |doi= 10.1074/jbc.M001943200 }}
{{reflist|33em}}
*{{cite journal | author=Hu RM, Han ZG, Song HD, ''et al.'' |title=Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 17 |pages= 9543-8 |year= 2000 |pmid= 10931946 |doi= 10.1073/pnas.160270997 }}
 
*{{cite journal | author=Declercq JP, Evrard C, Clippe A, ''et al.'' |title=Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 A resolution. |journal=J. Mol. Biol. |volume=311 |issue= 4 |pages= 751-9 |year= 2001 |pmid= 11518528 |doi= 10.1006/jmbi.2001.4853 }}
== Further reading ==
*{{cite journal | author=Rouhier N, Gelhaye E, Jacquot JP |title=Glutaredoxin-dependent peroxiredoxin from poplar: protein-protein interaction and catalytic mechanism. |journal=J. Biol. Chem. |volume=277 |issue= 16 |pages= 13609-14 |year= 2002 |pmid= 11832487 |doi= 10.1074/jbc.M111489200 }}
{{refbegin|33em}}
*{{cite journal | author=Wang MX, Wei A, Yuan J, ''et al.'' |title=Expression and regulation of peroxiredoxin 5 in human osteoarthritis. |journal=FEBS Lett. |volume=531 |issue= 2 |pages= 359-62 |year= 2002 |pmid= 12417342 |doi= }}
* {{cite journal | vauthors = Wood ZA, Schröder E, Robin Harris J, Poole LB | title = Structure, mechanism and regulation of peroxiredoxins | journal = Trends in Biochemical Sciences | volume = 28 | issue = 1 | pages = 32–40 | date = January 2003 | pmid = 12517450 | doi = 10.1016/S0968-0004(02)00003-8 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* {{cite journal | vauthors = Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R | title = Human liver protein map: a reference database established by microsequencing and gel comparison | journal = Electrophoresis | volume = 13 | issue = 12 | pages = 992–1001 | date = December 1992 | pmid = 1286669 | doi = 10.1002/elps.11501301201 }}
*{{cite journal | author=Leyens G, Donnay I, Knoops B |title=Cloning of bovine peroxiredoxins-gene expression in bovine tissues and amino acid sequence comparison with rat, mouse and primate peroxiredoxins. |journal=Comp. Biochem. Physiol. B, Biochem. Mol. Biol. |volume=136 |issue= 4 |pages= 943-55 |year= 2004 |pmid= 14662316 |doi= }}
* {{cite journal | vauthors = Kropotov A, Sedova V, Ivanov V, Sazeeva N, Tomilin A, Krutilina R, Oei SL, Griesenbeck J, Buchlow G, Tomilin N | title = 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 | journal = European Journal of Biochemistry | volume = 260 | issue = 2 | pages = 336–46 | date = March 1999 | pmid = 10095767 | doi = 10.1046/j.1432-1327.1999.00162.x }}
*{{cite journal | author=Banmeyer I, Marchand C, Verhaeghe C, ''et al.'' |title=Overexpression of human peroxiredoxin 5 in subcellular compartments of Chinese hamster ovary cells: effects on cytotoxicity and DNA damage caused by peroxides. |journal=Free Radic. Biol. Med. |volume=36 |issue= 1 |pages= 65-77 |year= 2004 |pmid= 14732291 |doi= 10.1016/j.freeradbiomed.2003.10.019 }}
* {{cite journal | vauthors = Wattiez R, Hermans C, Bernard A, Lesur O, Falmagne P | title = Human bronchoalveolar lavage fluid: two-dimensional gel electrophoresis, amino acid microsequencing and identification of major proteins | journal = Electrophoresis | volume = 20 | issue = 7 | pages = 1634–45 | date = June 1999 | pmid = 10424490 | doi = 10.1002/(SICI)1522-2683(19990601)20:7<1634::AID-ELPS1634>3.0.CO;2-J }}
*{{cite journal  | author=Salmon M, Dedessus Le Moutier J, Wenders F, ''et al.'' |title=Role of the PLA2-independent peroxiredoxin VI activity in the survival of immortalized fibroblasts exposed to cytotoxic oxidative stress. |journal=FEBS Lett. |volume=557 |issue= 1-3 |pages= 26-32 |year= 2004 |pmid= 14741336 |doi= }}
* {{cite journal | vauthors = Zhou Y, Kok KH, Chun AC, Wong CM, Wu HW, Lin MC, Fung PC, Kung H, Jin DY | title = Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis | journal = Biochemical and Biophysical Research Communications | volume = 268 | issue = 3 | pages = 921–7 | date = February 2000 | pmid = 10679306 | doi = 10.1006/bbrc.2000.2231 }}
*{{cite journal | author=Evrard C, Capron A, Marchand C, ''et al.'' |title=Crystal structure of a dimeric oxidized form of human peroxiredoxin 5. |journal=J. Mol. Biol. |volume=337 |issue= 5 |pages= 1079-90 |year= 2004 |pmid= 15046979 |doi= 10.1016/j.jmb.2004.02.017 }}
* {{cite journal | vauthors = Seo MS, Kang SW, Kim K, Baines IC, Lee TH, Rhee SG | title = Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate | journal = The Journal of Biological Chemistry | volume = 275 | issue = 27 | pages = 20346–54 | date = July 2000 | pmid = 10751410 | doi = 10.1074/jbc.M001943200 }}
*{{cite journal  | author=Yuan J, Murrell GA, Trickett A, ''et al.'' |title=Overexpression of antioxidant enzyme peroxiredoxin 5 protects human tendon cells against apoptosis and loss of cellular function during oxidative stress. |journal=Biochim. Biophys. Acta |volume=1693 |issue= 1 |pages= 37-45 |year= 2004 |pmid= 15276323 |doi= 10.1016/j.bbamcr.2004.04.006 }}
* {{cite journal | vauthors = Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL | title = Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 97 | issue = 17 | pages = 9543–8 | date = August 2000 | pmid = 10931946 | pmc = 16901 | doi = 10.1073/pnas.160270997 | bibcode = 2000PNAS...97.9543H | jstor = 123500 }}
*{{cite journal  | author=Dubuisson M, Vander Stricht D, Clippe A, ''et al.'' |title=Human peroxiredoxin 5 is a peroxynitrite reductase. |journal=FEBS Lett. |volume=571 |issue= 1-3 |pages= 161-5 |year= 2004 |pmid= 15280035 |doi= 10.1016/j.febslet.2004.06.080 }}
* {{cite journal | vauthors = Declercq JP, Evrard C, Clippe A, Stricht DV, Bernard A, Knoops B | title = Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 A resolution | journal = Journal of Molecular Biology | volume = 311 | issue = 4 | pages = 751–9 | date = August 2001 | pmid = 11518528 | doi = 10.1006/jmbi.2001.4853 }}
}}
* {{cite journal | vauthors = Rouhier N, Gelhaye E, Jacquot JP | title = Glutaredoxin-dependent peroxiredoxin from poplar: protein-protein interaction and catalytic mechanism | journal = The Journal of Biological Chemistry | volume = 277 | issue = 16 | pages = 13609–14 | date = April 2002 | pmid = 11832487 | doi = 10.1074/jbc.M111489200 }}
* {{cite journal | vauthors = Wang MX, Wei A, Yuan J, Trickett A, Knoops B, Murrell GA | title = Expression and regulation of peroxiredoxin 5 in human osteoarthritis | journal = FEBS Letters | volume = 531 | issue = 2 | pages = 359–62 | date = November 2002 | pmid = 12417342 | doi = 10.1016/S0014-5793(02)03511-1 }}
* {{cite journal | vauthors = Leyens G, Donnay I, Knoops B | title = Cloning of bovine peroxiredoxins-gene expression in bovine tissues and amino acid sequence comparison with rat, mouse and primate peroxiredoxins | journal = Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology | volume = 136 | issue = 4 | pages = 943–55 | date = December 2003 | pmid = 14662316 | doi = 10.1016/S1096-4959(03)00290-2 }}
* {{cite journal | vauthors = Banmeyer I, Marchand C, Verhaeghe C, Vucic B, Rees JF, Knoops B | title = Overexpression of human peroxiredoxin 5 in subcellular compartments of Chinese hamster ovary cells: effects on cytotoxicity and DNA damage caused by peroxides | journal = Free Radical Biology & Medicine | volume = 36 | issue = 1 | pages = 65–77 | date = January 2004 | pmid = 14732291 | doi = 10.1016/j.freeradbiomed.2003.10.019 }}
* {{cite journal | vauthors = Salmon M, Dedessus Le Moutier J, Wenders F, Chiarizia S, Eliaers F, Remacle J, Royer V, Pascal T, Toussaint O | title = Role of the PLA2-independent peroxiredoxin VI activity in the survival of immortalized fibroblasts exposed to cytotoxic oxidative stress | journal = FEBS Letters | volume = 557 | issue = 1-3 | pages = 26–32 | date = January 2004 | pmid = 14741336 | doi = 10.1016/S0014-5793(03)01437-6 }}
* {{cite journal | vauthors = Evrard C, Capron A, Marchand C, Clippe A, Wattiez R, Soumillion P, Knoops B, Declercq JP | title = Crystal structure of a dimeric oxidized form of human peroxiredoxin 5 | journal = Journal of Molecular Biology | volume = 337 | issue = 5 | pages = 1079–90 | date = April 2004 | pmid = 15046979 | doi = 10.1016/j.jmb.2004.02.017 }}
* {{cite journal | vauthors = Yuan J, Murrell GA, Trickett A, Landtmeters M, Knoops B, Wang MX | title = Overexpression of antioxidant enzyme peroxiredoxin 5 protects human tendon cells against apoptosis and loss of cellular function during oxidative stress | journal = Biochimica et Biophysica Acta | volume = 1693 | issue = 1 | pages = 37–45 | date = July 2004 | pmid = 15276323 | doi = 10.1016/j.bbamcr.2004.04.006 }}
* {{cite journal | vauthors = Dubuisson M, Vander Stricht D, Clippe A, Etienne F, Nauser T, Kissner R, Koppenol WH, Rees JF, Knoops B | title = Human peroxiredoxin 5 is a peroxynitrite reductase | journal = FEBS Letters | volume = 571 | issue = 1-3 | pages = 161–5 | date = July 2004 | pmid = 15280035 | doi = 10.1016/j.febslet.2004.06.080 }}
{{refend}}
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{{PDB Gallery|geneid=25824}}


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{{Peroxidases}}
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Revision as of 18:39, 7 September 2017

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Identifiers
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Orthologs
SpeciesHumanMouse
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Peroxiredoxin-5 (PRDX5), mitochondrial is a protein that in humans is encoded by the PRDX5 gene, located on chromosome 11.[1]

This gene encodes a member of the six-member peroxiredoxin family of antioxidant enzymes. Like the other five members, PRDX5 is widely expressed in tissues but differs by its large subcellular distribution.[2] In human cells, it has been shown that PRDX5 can be localized to mitochondria, peroxisomes, the cytosol, and the nucleus.[3] Human PRDX5 is identified by virtue of the sequence homologies to yeast peroxisomal antioxidant enzyme PMP20.[2][4]

Biochemically, PRDX5 is a peroxidase that can use cytosolic or mitochondrial thioredoxins to reduce alkyl hydroperoxides or peroxynitrite with high rate constants in the 106 to 107 M−1s−1 range, whereas its reaction with hydrogen peroxide is more modest, in the 105 M−1s−1 range.[3] So far, PRDX5 has been shown to be a cytoprotective antioxidant enzyme that inhibits endogenous or exogenous peroxide accumulation.[3]

Structure

According to its amino acid sequence, this 2-Cys peroxiredoxin, PRDX5, is the most divergent isoform among mammalian peroxiredoxins, processing only 28% to 30% sequence identity with typical 2-Cys and 1-Cys peroxiredoxins.[5] The divergent amino acid sequence of this atypical peroxiredoxin is reflected in its unique crystal structure. The typical peroxiredoxin is composed of a thioredoxin domain and a C-terminal, whereas PRDX5 has an N-terminal domain and a unique alpha helix replaces a loop structure in the typical thioredoxin domain.[3] In addition, typical 2-Cys or 1-Cys peroxiredoxins are associated as anti-parallel dimers via linkage of two beta-7-strands, whereas a PRDX5 dimer is formed by close contact between an alpha-3-helix of one molecule and an alpha-5-helix from the other molecule.[3]

Function

As a peroxiredoxin, PRDX5 has antioxidative and cytoprotective functions during oxidative stress. Overexpression of human PRDX5 has been shown to inhibit peroxide accumulation induced by TNF-alpha, PDGF, and p53 in NIH3T3 and HeLa cells and reduce cell death by exogenous peroxide in multiple organelles of CHO, HT-22, and human tendon cells.[2][6][7][8][9] Meanwhile, reduced expression of PRDX5 induces cell susceptibility to oxidative damage and etoposide, doxorubicin, MPP+, and peroxide-induced apoptosis.[10][11][12][13] In addition, expressing human PRDX5 in other organisms or tissues such as yeast, mouse brain, and Xenopus embryos also leads to protection against oxidative stress.[14][15][16] Interestingly, PRDX5 in Drosophila melanogaster has been shown to promote longevity in addition to antioxidant activity.[17]

Clinical significance

By examining 98 stroke patients, Kunze et al. showed an inverse correlation between stroke progression and PRDX5 concentration, suggesting that plasma PRDX5 can be a potential biomarker of inflammation in acute stroke.[18] In human breast cancer cells, knockdown of transcription factor, GATA1, led to increased expression of PRDX5 and inhibition of apoptosis.[6] A substantial increase in PRDX5 expression has been observed in astrocytes in multiple sclerosis lesion.[19] PRDX5 has also been identified as a candidate risk gene for the inflammatory disease, sarcoidosis.[20]

Interactions

Transcription factor GATA-binding protein 1 can bind to the PRDX5 gene and lead to increased expression of PRDX5.[6] PRDX5 has been shown to physically interact with PRDX1, PRDX2, PRDX6, SOD1, and PARK7 in at least two independent high-throughput proteomic analyses.[21]

References

  1. ↑ "PRDX5 peroxiredoxin 5 [Homo sapiens (human)]". NCBI. Retrieved 2016-07-19.
  2. ↑ 2.0 2.1 2.2 Zhou Y, Kok KH, Chun AC, Wong CM, Wu HW, Lin MC, Fung PC, Kung H, Jin DY (February 2000). "Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis". Biochemical and Biophysical Research Communications. 268 (3): 921–7. doi:10.1006/bbrc.2000.2231. PMID 10679306.
  3. ↑ 3.0 3.1 3.2 3.3 3.4 Knoops B, Goemaere J, Van der Eecken V, Declercq JP (August 2011). "Peroxiredoxin 5: structure, mechanism, and function of the mammalian atypical 2-Cys peroxiredoxin". Antioxidants & Redox Signaling. 15 (3): 817–29. doi:10.1089/ars.2010.3584. PMID 20977338.
  4. ↑ Yamashita H, Avraham S, Jiang S, London R, Van Veldhoven PP, Subramani S, Rogers RA, Avraham H (October 1999). "Characterization of human and murine PMP20 peroxisomal proteins that exhibit antioxidant activity in vitro". The Journal of Biological Chemistry. 274 (42): 29897–904. doi:10.1074/jbc.274.42.29897. PMID 10514471.
  5. ↑ Leyens G, Donnay I, Knoops B (December 2003). "Cloning of bovine peroxiredoxins-gene expression in bovine tissues and amino acid sequence comparison with rat, mouse and primate peroxiredoxins". Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology. 136 (4): 943–55. doi:10.1016/S1096-4959(03)00290-2. PMID 14662316.
  6. ↑ 6.0 6.1 6.2 Seo MS, Kang SW, Kim K, Baines IC, Lee TH, Rhee SG (July 2000). "Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate". The Journal of Biological Chemistry. 275 (27): 20346–54. doi:10.1074/jbc.M001943200. PMID 10751410.
  7. ↑ Zitzler J, Link D, Schäfer R, Liebetrau W, Kazinski M, Bonin-Debs A, Behl C, Buckel P, Brinkmann U (August 2004). "High-throughput functional genomics identifies genes that ameliorate toxicity due to oxidative stress in neuronal HT-22 cells: GFPT2 protects cells against peroxide". Molecular & Cellular Proteomics. 3 (8): 834–40. doi:10.1074/mcp.M400054-MCP200. PMID 15181156.
  8. ↑ Banmeyer I, Marchand C, Verhaeghe C, Vucic B, Rees JF, Knoops B (January 2004). "Overexpression of human peroxiredoxin 5 in subcellular compartments of Chinese hamster ovary cells: effects on cytotoxicity and DNA damage caused by peroxides". Free Radical Biology & Medicine. 36 (1): 65–77. doi:10.1016/j.freeradbiomed.2003.10.019. PMID 14732291.
  9. ↑ Yuan J, Murrell GA, Trickett A, Landtmeters M, Knoops B, Wang MX (July 2004). "Overexpression of antioxidant enzyme peroxiredoxin 5 protects human tendon cells against apoptosis and loss of cellular function during oxidative stress". Biochimica et Biophysica Acta. 1693 (1): 37–45. doi:10.1016/j.bbamcr.2004.04.006. PMID 15276323.
  10. ↑ Avila PC, Kropotov AV, Krutilina R, Krasnodembskay A, Tomilin NV, Serikov VB (2008). "Peroxiredoxin V contributes to antioxidant defense of lung epithelial cells". Lung. 186 (2): 103–14. doi:10.1007/s00408-007-9066-2. PMID 18219526.
  11. ↑ De Simoni S, Goemaere J, Knoops B (March 2008). "Silencing of peroxiredoxin 3 and peroxiredoxin 5 reveals the role of mitochondrial peroxiredoxins in the protection of human neuroblastoma SH-SY5Y cells toward MPP+". Neuroscience Letters. 433 (3): 219–24. doi:10.1016/j.neulet.2007.12.068. PMID 18262354.
  12. ↑ Kropotov A, Gogvadze V, Shupliakov O, Tomilin N, Serikov VB, Tomilin NV, Zhivotovsky B (September 2006). "Peroxiredoxin V is essential for protection against apoptosis in human lung carcinoma cells". Experimental Cell Research. 312 (15): 2806–15. doi:10.1016/j.yexcr.2006.05.006. PMID 16781710.
  13. ↑ Serikov VB, Leutenegger C, Krutilina R, Kropotov A, Pleskach N, Suh JH, Tomilin NV (January 2006). "Cigarette smoke extract inhibits expression of peroxiredoxin V and increases airway epithelial permeability". Inhalation Toxicology. 18 (1): 79–92. doi:10.1080/08958370500282506. PMID 16326404.
  14. ↑ Tiên Nguyên-nhu N, Knoops B (June 2003). "Mitochondrial and cytosolic expression of human peroxiredoxin 5 in Saccharomyces cerevisiae protect yeast cells from oxidative stress induced by paraquat". FEBS Letters. 544 (1–3): 148–52. doi:10.1016/s0014-5793(03)00493-9. PMID 12782306.
  15. ↑ Plaisant F, Clippe A, Vander Stricht D, Knoops B, Gressens P (April 2003). "Recombinant peroxiredoxin 5 protects against excitotoxic brain lesions in newborn mice". Free Radical Biology & Medicine. 34 (7): 862–72. doi:10.1016/s0891-5849(02)01440-5. PMID 12654475.
  16. ↑ Peng Y, Yang PH, Guo Y, Ng SS, Liu J, Fung PC, Tay D, Ge J, He ML, Kung HF, Lin MC (January 2004). "Catalase and peroxiredoxin 5 protect Xenopus embryos against alcohol-induced ocular anomalies". Investigative Ophthalmology & Visual Science. 45 (1): 23–9. doi:10.1167/iovs.03-0550. PMID 14691149.
  17. ↑ Radyuk SN, Michalak K, Klichko VI, Benes J, Rebrin I, Sohal RS, Orr WC (April 2009). "Peroxiredoxin 5 confers protection against oxidative stress and apoptosis and also promotes longevity in Drosophila". The Biochemical Journal. 419 (2): 437–45. doi:10.1042/BJ20082003. PMC 2842572. PMID 19128239.
  18. ↑ Kunze A, Zierath D, Tanzi P, Cain K, Becker K (February 2014). "Peroxiredoxin 5 (PRX5) is correlated inversely to systemic markers of inflammation in acute stroke". Stroke. 45 (2): 608–10. doi:10.1161/STROKEAHA.113.003813. PMC 3946812. PMID 24385276.
  19. ↑ Holley JE, Newcombe J, Winyard PG, Gutowski NJ (September 2007). "Peroxiredoxin V in multiple sclerosis lesions: predominant expression by astrocytes". Multiple Sclerosis. 13 (8): 955–61. doi:10.1177/1352458507078064. PMID 17623739.
  20. ↑ Fischer A, Schmid B, Ellinghaus D, Nothnagel M, Gaede KI, Schürmann M, Lipinski S, Rosenstiel P, Zissel G, Höhne K, Petrek M, Kolek V, Pabst S, Grohé C, Grunewald J, Ronninger M, Eklund A, Padyukov L, Gieger C, Wichmann HE, Nebel A, Franke A, Müller-Quernheim J, Hofmann S, Schreiber S (November 2012). "A novel sarcoidosis risk locus for Europeans on chromosome 11q13.1". American Journal of Respiratory and Critical Care Medicine. 186 (9): 877–85. doi:10.1164/rccm.201204-0708OC. PMID 22837380.
  21. ↑ Lab, Mike Tyers. "PRDX5 (SBBI10) Result Summary | BioGRID". thebiogrid.org. Retrieved 2016-07-19.

Further reading

  • Wood ZA, Schröder E, Robin Harris J, Poole LB (January 2003). "Structure, mechanism and regulation of peroxiredoxins". Trends in Biochemical Sciences. 28 (1): 32–40. doi:10.1016/S0968-0004(02)00003-8. PMID 12517450.
  • Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R (December 1992). "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.
  • Kropotov A, Sedova V, Ivanov V, Sazeeva N, Tomilin A, Krutilina R, Oei SL, Griesenbeck J, Buchlow G, Tomilin N (March 1999). "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". European Journal of Biochemistry. 260 (2): 336–46. doi:10.1046/j.1432-1327.1999.00162.x. PMID 10095767.
  • Wattiez R, Hermans C, Bernard A, Lesur O, Falmagne P (June 1999). "Human bronchoalveolar lavage fluid: two-dimensional gel electrophoresis, amino acid microsequencing and identification of major proteins". Electrophoresis. 20 (7): 1634–45. doi:10.1002/(SICI)1522-2683(19990601)20:7<1634::AID-ELPS1634>3.0.CO;2-J. PMID 10424490.
  • Zhou Y, Kok KH, Chun AC, Wong CM, Wu HW, Lin MC, Fung PC, Kung H, Jin DY (February 2000). "Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis". Biochemical and Biophysical Research Communications. 268 (3): 921–7. doi:10.1006/bbrc.2000.2231. PMID 10679306.
  • Seo MS, Kang SW, Kim K, Baines IC, Lee TH, Rhee SG (July 2000). "Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate". The Journal of Biological Chemistry. 275 (27): 20346–54. doi:10.1074/jbc.M001943200. PMID 10751410.
  • Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL (August 2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning". Proceedings of the National Academy of Sciences of the United States of America. 97 (17): 9543–8. Bibcode:2000PNAS...97.9543H. doi:10.1073/pnas.160270997. JSTOR 123500. PMC 16901. PMID 10931946.
  • Declercq JP, Evrard C, Clippe A, Stricht DV, Bernard A, Knoops B (August 2001). "Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5 A resolution". Journal of Molecular Biology. 311 (4): 751–9. doi:10.1006/jmbi.2001.4853. PMID 11518528.
  • Rouhier N, Gelhaye E, Jacquot JP (April 2002). "Glutaredoxin-dependent peroxiredoxin from poplar: protein-protein interaction and catalytic mechanism". The Journal of Biological Chemistry. 277 (16): 13609–14. doi:10.1074/jbc.M111489200. PMID 11832487.
  • Wang MX, Wei A, Yuan J, Trickett A, Knoops B, Murrell GA (November 2002). "Expression and regulation of peroxiredoxin 5 in human osteoarthritis". FEBS Letters. 531 (2): 359–62. doi:10.1016/S0014-5793(02)03511-1. PMID 12417342.
  • Leyens G, Donnay I, Knoops B (December 2003). "Cloning of bovine peroxiredoxins-gene expression in bovine tissues and amino acid sequence comparison with rat, mouse and primate peroxiredoxins". Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology. 136 (4): 943–55. doi:10.1016/S1096-4959(03)00290-2. PMID 14662316.
  • Banmeyer I, Marchand C, Verhaeghe C, Vucic B, Rees JF, Knoops B (January 2004). "Overexpression of human peroxiredoxin 5 in subcellular compartments of Chinese hamster ovary cells: effects on cytotoxicity and DNA damage caused by peroxides". Free Radical Biology & Medicine. 36 (1): 65–77. doi:10.1016/j.freeradbiomed.2003.10.019. PMID 14732291.
  • Salmon M, Dedessus Le Moutier J, Wenders F, Chiarizia S, Eliaers F, Remacle J, Royer V, Pascal T, Toussaint O (January 2004). "Role of the PLA2-independent peroxiredoxin VI activity in the survival of immortalized fibroblasts exposed to cytotoxic oxidative stress". FEBS Letters. 557 (1–3): 26–32. doi:10.1016/S0014-5793(03)01437-6. PMID 14741336.
  • Evrard C, Capron A, Marchand C, Clippe A, Wattiez R, Soumillion P, Knoops B, Declercq JP (April 2004). "Crystal structure of a dimeric oxidized form of human peroxiredoxin 5". Journal of Molecular Biology. 337 (5): 1079–90. doi:10.1016/j.jmb.2004.02.017. PMID 15046979.
  • Yuan J, Murrell GA, Trickett A, Landtmeters M, Knoops B, Wang MX (July 2004). "Overexpression of antioxidant enzyme peroxiredoxin 5 protects human tendon cells against apoptosis and loss of cellular function during oxidative stress". Biochimica et Biophysica Acta. 1693 (1): 37–45. doi:10.1016/j.bbamcr.2004.04.006. PMID 15276323.
  • Dubuisson M, Vander Stricht D, Clippe A, Etienne F, Nauser T, Kissner R, Koppenol WH, Rees JF, Knoops B (July 2004). "Human peroxiredoxin 5 is a peroxynitrite reductase". FEBS Letters. 571 (1–3): 161–5. doi:10.1016/j.febslet.2004.06.080. PMID 15280035.
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