PRDX5

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PRDX5
Protein PRDX5 PDB 1h4o.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases PRDX5, ACR1, AOEB166, B166, HEL-S-55, PLP, PMP20, PRDX6, PRXV, prx-V, SBBI10, peroxiredoxin 5
External IDs MGI: 1859821 HomoloGene: 8076 GeneCards: PRDX5
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_012094
NM_181651
NM_181652

NM_012021

RefSeq (protein)

NP_036226
NP_857634
NP_857635

NP_036151.1
NP_036151

Location (UCSC) Chr 11: 64.32 – 64.32 Mb Chr 19: 6.91 – 6.91 Mb
PubMed search [1] [2]
Wikidata
View/Edit Human View/Edit Mouse

Peroxiredoxin-5 (PRDX5), mitochondrial is a protein that in humans is encoded by the PRDX5 gene, located on chromosome 11.[3]

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.[4] In human cells, it has been shown that PRDX5 can be localized to mitochondria, peroxisomes, the cytosol, and the nucleus.[5] Human PRDX5 is identified by virtue of the sequence homologies to yeast peroxisomal antioxidant enzyme PMP20.[4][6]

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.[5] So far, PRDX5 has been shown to be a cytoprotective antioxidant enzyme that inhibits endogenous or exogenous peroxide accumulation.[5]

Structure[edit]

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.[7] 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.[5] 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.[5]

Function[edit]

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.[4][8][9][10][11] Meanwhile, reduced expression of PRDX5 induces cell susceptibility to oxidative damage and etoposide, doxorubicin, MPP+, and peroxide-induced apoptosis.[12][13][14][15] 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.[16][17][18] Interestingly, PRDX5 in Drosophila melanogaster has been shown to promote longevity in addition to antioxidant activity.[19]

Clinical significance[edit]

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.[20] In human breast cancer cells, knockdown of transcription factor, GATA1, led to increased expression of PRDX5 and inhibition of apoptosis.[8] A substantial increase in PRDX5 expression has been observed in astrocytes in multiple sclerosis lesion.[21] PRDX5 has also been identified as a candidate risk gene for the inflammatory disease, sarcoidosis.[22]

Interactions[edit]

Transcription factor GATA-binding protein 1 can bind to the PRDX5 gene and lead to increased expression of PRDX5.[8] PRDX5 has been shown to physically interact with PRDX1, PRDX2, PRDX6, SOD1, and PARK7 in at least two independent high-throughput proteomic analyses.[23]

References[edit]

  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ "PRDX5 peroxiredoxin 5 [Homo sapiens (human)]". NCBI. Retrieved 2016-07-19. 
  4. ^ a b c 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. 
  5. ^ a b c d e 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. 
  6. ^ 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. 
  7. ^ 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. 
  8. ^ a b c 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. 
  9. ^ 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. 
  10. ^ 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. 
  11. ^ 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. 
  12. ^ 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. 
  13. ^ 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. 
  14. ^ 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. 
  15. ^ 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. 
  16. ^ 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. 
  17. ^ 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. 
  18. ^ 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. 
  19. ^ 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 2842572Freely accessible. PMID 19128239. 
  20. ^ 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 3946812Freely accessible. PMID 24385276. 
  21. ^ 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. 
  22. ^ 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. 
  23. ^ Lab, Mike Tyers. "PRDX5 (SBBI10) Result Summary | BioGRID". thebiogrid.org. Retrieved 2016-07-19. 

Further reading[edit]

  • 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 16901Freely accessible. 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.