Peroxiredoxin 1: Difference between revisions

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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Peroxiredoxin-1''' is a [[protein]] that in humans is encoded by the ''PRDX1'' [[gene]].<ref name="pmid8496166">{{cite journal | vauthors = Prospéri MT, Ferbus D, Karczinski I, Goubin G | title = A human cDNA corresponding to a gene overexpressed during cell proliferation encodes a product sharing homology with amoebic and bacterial proteins | journal = The Journal of Biological Chemistry | volume = 268 | issue = 15 | pages = 11050–6 | date = May 1993 | pmid = 8496166 | pmc = | doi = }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: PRDX1 peroxiredoxin 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5052| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_PRDX1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1qq2.
| PDB = {{PDB2|1qq2}}
| Name = Peroxiredoxin 1
| HGNCid = 9352
| Symbol = PRDX1
| AltSymbols =; MSP23; NKEFA; PAG; PAGA; PAGB; TDPX2
| OMIM = 176763
| ECnumber = 
| Homologene = 21685
| MGIid = 99523
| GeneAtlas_image1 = PBB_GE_PRDX1_208680_at_tn.png
| Function = {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0051920 |text = peroxiredoxin activity}}
| Component =
| Process = {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0008283 |text = cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5052
    | Hs_Ensembl = ENSG00000117450
    | Hs_RefseqProtein = NP_002565
    | Hs_RefseqmRNA = NM_002574
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 45749295
    | Hs_GenLoc_end = 45760215
    | Hs_Uniprot = Q06830
    | Mm_EntrezGene = 18477
    | Mm_Ensembl = ENSMUSG00000028691
    | Mm_RefseqmRNA = NM_011034
    | Mm_RefseqProtein = NP_035164
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 4
    | Mm_GenLoc_start = 116183531
    | Mm_GenLoc_end = 116197932
    | Mm_Uniprot = Q3U9J9
  }}
}}
'''Peroxiredoxin 1''', also known as '''PRDX1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PRDX1 peroxiredoxin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5052| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes a member of the [[peroxiredoxin]] family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides <ref>{{cite journal |last1=Wu |first1=C |last2=Dai |first2=H |last3=Yan |first3=L |last4=Liu |first4=T |last5=Cui |first5=C |last6=Chen |first6=T |last7=Li |first7=H |title=Sulfonation of the resolving cysteine in human peroxiredoxin 1: A comprehensive analysis by mass spectrometry. |journal=Free Radical Biology & Medicine |date=July 2017 |volume=108 |pages=785–792 |doi=10.1016/j.freeradbiomed.2017.04.341 |pmid=28450148|pmc=5564515 }}</ref>. 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.<ref name="entrez"/>
{{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 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.<ref name="entrez">{{cite web | title = Entrez Gene: PRDX1 peroxiredoxin 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5052| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
 
==Further reading==
Peroxiredoxin 1 has been shown to [[Protein-protein interaction|interact]] with [[PRDX4]].<ref name=pmid9388242>{{cite journal | vauthors = Jin DY, Chae HZ, Rhee SG, Jeang KT | title = Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation | journal = The Journal of Biological Chemistry | volume = 272 | issue = 49 | pages = 30952–61 | date = Dec 1997 | pmid = 9388242 | doi = 10.1074/jbc.272.49.30952 }}</ref> A chemoproteomic approach has revealed that peroxiredoxin 1 is the main target of theonellasterone.<ref>{{cite journal | vauthors = Margarucci L, Monti MC, Tosco A, Esposito R, Zampella A, Sepe V, Mozzicafreddo M, Riccio R, Casapullo A | title = Theonellasterone, a steroidal metabolite isolated from a Theonella sponge, protects peroxiredoxin-1 from oxidative stress reactions | journal = Chemical Communications | volume = 51 | issue = 9 | pages = 1591–3 | date = Jan 2015 | pmid = 25503482 | doi = 10.1039/c4cc09205h | bibcode = 2008ChCom..44.5292T }}</ref>
 
== Clinical significance ==
 
As enzymes that combat [[oxidative stress]], peroxiredoxins play an important role in health and disease.<ref>{{cite journal | vauthors = El Eter E, Al-Masri AA | title = Peroxiredoxin isoforms are associated with cardiovascular risk factors in type 2 diabetes mellitus | journal = Brazilian Journal of Medical and Biological Research | volume = 48 | issue = 5 | pages = 465–9 | date = May 2015 | pmid = 25742636 | pmc = 4445671 | doi = 10.1590/1414-431X20144142 }}</ref> Peroxiredoxin 1 and peroxiredoxin 2 have been shown to be released by some cells when stimulated by LPS or TNF-alpha.<ref name="cite PMID| 25715249">{{cite journal | vauthors = Mullen L, Hanschmann EM, Lillig CH, Herzenberg LA, Ghezzi P | title = Cysteine Oxidation Targets Peroxiredoxins 1 and 2 for Exosomal Release through a Novel Mechanism of Redox-Dependent Secretion | journal = Molecular Medicine | volume = 21 | pages = 98–108 | year = 2015 | pmid = 25715249 | pmc = 4461588 | doi = 10.2119/molmed.2015.00033 }}</ref> The released peroxiredoxin can then act to produce inflammatory [[cytokines]].<ref name="cite PMID| 25715249"/> The levels of peroxiredoxin 1 are elevated in pancreatic cancer and it can potentially act as a marker for the diagnosis and prognosis of this disease.<ref>{{cite journal | vauthors = Cai CY, Zhai LL, Wu Y, Tang ZG | title = Expression and clinical value of peroxiredoxin-1 in patients with pancreatic cancer | journal = European Journal of Surgical Oncology | volume = 41 | issue = 2 | pages = 228–35 | date = Feb 2015 | pmid = 25434328 | doi = 10.1016/j.ejso.2014.11.037 }}</ref> In some types of [[cancer]], peroxiredoxin 1 has been determined to act as a tumor suppressor and other studies show that peroxiredoxin 1 is overexpressed in certain human cancers.<ref name="cite PMID| 25579166">{{cite journal | vauthors = Gong F, Hou G, Liu H, Zhang M | title = Peroxiredoxin 1 promotes tumorigenesis through regulating the activity of mTOR/p70S6K pathway in esophageal squamous cell carcinoma | journal = Medical Oncology | volume = 32 | issue = 2 | pages = 455 | date = Feb 2015 | pmid = 25579166 | doi = 10.1007/s12032-014-0455-0 }}</ref> A recent study has found that peroxiredoxin 1 may play a role in [[tumorigenesis]] by regulating the mTOR/p70S6K pathway in esophageal squamous cell carcinoma.<ref name="cite PMID| 25579166"/> The expression patterns of peroxiredoxin 1 along with peroxiredoxin 4 are involved in human lung cancer malignancy.<ref>{{cite journal | vauthors = Jiang H, Wu L, Mishra M, Chawsheen HA, Wei Q | title = Expression of peroxiredoxin 1 and 4 promotes human lung cancer malignancy | journal = American Journal of Cancer Research | volume = 4 | issue = 5 | pages = 445–60 | year = 2014 | pmid = 25232487 | pmc = 4163610 }}</ref> It has also been shown that peroxiredoxin 1 may be an important player in the pathogenesis of acute respiratory distress syndrome because of its role in promoting inflammation.<ref>{{cite journal | vauthors = Liu D, Mao P, Huang Y, Liu Y, Liu X, Pang X, Li Y | title = Proteomic analysis of lung tissue in a rat acute lung injury model: identification of PRDX1 as a promoter of inflammation | journal = Mediators of Inflammation | volume = 2014 | pages = 1–14 | year = 2014 | pmid = 25024510 | pmc = 4082880 | doi = 10.1155/2014/469358 }}</ref>
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{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 = Jan 2003 | pmid = 12517450 | doi = 10.1016/S0968-0004(02)00003-8 }}
| citations =
* {{cite journal | vauthors = Sauri H, Butterfield L, Kim A, Shau H | title = Antioxidant function of recombinant human natural killer enhancing factor | journal = Biochemical and Biophysical Research Communications | volume = 208 | issue = 3 | pages = 964–9 | date = Mar 1995 | pmid = 7702627 | doi = 10.1006/bbrc.1995.1428 }}
*{{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= }}
* {{cite journal | vauthors = Shau H, Butterfield LH, Chiu R, Kim A | title = Cloning and sequence analysis of candidate human natural killer-enhancing factor genes | journal = Immunogenetics | volume = 40 | issue = 2 | pages = 129–34 | year = 1994 | pmid = 8026862 | doi = 10.1007/BF00188176 }}
*{{cite journal | author=Sauri H, Butterfield L, Kim A, Shau H |title=Antioxidant function of recombinant human natural killer enhancing factor. |journal=Biochem. Biophys. Res. Commun. |volume=208 |issue= 3 |pages= 964-9 |year= 1995 |pmid= 7702627 |doi= }}
* {{cite journal | vauthors = Kawai S, Takeshita S, Okazaki M, Kikuno R, Kudo A, Amann E | title = Cloning and characterization of OSF-3, a new member of the MER5 family, expressed in mouse osteoblastic cells | journal = Journal of Biochemistry | volume = 115 | issue = 4 | pages = 641–3 | date = Apr 1994 | pmid = 8089076 | doi =  }}
*{{cite journal | author=Shau H, Butterfield LH, Chiu R, Kim A |title=Cloning and sequence analysis of candidate human natural killer-enhancing factor genes. |journal=Immunogenetics |volume=40 |issue= 2 |pages= 129-34 |year= 1994 |pmid= 8026862 |doi= }}
* {{cite journal | vauthors = Shau H, Kim A | title = Identification of natural killer enhancing factor as a major antioxidant in human red blood cells | journal = Biochemical and Biophysical Research Communications | volume = 199 | issue = 1 | pages = 83–8 | date = Feb 1994 | pmid = 8123050 | doi = 10.1006/bbrc.1994.1197 }}
*{{cite journal | author=Kawai S, Takeshita S, Okazaki M, ''et al.'' |title=Cloning and characterization of OSF-3, a new member of the MER5 family, expressed in mouse osteoblastic cells. |journal=J. Biochem. |volume=115 |issue= 4 |pages= 641-3 |year= 1994 |pmid= 8089076 |doi=  }}
* {{cite journal | vauthors = Prospéri MT, Apiou F, Dutrillaux B, Goubin G | title = Organization and chromosomal assignment of two human PAG gene loci: PAGA encoding a functional gene and PAGB a processed pseudogene | journal = Genomics | volume = 19 | issue = 2 | pages = 236–41 | date = Jan 1994 | pmid = 8188254 | doi = 10.1006/geno.1994.1053 }}
*{{cite journal | author=Shau H, Kim A |title=Identification of natural killer enhancing factor as a major antioxidant in human red blood cells. |journal=Biochem. Biophys. Res. Commun. |volume=199 |issue= 1 |pages= 83-8 |year= 1994 |pmid= 8123050 |doi= }}
* {{cite journal | vauthors = Wen ST, Van Etten RA | title = 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 | journal = Genes & Development | volume = 11 | issue = 19 | pages = 2456–67 | date = Oct 1997 | pmid = 9334312 | pmc = 316562 | doi = 10.1101/gad.11.19.2456 }}
*{{cite journal | author=Prospéri MT, Apiou F, Dutrillaux B, Goubin G |title=Organization and chromosomal assignment of two human PAG gene loci: PAGA encoding a functional gene and PAGB a processed pseudogene. |journal=Genomics |volume=19 |issue= 2 |pages= 236-41 |year= 1994 |pmid= 8188254 |doi= 10.1006/geno.1994.1053 }}
* {{cite journal | vauthors = Jin DY, Chae HZ, Rhee SG, Jeang KT | title = Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation | journal = The Journal of Biological Chemistry | volume = 272 | issue = 49 | pages = 30952–61 | date = Dec 1997 | pmid = 9388242 | doi = 10.1074/jbc.272.49.30952 }}
*{{cite journal | author=Prospéri MT, Ferbus D, Karczinski I, Goubin G |title=A human cDNA corresponding to a gene overexpressed during cell proliferation encodes a product sharing homology with amoebic and bacterial proteins. |journal=J. Biol. Chem. |volume=268 |issue= 15 |pages= 11050-6 |year= 1993 |pmid= 8496166 |doi= }}
* {{cite journal | vauthors = Outinen PA, Sood SK, Pfeifer SI, Pamidi S, Podor TJ, Li J, Weitz JI, Austin RC | title = Homocysteine-induced endoplasmic reticulum stress and growth arrest leads to specific changes in gene expression in human vascular endothelial cells | journal = Blood | volume = 94 | issue = 3 | pages = 959–67 | date = Aug 1999 | pmid = 10419887 | doi =  }}
*{{cite journal | author=Wen ST, Van Etten RA |title=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. |journal=Genes Dev. |volume=11 |issue= 19 |pages= 2456-67 |year= 1997 |pmid= 9334312 |doi= }}
* {{cite journal | vauthors = Yanagawa T, Ishikawa T, Ishii T, Tabuchi K, Iwasa S, Bannai S, Omura K, Suzuki H, Yoshida H | title = Peroxiredoxin I expression in human thyroid tumors | journal = Cancer Letters | volume = 145 | issue = 1–2 | pages = 127–32 | date = Oct 1999 | pmid = 10530780 | doi = 10.1016/S0304-3835(99)00243-8 }}
*{{cite journal | author=Jin DY, Chae HZ, Rhee SG, Jeang KT |title=Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation. |journal=J. Biol. Chem. |volume=272 |issue= 49 |pages= 30952-61 |year= 1998 |pmid= 9388242 |doi=  }}
* {{cite journal | vauthors = Noh DY, Ahn SJ, Lee RA, Kim SW, Park IA, Chae HZ | title = Overexpression of peroxiredoxin in human breast cancer | journal = Anticancer Research | volume = 21 | issue = 3B | pages = 2085–90 | year = 2001 | pmid = 11497302 | doi =  }}
*{{cite journal | author=Outinen PA, Sood SK, Pfeifer SI, ''et al.'' |title=Homocysteine-induced endoplasmic reticulum stress and growth arrest leads to specific changes in gene expression in human vascular endothelial cells. |journal=Blood |volume=94 |issue= 3 |pages= 959-67 |year= 1999 |pmid= 10419887 |doi= }}
* {{cite journal | vauthors = Xu XR, Huang J, Xu ZG, Qian BZ, Zhu ZD, Yan Q, Cai T, Zhang X, Xiao HS, Qu J, Liu F, Huang QH, Cheng ZH, Li NG, Du JJ, Hu W, Shen KT, Lu G, Fu G, Zhong M, Xu SH, Gu WY, Huang W, Zhao XT, Hu GX, Gu JR, Chen Z, Han ZG | title = Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 98 | issue = 26 | pages = 15089–94 | date = Dec 2001 | pmid = 11752456 | pmc = 64988 | doi = 10.1073/pnas.241522398 | bibcode = 2001PNAS...9815089X }}
*{{cite journal | author=Yanagawa T, Ishikawa T, Ishii T, ''et al.'' |title=Peroxiredoxin I expression in human thyroid tumors. |journal=Cancer Lett. |volume=145 |issue= 1-2 |pages= 127-32 |year= 1999 |pmid= 10530780 |doi=  }}
* {{Cite book | vauthors = Kim SH, Fountoulakis M, Cairns N, Lubec G | title = Protein levels of human peroxiredoxin subtypes in brains of patients with Alzheimer's disease and Down syndrome | journal = Journal of Neural Transmission. Supplementum | volume = | issue = 61 | pages = 223–35 | year = 2002 | pmid = 11771746 | doi = 10.1007/978-3-7091-6262-0_18 | isbn = 978-3-211-83704-7 }}
*{{cite journal | author=Noh DY, Ahn SJ, Lee RA, ''et al.'' |title=Overexpression of peroxiredoxin in human breast cancer. |journal=Anticancer Res. |volume=21 |issue= 3B |pages= 2085-90 |year= 2001 |pmid= 11497302 |doi= }}
* {{cite journal | vauthors = Rabilloud T, Heller M, Gasnier F, Luche S, Rey C, Aebersold R, Benahmed M, Louisot P, Lunardi J | title = Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site | journal = The Journal of Biological Chemistry | volume = 277 | issue = 22 | pages = 19396–401 | date = May 2002 | pmid = 11904290 | doi = 10.1074/jbc.M106585200 }}
*{{cite journal  | author=Xu XR, Huang J, Xu ZG, ''et al.'' |title=Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 26 |pages= 15089-94 |year= 2002 |pmid= 11752456 |doi= 10.1073/pnas.241522398 }}
* {{cite journal | vauthors = Chang TS, Jeong W, Choi SY, Yu S, Kang SW, Rhee SG | title = Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation | journal = The Journal of Biological Chemistry | volume = 277 | issue = 28 | pages = 25370–6 | date = Jul 2002 | pmid = 11986303 | doi = 10.1074/jbc.M110432200 }}
*{{cite journal | author=Kim SH, Fountoulakis M, Cairns N, Lubec G |title=Protein levels of human peroxiredoxin subtypes in brains of patients with Alzheimer's disease and Down syndrome. |journal=J. Neural Transm. Suppl. |volume= |issue= 61 |pages= 223-35 |year= 2002 |pmid= 11771746 |doi= }}
* {{cite journal | vauthors = Wagner E, Luche S, Penna L, Chevallet M, Van Dorsselaer A, Leize-Wagner E, Rabilloud T | title = A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress | journal = The Biochemical Journal | volume = 366 | issue = Pt 3 | pages = 777–85 | date = Sep 2002 | pmid = 12059788 | pmc = 1222825 | doi = 10.1042/BJ20020525 }}
*{{cite journal | author=Rabilloud T, Heller M, Gasnier F, ''et al.'' |title=Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site. |journal=J. Biol. Chem. |volume=277 |issue= 22 |pages= 19396-401 |year= 2002 |pmid= 11904290 |doi= 10.1074/jbc.M106585200 }}
* {{cite journal | vauthors = Shen C, Nathan C | title = Nonredundant antioxidant defense by multiple two-cysteine peroxiredoxins in human prostate cancer cells | journal = Molecular Medicine | volume = 8 | issue = 2 | pages = 95–102 | date = Feb 2002 | pmid = 12080185 | pmc = 2039972 | doi = }}
*{{cite journal | author=Chang TS, Jeong W, Choi SY, ''et al.'' |title=Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation. |journal=J. Biol. Chem. |volume=277 |issue= 28 |pages= 25370-6 |year= 2002 |pmid= 11986303 |doi= 10.1074/jbc.M110432200 }}
* {{cite journal | vauthors = Yang KS, Kang SW, Woo HA, Hwang SC, Chae HZ, Kim K, Rhee SG | title = Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid | journal = The Journal of Biological Chemistry | volume = 277 | issue = 41 | pages = 38029–36 | date = Oct 2002 | pmid = 12161445 | doi = 10.1074/jbc.M206626200 }}
*{{cite journal | author=Wagner E, Luche S, Penna L, ''et al.'' |title=A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress. |journal=Biochem. J. |volume=366 |issue= Pt 3 |pages= 777-85 |year= 2002 |pmid= 12059788 |doi= 10.1042/BJ20020525 }}
* {{cite journal | vauthors = Geiben-Lynn R, Kursar M, Brown NV, Addo MM, Shau H, Lieberman J, Luster AD, Walker BD | title = HIV-1 antiviral activity of recombinant natural killer cell enhancing factors, NKEF-A and NKEF-B, members of the peroxiredoxin family | journal = The Journal of Biological Chemistry | volume = 278 | issue = 3 | pages = 1569–74 | date = Jan 2003 | pmid = 12421812 | doi = 10.1074/jbc.M209964200 }}
*{{cite journal | author=Shen C, Nathan C |title=Nonredundant antioxidant defense by multiple two-cysteine peroxiredoxins in human prostate cancer cells. |journal=Mol. Med. |volume=8 |issue= 2 |pages= 95-102 |year= 2002 |pmid= 12080185 |doi= }}
*{{cite journal | author=Yang KS, Kang SW, Woo HA, ''et al.'' |title=Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid. |journal=J. Biol. Chem. |volume=277 |issue= 41 |pages= 38029-36 |year= 2002 |pmid= 12161445 |doi= 10.1074/jbc.M206626200 }}
*{{cite journal  | author=Geiben-Lynn R, Kursar M, Brown NV, ''et al.'' |title=HIV-1 antiviral activity of recombinant natural killer cell enhancing factors, NKEF-A and NKEF-B, members of the peroxiredoxin family. |journal=J. Biol. Chem. |volume=278 |issue= 3 |pages= 1569-74 |year= 2003 |pmid= 12421812 |doi= 10.1074/jbc.M209964200 }}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=5052}}


{{protein-stub}}
{{Peroxidases}}

Latest revision as of 06:50, 27 September 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
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View/Edit Human

Peroxiredoxin-1 is a protein that in humans is encoded by the PRDX1 gene.[1][2]

Function

This gene encodes a member of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides [3]. 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.[2]

Interactions

Peroxiredoxin 1 has been shown to interact with PRDX4.[4] A chemoproteomic approach has revealed that peroxiredoxin 1 is the main target of theonellasterone.[5]

Clinical significance

As enzymes that combat oxidative stress, peroxiredoxins play an important role in health and disease.[6] Peroxiredoxin 1 and peroxiredoxin 2 have been shown to be released by some cells when stimulated by LPS or TNF-alpha.[7] The released peroxiredoxin can then act to produce inflammatory cytokines.[7] The levels of peroxiredoxin 1 are elevated in pancreatic cancer and it can potentially act as a marker for the diagnosis and prognosis of this disease.[8] In some types of cancer, peroxiredoxin 1 has been determined to act as a tumor suppressor and other studies show that peroxiredoxin 1 is overexpressed in certain human cancers.[9] A recent study has found that peroxiredoxin 1 may play a role in tumorigenesis by regulating the mTOR/p70S6K pathway in esophageal squamous cell carcinoma.[9] The expression patterns of peroxiredoxin 1 along with peroxiredoxin 4 are involved in human lung cancer malignancy.[10] It has also been shown that peroxiredoxin 1 may be an important player in the pathogenesis of acute respiratory distress syndrome because of its role in promoting inflammation.[11]

References

  1. ↑ Prospéri MT, Ferbus D, Karczinski I, Goubin G (May 1993). "A human cDNA corresponding to a gene overexpressed during cell proliferation encodes a product sharing homology with amoebic and bacterial proteins". The Journal of Biological Chemistry. 268 (15): 11050–6. PMID 8496166.
  2. ↑ 2.0 2.1 "Entrez Gene: PRDX1 peroxiredoxin 1".
  3. ↑ Wu, C; Dai, H; Yan, L; Liu, T; Cui, C; Chen, T; Li, H (July 2017). "Sulfonation of the resolving cysteine in human peroxiredoxin 1: A comprehensive analysis by mass spectrometry". Free Radical Biology & Medicine. 108: 785–792. doi:10.1016/j.freeradbiomed.2017.04.341. PMC 5564515. PMID 28450148.
  4. ↑ Jin DY, Chae HZ, Rhee SG, Jeang KT (Dec 1997). "Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation". The Journal of Biological Chemistry. 272 (49): 30952–61. doi:10.1074/jbc.272.49.30952. PMID 9388242.
  5. ↑ Margarucci L, Monti MC, Tosco A, Esposito R, Zampella A, Sepe V, Mozzicafreddo M, Riccio R, Casapullo A (Jan 2015). "Theonellasterone, a steroidal metabolite isolated from a Theonella sponge, protects peroxiredoxin-1 from oxidative stress reactions". Chemical Communications. 51 (9): 1591–3. Bibcode:2008ChCom..44.5292T. doi:10.1039/c4cc09205h. PMID 25503482.
  6. ↑ El Eter E, Al-Masri AA (May 2015). "Peroxiredoxin isoforms are associated with cardiovascular risk factors in type 2 diabetes mellitus". Brazilian Journal of Medical and Biological Research. 48 (5): 465–9. doi:10.1590/1414-431X20144142. PMC 4445671. PMID 25742636.
  7. ↑ 7.0 7.1 Mullen L, Hanschmann EM, Lillig CH, Herzenberg LA, Ghezzi P (2015). "Cysteine Oxidation Targets Peroxiredoxins 1 and 2 for Exosomal Release through a Novel Mechanism of Redox-Dependent Secretion". Molecular Medicine. 21: 98–108. doi:10.2119/molmed.2015.00033. PMC 4461588. PMID 25715249.
  8. ↑ Cai CY, Zhai LL, Wu Y, Tang ZG (Feb 2015). "Expression and clinical value of peroxiredoxin-1 in patients with pancreatic cancer". European Journal of Surgical Oncology. 41 (2): 228–35. doi:10.1016/j.ejso.2014.11.037. PMID 25434328.
  9. ↑ 9.0 9.1 Gong F, Hou G, Liu H, Zhang M (Feb 2015). "Peroxiredoxin 1 promotes tumorigenesis through regulating the activity of mTOR/p70S6K pathway in esophageal squamous cell carcinoma". Medical Oncology. 32 (2): 455. doi:10.1007/s12032-014-0455-0. PMID 25579166.
  10. ↑ Jiang H, Wu L, Mishra M, Chawsheen HA, Wei Q (2014). "Expression of peroxiredoxin 1 and 4 promotes human lung cancer malignancy". American Journal of Cancer Research. 4 (5): 445–60. PMC 4163610. PMID 25232487.
  11. ↑ Liu D, Mao P, Huang Y, Liu Y, Liu X, Pang X, Li Y (2014). "Proteomic analysis of lung tissue in a rat acute lung injury model: identification of PRDX1 as a promoter of inflammation". Mediators of Inflammation. 2014: 1–14. doi:10.1155/2014/469358. PMC 4082880. PMID 25024510.

Further reading

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