Peroxiredoxin 1
Peroxiredoxin-1 is a protein that in humans is encoded by the PRDX1 gene.[1][2]
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.[2]
Interactions
Peroxiredoxin 1 has been shown to interact with PRDX4.[3] A chemoproteomic approach has revealed that peroxiredoxin 1 is the main target of theonellasterone.[4]
Clinical Significance
As enzymes that combat oxidative stress, peroxiredoxins play an important role in health and disease.[5] Peroxiredoxin 1 and peroxiredoxin 2 have been shown to be released by some cells when stimulated by LPS or TNF-alpha.[6] The released peroxiredoxin can then act to produce inflammatory cytokines.[6] 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.[7] 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.[8] 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.[8] The expression patterns of peroxiredoxin 1 along with peroxiredoxin 4 are involved in human lung cancer malignancy.[9] 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.[10]
References
- ↑ Prosperi MT, Ferbus D, Karczinski I, Goubin G (June 1993). "A human cDNA corresponding to a gene overexpressed during cell proliferation encodes a product sharing homology with amoebic and bacterial proteins". J Biol Chem 268 (15): 11050–6. PMID 8496166.
- ↑ 2.0 2.1 "Entrez Gene: PRDX1 peroxiredoxin 1".
- ↑ Jin, D Y; Chae H Z; Rhee S G; Jeang K T (December 1997). "Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation". J. Biol. Chem. (UNITED STATES) 272 (49): 30952–61. doi:10.1074/jbc.272.49.30952. ISSN 0021-9258. PMID 9388242.
- ↑ Margarucci, L; Monti, M. C.; Tosco, A; Esposito, R; Zampella, A; Sepe, V; Mozzicafreddo, M; Riccio, R; Casapullo, A (2015). "Theonellasterone, a steroidal metabolite isolated from a Theonella sponge, protects peroxiredoxin-1 from oxidative stress reactions". Chem. Commun 51 (9): 1591–3. doi:10.1039/c4cc09205h. PMID 25503482.
- ↑ El Eter, E; Al-Masri, A. A. (2015). "Peroxiredoxin isoforms are associated with cardiovascular risk factors in type 2 diabetes mellitus". Brazilian Journal of Medical and Biological Research 0: 0. doi:10.1590/1414-431X20144142. PMID 25742636.
- ↑ 6.0 6.1 Mullen, L; Hanschmann, E. M.; Lillig, C. H.; Herzenberg, L. A.; Ghezzi, P (2015). "Cysteine Oxidation Targets Peroxiredoxins 1 and 2 for Exosomal Release through a Novel Mechanism of Redox-Dependent Secretion". Molecular medicine (Cambridge, Mass.). doi:10.2119/molmed.2015.00033 (inactive 2015-04-02). PMID 25715249.
- ↑ Cai, C. Y.; Zhai, L. L.; Wu, Y; Tang, Z. G. (2015). "Expression and clinical value of peroxiredoxin-1 in patients with pancreatic cancer". European Journal of Surgical Oncology (EJSO) 41 (2): 228–35. doi:10.1016/j.ejso.2014.11.037. PMID 25434328.
- ↑ 8.0 8.1 Gong, F; Hou, G; Liu, H; Zhang, M (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.
- ↑ Jiang, H; Wu, L; Mishra, M; Chawsheen, H. A.; 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.
- ↑ 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: 469358. doi:10.1155/2014/469358. PMC 4082880. PMID 25024510.
Further reading
- Wood ZA, Schröder E, Robin Harris J, Poole LB (2003). "Structure, mechanism and regulation of peroxiredoxins.". Trends Biochem. Sci. 28 (1): 32–40. doi:10.1016/S0968-0004(02)00003-8. PMID 12517450.
- Sauri H, Butterfield L, Kim A, Shau H (1995). "Antioxidant function of recombinant human natural killer enhancing factor.". Biochem. Biophys. Res. Commun. 208 (3): 964–9. doi:10.1006/bbrc.1995.1428. PMID 7702627.
- Shau H, Butterfield LH, Chiu R, Kim A (1994). "Cloning and sequence analysis of candidate human natural killer-enhancing factor genes.". Immunogenetics 40 (2): 129–34. doi:10.1007/BF00188176. PMID 8026862.
- Kawai S, Takeshita S, Okazaki M et al. (1994). "Cloning and characterization of OSF-3, a new member of the MER5 family, expressed in mouse osteoblastic cells.". J. Biochem. 115 (4): 641–3. PMID 8089076.
- Shau H, Kim A (1994). "Identification of natural killer enhancing factor as a major antioxidant in human red blood cells.". Biochem. Biophys. Res. Commun. 199 (1): 83–8. doi:10.1006/bbrc.1994.1197. PMID 8123050.
- Prospéri MT, Apiou F, Dutrillaux B, Goubin G (1994). "Organization and chromosomal assignment of two human PAG gene loci: PAGA encoding a functional gene and PAGB a processed pseudogene.". Genomics 19 (2): 236–41. doi:10.1006/geno.1994.1053. PMID 8188254.
- Wen ST, Van Etten RA (1997). "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.". Genes Dev. 11 (19): 2456–67. doi:10.1101/gad.11.19.2456. PMC 316562. PMID 9334312.
- Jin DY, Chae HZ, Rhee SG, Jeang KT (1998). "Regulatory role for a novel human thioredoxin peroxidase in NF-kappaB activation.". J. Biol. Chem. 272 (49): 30952–61. doi:10.1074/jbc.272.49.30952. PMID 9388242.
- Outinen PA, Sood SK, Pfeifer SI et al. (1999). "Homocysteine-induced endoplasmic reticulum stress and growth arrest leads to specific changes in gene expression in human vascular endothelial cells.". Blood 94 (3): 959–67. PMID 10419887.
- Yanagawa T, Ishikawa T, Ishii T et al. (1999). "Peroxiredoxin I expression in human thyroid tumors.". Cancer Lett. 145 (1–2): 127–32. doi:10.1016/S0304-3835(99)00243-8. PMID 10530780.
- Noh DY, Ahn SJ, Lee RA et al. (2001). "Overexpression of peroxiredoxin in human breast cancer". Anticancer Res. 21 (3B): 2085–90. PMID 11497302.
- Xu XR, Huang J, Xu ZG et al. (2002). "Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver". Proc. Natl. Acad. Sci. U.S.A. 98 (26): 15089–94. doi:10.1073/pnas.241522398. PMC 64988. PMID 11752456.
- Kim SH, Fountoulakis M, Cairns N, Lubec G (2002). "Protein levels of human peroxiredoxin subtypes in brains of patients with Alzheimer's disease and Down syndrome". J. Neural Transm. Suppl. (61): 223–35. doi:10.1007/978-3-7091-6262-0_18. PMID 11771746.
- Rabilloud T, Heller M, Gasnier F et al. (2002). "Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site". J. Biol. Chem. 277 (22): 19396–401. doi:10.1074/jbc.M106585200. PMID 11904290.
- Chang TS, Jeong W, Choi SY et al. (2002). "Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation". J. Biol. Chem. 277 (28): 25370–6. doi:10.1074/jbc.M110432200. PMID 11986303.
- 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.
- Shen C, Nathan C (2002). "Nonredundant antioxidant defense by multiple two-cysteine peroxiredoxins in human prostate cancer cells". Mol. Med. 8 (2): 95–102. PMC 2039972. PMID 12080185.
- Yang KS, Kang SW, Woo HA et al. (2002). "Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid". J. Biol. Chem. 277 (41): 38029–36. doi:10.1074/jbc.M206626200. PMID 12161445.
- Geiben-Lynn R, Kursar M, Brown NV et al. (2003). "HIV-1 antiviral activity of recombinant natural killer cell enhancing factors, NKEF-A and NKEF-B, members of the peroxiredoxin family". J. Biol. Chem. 278 (3): 1569–74. doi:10.1074/jbc.M209964200. PMID 12421812.
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