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
↑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. PMID8496166.
↑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. PMID9388242.
↑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. PMID25503482.
↑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. PMID25434328.
↑ 9.09.1Gong 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. PMID25579166.
Wood ZA, Schröder E, Robin Harris J, Poole LB (Jan 2003). "Structure, mechanism and regulation of peroxiredoxins". Trends in Biochemical Sciences. 28 (1): 32–40. doi:10.1016/S0968-0004(02)00003-8. PMID12517450.
Sauri H, Butterfield L, Kim A, Shau H (Mar 1995). "Antioxidant function of recombinant human natural killer enhancing factor". Biochemical and Biophysical Research Communications. 208 (3): 964–9. doi:10.1006/bbrc.1995.1428. PMID7702627.
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. PMID8026862.
Kawai S, Takeshita S, Okazaki M, Kikuno R, Kudo A, Amann E (Apr 1994). "Cloning and characterization of OSF-3, a new member of the MER5 family, expressed in mouse osteoblastic cells". Journal of Biochemistry. 115 (4): 641–3. PMID8089076.
Shau H, Kim A (Feb 1994). "Identification of natural killer enhancing factor as a major antioxidant in human red blood cells". Biochemical and Biophysical Research Communications. 199 (1): 83–8. doi:10.1006/bbrc.1994.1197. PMID8123050.
Prospéri MT, Apiou F, Dutrillaux B, Goubin G (Jan 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. PMID8188254.
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. PMID9388242.
Outinen PA, Sood SK, Pfeifer SI, Pamidi S, Podor TJ, Li J, Weitz JI, Austin RC (Aug 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. PMID10419887.
Yanagawa T, Ishikawa T, Ishii T, Tabuchi K, Iwasa S, Bannai S, Omura K, Suzuki H, Yoshida H (Oct 1999). "Peroxiredoxin I expression in human thyroid tumors". Cancer Letters. 145 (1–2): 127–32. doi:10.1016/S0304-3835(99)00243-8. PMID10530780.
Noh DY, Ahn SJ, Lee RA, Kim SW, Park IA, Chae HZ (2001). "Overexpression of peroxiredoxin in human breast cancer". Anticancer Research. 21 (3B): 2085–90. PMID11497302.
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. Journal of Neural Transmission. Supplementum. pp. 223–35. doi:10.1007/978-3-7091-6262-0_18. ISBN978-3-211-83704-7. PMID11771746.
Rabilloud T, Heller M, Gasnier F, Luche S, Rey C, Aebersold R, Benahmed M, Louisot P, Lunardi J (May 2002). "Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site". The Journal of Biological Chemistry. 277 (22): 19396–401. doi:10.1074/jbc.M106585200. PMID11904290.
Chang TS, Jeong W, Choi SY, Yu S, Kang SW, Rhee SG (Jul 2002). "Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation". The Journal of Biological Chemistry. 277 (28): 25370–6. doi:10.1074/jbc.M110432200. PMID11986303.
Yang KS, Kang SW, Woo HA, Hwang SC, Chae HZ, Kim K, Rhee SG (Oct 2002). "Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid". The Journal of Biological Chemistry. 277 (41): 38029–36. doi:10.1074/jbc.M206626200. PMID12161445.
Geiben-Lynn R, Kursar M, Brown NV, Addo MM, Shau H, Lieberman J, Luster AD, Walker BD (Jan 2003). "HIV-1 antiviral activity of recombinant natural killer cell enhancing factors, NKEF-A and NKEF-B, members of the peroxiredoxin family". The Journal of Biological Chemistry. 278 (3): 1569–74. doi:10.1074/jbc.M209964200. PMID12421812.
