Peroxiredoxin 1

Peroxiredoxin-1 is a protein that in humans is encoded by the PRDX1 gene.[4][5]

PRDX1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPRDX1, MSP23, NKEF-A, NKEFA, PAG, PAGA, PAGB, PRX1, PRXI, TDPX2, Peroxiredoxin 1
External IDsOMIM: 176763 MGI: 99523 HomoloGene: 99789 GeneCards: PRDX1
Gene location (Human)
Chr.Chromosome 1 (human)[1]
Band1p34.1Start45,511,036 bp[1]
End45,523,047 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

5052

18477

Ensembl

ENSG00000117450

ENSMUSG00000028691

UniProt

Q06830

P35700

RefSeq (mRNA)

NM_181697
NM_001202431
NM_002574
NM_181696

NM_011034

RefSeq (protein)

NP_001189360
NP_002565
NP_859047
NP_859048

NP_035164

Location (UCSC)Chr 1: 45.51 – 45.52 Mbn/a
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

Function

This gene encodes a member of the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides.[6] 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.[5]

Interactions

Peroxiredoxin 1 has been shown to interact with PRDX4.[7] A chemoproteomic approach has revealed that peroxiredoxin 1 is the main target of theonellasterone.[8]

Clinical significance

As enzymes that combat oxidative stress, peroxiredoxins play an important role in health and disease.[9] Peroxiredoxin 1 and peroxiredoxin 2 have been shown to be released by some cells when stimulated by LPS or TNF-alpha.[10] The released peroxiredoxin can then act to produce inflammatory cytokines.[10] 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.[11] 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.[12] 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.[12] The expression patterns of peroxiredoxin 1 along with peroxiredoxin 4 are involved in human lung cancer malignancy.[13] 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.[14]

References
  1. GRCh38: Ensembl release 89: ENSG00000117450 - Ensembl, May 2017
  2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. 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.
  5. "Entrez Gene: PRDX1 peroxiredoxin 1".
  6. 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.
  7. 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.
  8. 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. doi:10.1039/c4cc09205h. PMID 25503482.
  9. 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.
  10. 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.
  11. 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.
  12. 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.
  13. 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.
  14. 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
  • Overview of all the structural information available in the PDB for UniProt: Q06830 (Peroxiredoxin-1) at the PDBe-KB.
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