PRDX3

Jump to navigation Jump to search
VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

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

Thioredoxin-dependent peroxide reductase, mitochondrial is an enzyme that in humans is encoded by the PRDX3 gene.[1][2][3] It is a member of the peroxiredoxin family of antioxidant enzymes.

Function

This gene encodes a protein with antioxidant function and is localized in the mitochondrion. This gene shows significant nucleotide sequence similarity to the gene coding for the C22 subunit of Salmonella typhimurium alkylhydroperoxide reductase. Expression of this gene product in E. coli deficient in the C22-subunit gene rescued resistance of the bacteria to alkylhydroperoxide. The human and mouse genes are highly conserved, and they map to the regions syntenic between mouse and human chromosomes. Sequence comparisons with recently cloned mammalian homologues suggest that these genes consist of a family that is responsible for regulation of cellular proliferation, differentiation, and antioxidant functions. Two transcript variants encoding two different isoforms have been found for this gene.[3]

Interactions

PRDX3 has been shown to interact with MAP3K13.[4]

Clinical significance

It has been demonstrated that serum peroxiredoxin 3 can be a valuable biomarker for the diagnosis and assessment of hepatocellular carcinoma[5] It has been shown that peroxiredoxin proteins protect MCF-7 breast cancer cells against doxorubicin-mediated toxicity.[6] Additionally, it has been shown that peroxiredoxin 3 is overexpressed in prostate cancer and promotes cancer cell survival by defending cells against the damages incurred by oxidative stress.[7]

References

  1. Tsuji K, Copeland NG, Jenkins NA, Obinata M (May 1995). "Mammalian antioxidant protein complements alkylhydroperoxide reductase (ahpC) mutation in Escherichia coli". Biochem. J. 307 (2): 377–81. doi:10.1042/bj3070377. PMC 1136659. PMID 7733872.
  2. Watabe S, Hiroi T, Yamamoto Y, Fujioka Y, Hasegawa H, Yago N, Takahashi SY (Dec 1997). "SP-22 is a thioredoxin-dependent peroxide reductase in mitochondria". Eur. J. Biochem. 249 (1): 52–60. doi:10.1111/j.1432-1033.1997.t01-1-00052.x. PMID 9363753.
  3. 3.0 3.1 "Entrez Gene: PRDX3 peroxiredoxin 3".
  4. Masaki M, Ikeda A, Shiraki E, Oka S, Kawasaki T (Jan 2003). "Mixed lineage kinase LZK and antioxidant protein-1 activate NF-kappaB synergistically". Eur. J. Biochem. 270 (1): 76–83. doi:10.1046/j.1432-1033.2003.03363.x. PMID 12492477.
  5. Shi L, Wu LL, Yang JR, Chen XF, Zhang Y, Chen ZQ, Liu CL, Chi SY, Zheng JY, Huang HX, Yu FJ, Lin XY (2014). "Serum peroxiredoxin3 is a useful biomarker for early diagnosis and assessment of prognosis of hepatocellular carcinoma in Chinese patients". Asian Pacific Journal of Cancer Prevention. 15 (7): 2979–86. doi:10.7314/apjcp.2014.15.7.2979. PMID 24815434.
  6. McDonald C, Muhlbauer J, Perlmutter G, Taparra K, Phelan SA (Jul 2014). "Peroxiredoxin proteins protect MCF-7 breast cancer cells from doxorubicin-induced toxicity". International Journal of Oncology. 45 (1): 219–26. doi:10.3892/ijo.2014.2398. PMID 24789097.
  7. Whitaker HC, Patel D, Howat WJ, Warren AY, Kay JD, Sangan T, Marioni JC, Mitchell J, Aldridge S, Luxton HJ, Massie C, Lynch AG, Neal DE (Aug 2013). "Peroxiredoxin-3 is overexpressed in prostate cancer and promotes cancer cell survival by protecting cells from oxidative stress". British Journal of Cancer. 109 (4): 983–93. doi:10.1038/bjc.2013.396. PMC 3749568. PMID 23880827.

Further reading