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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Peroxiredoxin 3

peroxiredoxin 3, Prx III, PRDX3, MER5
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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Thioredoxin, Ros, fibrillin-1, CAN, HAD
Papers using peroxiredoxin 3 antibodies
Thioredoxin peroxidase is a novel inhibitor of apoptosis with a mechanism distinct from that of Bcl-2
Winyard Paul G. et al., In The International Journal of Biochemistry & Cell Biology, 1996
... Recombinant human Prdx2 and Prdx3 were obtained from AbFrontier (Seoul, South Korea), and ...
Papers on peroxiredoxin 3
Quantitative tissue proteomic investigation of invasive ductal carcinoma of breast with luminal B HER2 positive and HER2 enriched subtypes towards potential diagnostic and therapeutic biomarkers.
Rapole et al., Pune, India. In J Proteomics, Mar 2016
Immunoblotting and MRM based validation in a separate cohort of samples confirmed that panel of biosignatures for LB are APOA1, GELS, HS90B, EF1A1, NHRF1 and PRDX3 and for HE are PRDX1, CATD, CALR, ATPB and CH60.
Loss of Peroxiredoxin Expression Is Associated with an Aggressive Phenotype in Pancreatic Adenocarcinoma.
Karihtala et al., Oulu, Finland. In Anticancer Res, Jan 2016
Stronger cytoplasmic Prx III expression was associated with node negativity (p=0.007) and better tumor differentiation (p=0.033).
The functional role of peroxiredoxin 3 in reactive oxygen species, apoptosis, and chemoresistance of cancer cells.
Yu et al., Yantai, China. In J Cancer Res Clin Oncol, Dec 2015
Different from other members, PRX3 is predominantly located in mitochondria, a major apoptosis mediator.
Cytoprotective effect of Makgeolli lees on paraquat induced oxidative stress in A549 cells via activation of NRF2 and antioxidant genes.
Kim et al., South Korea. In J Microbiol Biotechnol, Dec 2015
Moreover, we found that expression of cytoprotective genes including glutathione peroxidases (GPXs), superoxide dismutase (SOD1), catalase (CAT), peroxiredoxin 3 (PRDX3), and peroxiredoxin 4 (PRDX4) was greatly enhanced by treatment with ML during PQ exposure.
Expression and distribution of peroxiredoxins in the retina and optic nerve.
Casson et al., Adelaide, Australia. In Brain Struct Funct, Nov 2015
In the retina, Prdx1 and Prdx2 were principally localized to neurons in the inner nuclear layer and cone photoreceptors, Prdx3 and Prdx5 displayed characteristic mitochondrial immunolabeling, while Prdx6 was associated with astrocytes and Müller cells.
FOXM1-Induced PRX3 Regulates Stemness and Survival of Colon Cancer Cells via Maintenance of Mitochondrial Function.
Han et al., Pusan, South Korea. In Gastroenterology, Oct 2015
We used immunohistochemistry and quantitative polymerase chain reaction to compare expression of mitochondrial peroxiredoxin 3 (PRX3) in CD133(+)CD44(+) Lgr5(+)cells (CSCs) vs CD133(-)CD44(-)Lgr5(-) colon tumor cells (non-CSCs).
Mitochondrial metabolism in cancer stem cells: a therapeutic target for colon cancer.
Han et al., Pusan, South Korea. In Bmb Rep, Oct 2015
We also found that forkhead box protein 1 (FOXM1)-induced peroxiredoxin 3 (PRDX3) maintains the mitochondrial function, and the FOXM1/PRDX3 mitochondrial pathway maintains survival of colon CSCs.
Upregulation of peroxiredoxin III in doxorubicin-induced cytotoxicity and the FoxO3a-dependent expression in H9c2 cardiac cells.
Lin et al., Hengyang, China. In Exp Ther Med, Oct 2015
The aim of the present study was to investigate the role of peroxiredoxin III (Prx III) in DOX-induced H9c2 cell injuries.
NLRP3 inflammasome activation by mitochondrial reactive oxygen species plays a key role in long-term cognitive impairment induced by paraquat exposure.
Ran et al., San Antonio, United States. In Neurobiol Aging, Sep 2015
Moreover, transgenic mice overexpressing Prdx3, a key enzyme in detoxifying mitochondrial H2O2, had suppressed NLRP3 inflammasome activation, reduced brain inflammation, and attenuated cognition impairment after paraquat exposure.
The roles of redox enzymes in Parkinson's disease: Focus on glutaredoxin.
Mieyal et al., Cleveland, United States. In Ther Targets Neurol Dis, 2014
Dysregulation of redox proteins in PD is highlighted by some of the work detailing the roles of peroxiredoxin-3 and thioredoxin-1 in models of PD.
Clinical relevance of thyroid cell models in redox research.
Laukkanen et al., Napoli, Italy. In Cancer Cell Int, 2014
RESULTS: Based on the current results, rat thyroid PC Cl3, PC PTC1, PC E1A, or FRLT5 cell models can be used to study NOX2, NOX4, SOD2, SOD3, CATALASE, GPX1, GPX2, GPX5, PRDX2, and PRDX3 gene expression and function.
MicroRNA-23b downregulates peroxiredoxin III in human prostate cancer.
Zhong et al., Guangzhou, China. In Febs Lett, 2012
the effects of PRDX3 in PCa progression may be caused by the regulation function of miR-23b, and consequently, miR-23b may be involved in the response of PCa cells to hypoxia stress
Detection and identification of peroxiredoxin 3 as a biomarker in hepatocellular carcinoma by a proteomic approach.
Ye et al., Changsha, China. In Int J Mol Med, 2012
The results indicated that overexpression of PRDX3 was associated with 94.9% hepatocellular carcinoma, and correlated with poor differentiation (P<0.05), which suggest that PRDX3 has substantial clinical impact on the progression of hepatocarcinoma.
Peroxiredoxins 3 and 4 are overexpressed in prostate cancer tissue and affect the proliferation of prostate cancer cells in vitro.
Balabanov et al., Hamburg, Germany. In J Proteome Res, 2012
Reverse phase protein arrays verified that the overexpression of both PRDX3 and PRDX4 in prostate tumor samples is negatively correlated with the presence of the TMPRSS2-ERG gene fusion.
Oxidative stress in Fanconi anaemia: from cells and molecules towards prospects in clinical management.
Degan et al., Napoli, Italy. In Biol Chem, 2012
Some FA gene products involved in redox homeostasis can be summarized as follows: (a) FANCA, FANCC, and FANCG interact with cytochrome P450-related activities and/or respond to oxidative damage; (b) FANCD2 in OS response interacts with forkhead box O3 and ataxia telangiectasia mutated protein; (c) FANCG is found in mitochondria and interacts with PRDX3, and FA-G cells display distorted mitochondria and decreased peroxidase activity; (d) FANCJ (BACH1/BRIP1) is a repressor of haeme oxygenase-1 gene and senses oxidative base damage; (e) antioxidants, such as tempol and resveratrol decrease cancer incidence and haematopoietic defects in Fancd2(-/-) mice.
Single nucleotide polymorphisms in the PRDX3 and RPS19 and risk of HPV persistence and cervical precancer/cancer.
Wang et al., Bethesda, United States. In Plos One, 2011
Single nucleotide polymorphisms in the PRDX3 and RPS19 is associated with HPV persistence and cervical precancer/cancer.
Nuclear factor E2-related factor 2 dependent overexpression of sulfiredoxin and peroxiredoxin III in human lung cancer.
Hwang et al., Suwŏn, South Korea. In Korean J Intern Med, 2011
Report nuclear factor E2-related factor 2 dependent overexpression of sulfiredoxin and peroxiredoxin III in human lung cancer.
Mitochondrial peroxiredoxin III is a potential target for cancer therapy.
Han et al., Pusan, South Korea. In Int J Mol Sci, 2010
The peroxiredoxin (Prx) system is a cellular defense system against oxidative stress, and mitochondria in cancer cells are known to contain high levels of Prx III.
Mitochondrial oxidative stress and dysfunction in myocardial remodelling.
Matsushima et al., Sapporo, Japan. In Cardiovasc Res, 2009
Overexpression of the genes for peroxiredoxin-3 (Prx-3), a mitochondrial antioxidant, or mitochondrial transcription factor A (TFAM), could ameliorate the decline in mtDNA copy number in failing hearts.
Oxidative stress and mitochondrial DNA damage in heart failure.
Matsushima et al., Sapporo, Japan. In Circ J, 2007
Overexpression of peroxiredoxin-3 (Prx-3), mitochondrial antioxidant, or mitochondrial transcription factor A (TFAM) could ameliorate the decline in mtDNA copy number in failing hearts.
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