gopubmed logo
find other proteinsAll proteins
GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Peroxiredoxin 4

PRDX4, peroxiredoxin 4, Peroxiredoxin IV, Prx4, AOE372, Prx-IV
The protein encoded by this gene is an antioxidant enzyme and belongs to the peroxiredoxin family. The protein is localized to the cytoplasm. Peroxidases of the peroxiredoxin family reduce hydrogen peroxide and alkyl hydroperoxides to water and alcohol with the use of reducing equivalents derived from thiol-containing donor molecules. This protein has been found to play a regulatory role in the activation of the transcription factor NF-kappaB. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: fibrillin-1, Thioredoxin, CAN, HAD, V1a
Papers using PRDX4 antibodies
Calcium-G protein interactions in the regulation of macrophage secretion
Malik Asrar B. et al., In Nature Immunology, 2000
... Overexpression of peroxiredoxin 4 protects against high-dose streptozotocin-induced diabetes by suppressing oxidative stress and cytokines in transgenic mice ...
Papers on PRDX4
The role of peroxiredoxin 4 in inflammatory response and aging.
Radyuk et al., Dallas, United States. In Biochim Biophys Acta, Feb 2016
In prior studies, we determined that the moderate overexpression of the Drosophila endoplasmic reticulum (ER)-localized peroxiredoxin (Prx), dPrx4, reduced oxidative damage and conferred beneficial effects on life span, while a high-level expression increased the incidence of tissue-specific apoptosis and dramatically shortened longevity.
Blueberry Component Pterostilbene Protects Corneal Epithelial Cells from Inflammation via Anti-oxidative Pathway.
Li et al., Wenzhou, China. In Sci Rep, Dec 2015
Importantly, PS was found to rebalance homeostasis between oxygenases and anti-oxidative enzymes by decreasing cyclooxygenase 2 (COX2) expression and restoring the activity of antioxidant enzymes, superoxide dismutase 1 (SOD1) and peroxiredoxin-4 (PRDX4) during hyperosmotic stress.
Redoxins in peripheral neurons after sciatic nerve injury.
Tegeder et al., Frankfurt am Main, Germany. In Free Radic Biol Med, Dec 2015
The expression and localization of Glrx, Txn and Txnrd proteins was not affected by sciatic nerve injury but peroxiredoxins were upregulated in the DRGs, Prdx1 and Prdx6 mainly in non-neuronal cells and Prdx4 and Prdx5 in DRG neurons, the latter associated with an increase of respective mRNAs and protein accumulation in peripheral and/or central fibers.
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.
Spirulina phycocyanin induces differential protein expression and apoptosis in SKOV-3 cells.
Bao et al., Wenzhou, China. In Int J Biol Macromol, Nov 2015
The decreased proteins such as HSP60, nucleolin, PPase, peroxiredoxin-4 and the increased protein (mtSSB) were identified in SKOV-3 cells after PC treatment, indicating that the effects of PC on tumor cell apoptosis may be relate to multiple target proteins.
ERO1-independent production of H2O2 within the endoplasmic reticulum fuels Prdx4-mediated oxidative protein folding.
Avezov et al., Hannover, Germany. In J Cell Biol, Nov 2015
The endoplasmic reticulum (ER)-localized peroxiredoxin 4 (PRDX4) supports disulfide bond formation in eukaryotic cells lacking endoplasmic reticulum oxidase 1 (ERO1).
Expression and distribution of peroxiredoxins in the retina and optic nerve.
Casson et al., Adelaide, Australia. In Brain Struct Funct, Nov 2015
With regard to protein expression, each isoform was detected in the retina and optic nerve by either Western blotting and/or immunohistochemistry. Excepting Prdx4, there was a good correspondence between the rodent and primate results.
Using Targeted Resequencing for Identification of Candidate Genes and SNPs for a QTL Affecting the pH Value of Chicken Meat.
De Koning et al., Uppsala, Sweden. In G3 (bethesda), Oct 2015
Four nonsynonymous SNPs differentiating the two QTL genotype groups were identified within four local genes (PRDX4, EIF2S3, PCYT1B, and E1BTD2).
Protective Effects of L-Carnitine Against Oxidative Injury by Hyperosmolarity in Human Corneal Epithelial Cells.
Li et al., Houston, United States. In Invest Ophthalmol Vis Sci, Aug 2015
Hyperosmotic stress also increased the mRNA expression and/or protein production of heme oxygenase-1 (HMOX1) and cyclooxygenase-2 (COX2), but inhibited the levels of antioxidant enzymes, superoxide dismutase-1 (SOD1), glutathione peroxidase-1 (GPX1), and peroxiredoxin-4 (PRDX4).
Physiological and pathological views of peroxiredoxin 4.
Homma et al., Yamagata, Japan. In Free Radic Biol Med, Jun 2015
Among six PRDX members in mammalian cells, PRDX4 uniquely possesses a hydrophobic signal peptide at the amino terminus, and, hence, it undergoes either secretion or retention by the endoplasmic reticulum (ER) lumen.
Transcriptome analysis of human OXR1 depleted cells reveals its role in regulating the p53 signaling pathway.
Bjørås et al., Oslo, Norway. In Sci Rep, 2014
HIF1A, SP6, E2F8 and TCF3), antioxidant genes (PRDX4, PTGS1 and CYGB) and numerous genes of the p53 signaling pathway involved in cell-cycle arrest (i.e.
Detoxification of oxidative stress in glioma stem cells: mechanism, clinical relevance, and therapeutic development.
Nakano et al., Columbus, United States. In J Neurosci Res, 2014
This review article summarizes recent studies on the role of ROS-reducing enzymes, including peroxiredoxin 4, in detoxifying oxidative stress preferentially for GSCs in HGGs.
The role of ascorbate in protein folding.
Lőrincz et al., Budapest, Hungary. In Protoplasma, 2014
However, very recently, low tissue ascorbate levels and a noncanonical scurvy were observed in endoplasmic reticulum thiol oxidase- and peroxiredoxin 4-compromised mice.
Regulating the level of intracellular hydrogen peroxide: the role of peroxiredoxin IV.
Bulleid et al., Glasgow, United Kingdom. In Biochem Soc Trans, 2014
We have been studying how the H2O2 produced during disulfide formation in the ER (endoplasmic reticulum) is metabolized and have shown that ER-resident peroxiredoxin IV not only can remove H2O2, but also contributes to de novo disulfide formation.
PRDX4, an endoplasmic reticulum-localized peroxiredoxin at the crossroads between enzymatic oxidative protein folding and nonenzymatic protein oxidation.
Zito, Cambridge, United Kingdom. In Antioxid Redox Signal, 2013
SIGNIFICANCE: Peroxiredoxin 4 (PRDX4) is an endoplasmic reticulum (ER)-resident peroxiredoxin that has the characteristic of coupling hydrogen peroxide (H(2)O(2)) catabolism with oxidative protein folding.
Proteomic analysis identifies dysfunction in cellular transport, energy, and protein metabolism in different brain regions of atypical frontotemporal lobar degeneration.
Bahn et al., Cambridge, United Kingdom. In J Proteome Res, 2012
A protein encoded by this locus was found to be differentially expressed in postmortem brains from patients with atypical frontotemporal lobar degeneration.
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.
Structural insights into the peroxidase activity and inactivation of human peroxiredoxin 4.
Wang et al., Beijing, China. In Biochem J, 2012
This study solved crystal structures of human Prx4 in three different redox forms and characterized the reaction features of Prx4 with hydrogen peroxide.
Crystal structure of reduced and of oxidized peroxiredoxin IV enzyme reveals a stable oxidized decamer and a non-disulfide-bonded intermediate in the catalytic cycle.
Bulleid et al., Glasgow, United Kingdom. In J Biol Chem, 2012
Crystal structure of reduced and of oxidized peroxiredoxin IV enzyme reveals a stable oxidized decamer and a non-disulfide-bonded intermediate in the catalytic cycle
Peroxiredoxin-controlled G-CSF signalling at the endoplasmic reticulum-early endosome interface.
Touw et al., Rotterdam, Netherlands. In J Cell Sci, 2011
Prdx4 inhibits G-CSF-induced signalling and proliferation in myeloid progenitors.
share on facebooktweetadd +1mail to friends