1-Cys peroxiredoxin overexpression protects cells against phospholipid peroxidation-mediated membrane damage

Manevich, Yefim; Sweitzer, Tom; Pak, Jhang Ho; Feinstein, Sheldon I.; Muzykantov, Vladimir R.; Fisher, Aron B.

doi:10.1073/pnas.182384499

Cited by 197 publications

(181 citation statements)

References 27 publications

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“…Previous studies have demonstrated that overexpression of 1-cysPrx in NIH 3T3 cells enhances their ability to reduce H 2 O 2 and protects their glutamine synthetase against H 2 O 2 -mediated inactivation (12). Our laboratory has shown that 1-cysPrx can reduce peroxidized membrane phospholipids in H441 cells, a lung epithelial cell line (17), whereas an antisense-mediated decrease in expression of 1-cysPrx in L2 cells, another lung epithelial cell line, resulted in apoptotic cell death (20). Recently, gene-targeted mice with absent 1-cysPrx have been shown to be more sensitive to paraquat-induced oxidative injury (23).…”

mentioning

confidence: 80%

“…Protein samples (10 g) were subjected to a 12% SDS-PAGE gel on a XCell electrophoresis apparatus (Invitrogen, Carlsbad, CA) and then were transferred to a polyvinylidene fluoride membrane (Millipore, Bedford, MA). Membranes were incubated in blocking solution (0.1% Tween 20-TBS buffer containing 10% nonfat dry milk; Bio-Rad, Richmond, CA) for 1 h and then were probed with a polyclonal antibody (1:2,000 dilution) to a 1-cysPrx peptide (1: 2,000 dilution) followed by peroxidase-conjugated secondary antibody as described previously (17,20). The reaction was detected by enhanced chemiluminescence (ECL; NEN Life Science, Bos- ton, MA) and quantitated by densitometric scanning of X-ray film using the FluorS multi-imager (Bio-Rad).…”

Section: Methodsmentioning

confidence: 99%

“…DISCUSSION 1-cysPrx is a recently described antioxidant enzyme member of the Prx family that is expressed at relatively high levels in the lung (14). In lung epithelial cell lines, overexpression of 1-cysPrx protein was shown to increase the ability of these cells to degrade H 2 O 2 and to protect them against oxidantinduced plasma membrane damage (17), whereas treatment with an antisense oligonucleotide to 1-cysPrx resulted in lipid peroxidation and apoptosis (20). 1-cysPrx knockout mice showed increased sensitivity to paraquat-induced oxidative lung injury compared with wild-type mice (23).…”

Section: Lung Distribution Of Gene Transfermentioning

confidence: 96%

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Adenovirus-mediated transfer of the 1-cys peroxiredoxin gene to mouse lung protects against hyperoxic injury

Wang

Manevich

Feinstein

et al. 2004

American Journal of Physiology-Lung Cellular and Molecular Phys

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1-Cys peroxiredoxin (1-cysPrx) is a novel antioxidant enzyme that has been shown to reduce a broad spectrum of peroxides including phospholipid hydroperoxides. We tested the hypothesis that adenovirus-mediated transfer of the 1-cysPrx gene can protect lungs of mice from oxidant injury. Mice infected with AdLacZ/AdNull were used as a control (AdCon). X-galactosidase staining revealed widespread expression of the LacZ gene in airways and lung alveoli. Compared with AdCon, 1-cysPrx expression was increased about twofold at 3 days after adenovirus infection. Mice with increased Prx expression showed less loss of body weight and longer survival during exposure to 100% O2 or to 85% O2 for 4 days followed by 100% O2. At 72 h of 100% O2 exposure, AdPrx infection protected mouse lungs from injury as indicated by less pleural effusion, lower lung wet/dry weight, less protein and fewer nucleated cells in bronchoalveolar lavage fluid, and lower content of thiobarbituric acid-reactive substances and protein carbonyls in lung homogenate. These findings show that increased expression of 1-cysPrx through adenovirus-mediated gene transfer protects mouse lungs from hyperoxic injury and delays death.

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mentioning

confidence: 80%

Section: Methodsmentioning

confidence: 99%

Section: Lung Distribution Of Gene Transfermentioning

confidence: 96%

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Adenovirus-mediated transfer of the 1-cys peroxiredoxin gene to mouse lung protects against hyperoxic injury

Wang

Manevich

Feinstein

et al. 2004

American Journal of Physiology-Lung Cellular and Molecular Phys

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“…Five of them have two conserved and catalytically active Cys residues (PRDX1 to 5), though only that of the N-terminal region is directly involved in peroxidatic activity. PRDX6 only has the catalytic Cys residue of the N-terminal region and thus belongs to 1-Cys PRDX subclass with both glutathione peroxidase and phospholipase A activities leading to reduced membrane phospholipid peroxidation [4,5].…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization and expression analysis of six peroxiredoxin paralogous genes in gilthead sea bream (Sparus aurata): Insights from fish exposed to dietary, pathogen and confinement stressors

Pérez‐Sánchez

Bermejo-Nogales

Calduch-Giner

et al. 2011

Fish & Shellfish Immunology

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ABSTRACT. The aim of this work was to underline the physiological role of the antioxidant peroxiredoxin (PRDX) family in gilthead sea bream (Sparus aurata L.), a perciform fish extensively cultured in the Mediterranean area. First, extensive BLAST searches were done on the gilthead sea bream cDNA database of the AQUAMAX European Project (www.sigenae.org/iats), and six contigs were unequivocally identified as PRDX1-6 after sequence completion by RT-PCR. The phylogenetic analysis evidenced three major clades corresponding to PRDX1-4 (true 2-Cyst PRDX subclass), PRDX5 (atypical 2-Cys PRDX subclass) and PRDX6 (1-Cys PRDX subclass) that reflected the present hierarchy of vertebrates. However, the PRDX2 branch of modern fish including gilthead sea bream was related to the monophyletic PRDX1 node rather than to PRDX2 cluster of mammals and primitive fish, which probably denotes the acquisition of novel functions through vertebrate evolution. Transcriptional studies by means of quantitative real-time PCR evidenced a ubiquitous PRDX gene expression that was tissue-specific for each PRDX isoform. In a second set of transcriptional studies, liver and head kidney were chosen as target tissues in fish challenged with i) the intestinal parasite Enteromyxum leei, ii) a plant oil (VO) diet with deficiencies in essential fatty acids and iii) prolonged exposure to high rearing densities. These studies showed that PRDX genes were highly and mostly constitutively expressed in the liver and were not affected by dietary intervention or high density. In contrast, head kidney was highly sensitive to the different experimental challenges: significantly lower values were found for PRDX5 in the three trials, for PRDX6 in parasitized and high density fish and for PRDX1 in parasitized and VO fish. PRDX2, 3 and 5 were decreased only in VO, high density and parasitized animals, respectively. These findings would highlight the role of PRDXs as integrative and highly predictive biomarkers of health and welfare in fish and gilthead sea bream in particular.

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“…1-cys Prx is one of six Prx isoforms, and is expressed in various tissues -in particular liver tisses -related to the protection of cellular oxidative stresses (10).…”

Section: Introductionmentioning

confidence: 99%

Transcriptional regulation of 1-cys peroxiredoxin by the proto-oncogene protein DEK

Kim

Choi

et al. 2010

Mol Med Rep

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Abstract. The nuclear phosphoprotein deK is abundantly present in cells and is implicated in diseases including leukemia and autoimmune disorders. deK has three highly acidic amino acid domains and inhibits histone acetyltransferase activity by binding directly to histones. in a previous study, differentially regulated proteins under deK knockdown conditions, including the up-regulated protein 1-cys peroxiredoxin (1-cys Prx), were identified by proteome analysis. Here, an in vivo reporter assay with short hairpin rna-mediated deK knockdown revealed that deK negatively regulated 1-cys Prx transcription, and that the nF-κB subunit p65 had a synergistic effect on this deK-mediated repression. Both proteins are recruited to the 1-cys Prx promoter region and regulate its transcription. our study demonstrates that deK modulates the transcriptional regulation of the target gene through protein interaction with other regulatory proteins. IntroductionThe DEK protein was first identified in a specific chromosomal translocation t(6;9)(p23;q34) in an acute myelogenous leukemia, which results in the formation of a fusion gene with the can nucleoporin protein nuP214 (1). This translocated fusion gene makes a fusion protein, in which part of the n-terminal (1-349 amino acids) of deK is fused with part of the c-terminal (813-2,090 amino acids) of can. The deK protein, as a phosphoprotein, is an abundantly and ubiquitously expressed nuclear protein with two functional domains (SaP and dna binding/multimerization), several phosphorylation sites and three highly acidic domains (2,3). deK binds dna and induces deK-deK multimerization in a phosphorylation-dependent manner (4). a recent report showed that a highly acidic domain in deK inhibits histone acetyltransferase (HAT) activity through histone binding (2). It has been revealed that DEK influences chromatin remodeling through the alteration of chromatin topology (5,6). deK also regulates transcriptional activity by recruiting transcriptional co-repressors, such as hdaxx and histone deacetylase-2, to chromatin (7).deK is also involved in carcinogenesis and autoimmune diseases, such as systemic lupus erythematosus, juvenile rheumatoid arthritis and ataxia telangiectasia (8). a recent proteomic analysis revealed that deK knockdown up-regulated 1-cys peroxiredoxin (1-cys Prx) (Prx 6) and caused the hyperacetylation of histones around the 1-cys Prx promoter (9).1-cys Prx is one of six Prx isoforms, and is expressed in various tissues -in particular liver tisses -related to the protection of cellular oxidative stresses (10).nF-κB is a transcription factor with multiple biological functions, including immune and inflammatory response, cell growth and differentiation, and the suppression of apoptosis (11). The nF-κB family consists of five members, p65/RelA, p50 (p105), p52 (p100), relB and c-rel (12). a previous study showed that the p65 subunit of nF-κB interacts with deK (13).In this study, we identified the negative regulatory role of deK in 1-cys Prx transcription: its knockdown re...

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1-Cys peroxiredoxin overexpression protects cells against phospholipid peroxidation-mediated membrane damage

Cited by 197 publications

References 27 publications

Adenovirus-mediated transfer of the 1-cys peroxiredoxin gene to mouse lung protects against hyperoxic injury

Adenovirus-mediated transfer of the 1-cys peroxiredoxin gene to mouse lung protects against hyperoxic injury

Molecular characterization and expression analysis of six peroxiredoxin paralogous genes in gilthead sea bream (Sparus aurata): Insights from fish exposed to dietary, pathogen and confinement stressors

Transcriptional regulation of 1-cys peroxiredoxin by the proto-oncogene protein DEK

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