Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P30044 (antioxidant enzyme)
 8,037 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A cDNA corresponding to 1-Cys peroxiredoxin, an evolutionarily conserved thiol-specific antioxidant enzyme, was isolated from buckwheat (Fagopyrum esculentum Moench), a dicotyledonous plant species belonging to the Polygonaceae family. The cDNA, which we have designated as FePer1, contains a major open reading frame capable of encoding a polypeptide of 219 residues with a predicted molecular mass of 24.3kDa. The deduced primary structure of FePer1 polypeptide shows a high level (about 70%) of sequence homology to other recently identified plant 1-Cys peroxiredoxins. FePer1 also exhibits a significant level of sequence similarity to non-plant 1-Cys peroxiredoxins, sharing 52 and 42% identities with mammalian and fungal 1-Cys peroxiredoxins, respectively. As for all 1-Cys peroxiredoxins identified from various organisms, the amino acid sequence proposed to constitute the active site of the enzyme is highly conserved in FePer1 polypeptide. The gene corresponding to FePer1 cDNA is a single-copy gene in the buckwheat genome. Its expression is regulated in a seed-specific and temporal manner during seed development. FePer1 gene is induced transiently for a short period immediately after seed imbibition.
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PMID:FePer 1, a gene encoding an evolutionarily conserved 1-Cys peroxiredoxin in buckwheat (Fagopyrum esculentum Moench), is expressed in a seed-specific manner and induced during seed germination. 1076 29

Exposure of living organisms to reactive oxygen species (ROS), notably oxygen free radicals and hydrogen peroxide is closely linked to the very fact of aerobic life. Oxidants, however, are not always detrimental for cell survival, indeed moderate concentrations of ROS serve as signaling molecules. To maintain this level, cells have evolved an antioxidant defense system. Disruption of this balance leads either to oxidative or reductive stress. Down syndrome (DS) is a genetic disorder associated with oxidative stress. Overexpression of superoxide dismutase-1 (SOD-1) as a result of gene loading is suggested to be responsible for this phenomenon. To examine this view, we investigated the expression of thirteen different proteins involved in the cellular antioxidant defense system in brains of control and DS fetuses by two-dimensional electrophoresis (2-DE) coupled with matrix-assisted laser desorption/ionization mass spectroscopy (MALDI-MS). No detectable change was found in expression of SOD-1, catalase, phospholipid hydroperoxide glutathione peroxidase, glutathione reductase, antioxidant enzyme AOE372, thioredoxin-like protein and selenium binding protein between control and DS fetuses. By contrast, a significant reduction was observed in levels of glutathione synthetase (P < 0.01), glutathione-S-transferase mu2 (P < 0.01), glutathione-S-transferase p (P < 0.05), antioxidant protein 2 (P < 0.05), thioredoxin peroxidase-I (P < 0.05) and thioredoxin peroxidase-II (P < 0.01) in DS compared with controls. The data suggest that oxidative stress in fetal DS does not result from overexpression of SOD-1 protein, rather oxidative stress appears to be the consequence of low levels of reducing agents and enzymes involved in removal of hydrogen peroxide.
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PMID:Antioxidant proteins in fetal brain: superoxide dismutase-1 (SOD-1) protein is not overexpressed in fetal Down syndrome. 1177 62

1-Cys peroxiredoxin (1-cysPrx) is a novel antioxidant enzyme able to reduce phospholipid hydroperoxides in vitro by using glutathione as a reductant. This enzyme is widely expressed and is enriched in lungs. A fusion protein of green fluorescent protein with 1-cysPrx was stably expressed in a lung-derived cell line (NCI-H441) lacking endogenous enzyme. Overexpressing cells (C17 or C48) degraded H(2)O(2) and t-butylhydroperoxide more rapidly and showed decreased sensitivity to oxidant stress as measured by (51)Cr release. On exposure to (*)OH generated by Cu(2+)-ascorbate (Asc), overexpressing cells compared with H441 showed less increase in thiobarbituric acid-reactive substance and phosphatidylcholine hydroperoxide content. This effect was reversed by depletion of cellular glutathione. Diphenyl-1-pyrenoylphosphonium fluorescence, used as a real-time probe of membrane phospholipid peroxidation, increased immediately on exposure to Cu(2+)-Asc and was abolished by preincubation of cells with Trolox (a soluble vitamin E) or Tempol (a radical scavenger). The rate of diphenyl-1-pyrenoylphosphonium fluorescence increase with Cu(2+)-Asc exposure was markedly attenuated in C17 and C48 cells as compared with H441. Annexin V-Cy3 was used to detect phosphatidylserine translocation from the inner to outer leaflet of the plasma membrane. Cu(2+)-Asc treatment induced phosphatidylserine translocation within 2 h in H441 cells but none was observed in C48 cells up to 24 h. These results indicate that 1-cysPrx can scavenge peroxides but in addition can reduce peroxidized membrane phospholipids. Thus, the enzyme can protect cells against oxidant-induced plasma membrane damage, thereby playing an important role in cellular defense against oxidant stress.
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PMID:1-Cys peroxiredoxin overexpression protects cells against phospholipid peroxidation-mediated membrane damage. 1219 53

A cDNA corresponding to 1-Cys peroxiredoxin, an evolutionarily conserved thiol-specific antioxidant enzyme, was isolated from Xerophyta viscosa Baker, a resurrection plant indigenous to Southern Africa and belonging to the family Velloziaceae. The cDNA, designated XvPer1, contains an open reading frame that encodes a polypeptide of 219 residues with a predicted molecular weight of 24.2 kDa. The XvPer1 polypeptide shows significant sequence identity (approx. 70%) to other recently identified plant 1-Cys peroxiredoxins and relatively high levels of sequence similarity (approx. 40%) to non-plant 1-Cys peroxiredoxins. The XvPer1 cDNA contains a putative polyadenylation site. As for all 1-Cys peroxiredoxins identified to date, the amino acid sequence proposed to constitute the active site of the enzyme, PVCTTE, is highly conserved in XvPer1. It also contains a putative bipartite nuclear localization signal. Southern blot analysis revealed that there is a single copy of XvPer1 in the X. viscosa genome. All angiosperm 1-Cys peroxiredoxins described to date are seed-specific and absent in vegetative tissues even under stress conditions; therefore, XvPer1 is unique in that it is expressed in the vegetative tissues of X. viscosa. The XvPer1 transcript was absent in fully hydrated X. viscosa tissue but levels increased in tissues subjected to abiotic stresses such as dehydration, heat (42 degrees C), high light intensity (1,500 micro mol photons m(-2) s(-1)) and when treated with abscisic acid (100 micro M ABA) and sodium chloride (100 mM NaCl). Western blot analyses correlated with the patterns of expression of XvPer1 transcripts under different stress conditions. Immunofluorescence analyses revealed that XvPer1 is localized in the nucleus of dehydrated X. viscosa leaf cells. These results suggest that XvPer1 is a stress-inducible gene, which may function to protect nucleic acids within the nucleus against oxidative injury.
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PMID:A novel stress-inducible antioxidant enzyme identified from the resurrection plant Xerophyta viscosa Baker. 1224 36

1-Cys peroxiredoxin (1-cysPrx), a member of the peroxiredoxin family that contains a single conserved cysteine residue, reduces a broad spectrum of hydroperoxides. We studied changes in 1-cysPrx expression in rat lungs and lung cell lines in response to oxidative stress due to hyperoxia, H2O2, or paraquat. After 60 h of hyperoxia (>95% O2), mRNA and protein levels of 1-cysPrx and peroxidase activity were significantly elevated in rat lungs by approximately 1.5- to 2-fold compared with the control (P < 0.05). A similar induction of 1-cysPrx was observed in mouse lungs following exposure to O2 for 63 or 72 h; enzyme induction in mouse lungs was similar for wild-type and glutathione peroxidase 1 gene-targeted mice. H2O2 and paraquat treatment induced 1-cysPrx gene expression in L2 cells. Enzyme induction was attenuated by pretreatment with Trolox or N-acetylcysteine. Actinomycin D treatment showed that stability of 1-cysPrx mRNA was not altered in the presence of H2O2 or paraquat, indicating that increased expression with oxidative stress is regulated at the transcriptional level. These data indicate that the antioxidant enzyme 1-cysPrx is induced in lung cells by oxidative stress.
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PMID:Induction of 1-cys peroxiredoxin expression by oxidative stress in lung epithelial cells. 1285 Dec 11

1-Cys peroxiredoxin (1-cysPrx), a member of the peroxiredoxin family with a single conserved cysteine, is a unique antioxidant enzyme. We have generated mice in which the 1-cysPrx gene has been inactivated; they are viable and fertile. Mice have a highly related intronless gene (1-cysPrx-P1, GenBank accession number AF085220) with the same length of open reading frame (224 aa) as 1-cysPrx but located on a different chromosome. Since the product of this gene possibly could mimic 1-cysPrx function, we compared expression of 1-cysPrx and 1-cysPrx-P1 in mouse tissues by real-time polymerase chain reaction and Western blot. 1-cysPrx mRNA and protein were expressed in all mouse tissues that were examined with the highest expression level in lung. 1-cysPrx-P1 mRNA was expressed only in testis. In the 1-cysPrx 'knock-out' mouse, 1-cysPrx-P1 mRNA expression level was similar to the wild type but protein expression was not detected. Thus, mouse 1-cysPrx-P1 is an mRNA-expressed pseudogene that does not result in detectable protein in vivo.
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PMID:1-Cys peroxiredoxin knock-out mice express mRNA but not protein for a highly related intronless gene. 1464 14

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% O(2) or to 85% O(2) for 4 days followed by 100% O(2). At 72 h of 100% O(2) 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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PMID:Adenovirus-mediated transfer of the 1-cys peroxiredoxin gene to mouse lung protects against hyperoxic injury. 1513 96

The muscle sarcoplasmic proteins from bovine M. longissimus thoracis muscle were studied using proteomics to identify possible protein markers for meat tenderness. This study included 3 experiments: A1, A2, and B. From a collection of biopsies from the bovine M. longissimus thoracis muscle, excised 4 d before slaughter from 178 Norwegian Red young bulls, 26 biopsies were studied in Exp. A1. Based on Warner-Bratzler shear force (WBSF) values at 7 d postmortem, the biopsies were separated into a tender and a tough group of 13 bulls each and analyzed by 2-dimensional gel electrophoresis (2-DE) and Western blotting. The 2-DE experiments identified 4 different proteins: stress-70 protein, protein DJ-1, peroxiredoxin-6, and malate dehydrogenase, which were different in abundance in the tender and tough groups. However, only peroxiredoxin-6 was confirmed by quantification from Western blots. Peroxiredoxin-6 is an antioxidant enzyme that plays a role in protecting cells from oxidative stress. Peroxiredoxin-6 was identified through 3 spots of the same molecular weight, but with different pI on the Western blots. Only one of the spots was more abundant in the biopsies from the tender group. In Exp. A2, samples collected 1 h postmortem from the same animals and muscles as in Exp. A1 were analyzed by Western blotting. In these postmortem samples, the same spot from peroxiredoxin-6 as in Exp. A1 was more abundant in the tender group. In addition, one of the other peroxiredoxin-6 spots was also more abundant in the tender group. To verify the results from Exp. A, biopsies from 14 additional animals were analyzed in Exp. B by Western blotting against stress-70 protein, protein DJ-1, peroxiredoxin-6, and malate dehydrogenase. No significant differences between the tough and tender groups could be observed in these biopsies. However, for peroxiredoxin-6, the tendencies pointed in the same direction as in Exp. A. In conclusion, peroxiredoxin-6 might be a potential protein marker for meat tenderness detectable in biopsies and in samples collected shortly after slaughter. However, more animals are needed to verify the findings in the present study.
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PMID:Peroxiredoxin-6--a potential protein marker for meat tenderness in bovine longissimus thoracis muscle. 1935 13