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Query: UNIPROT:P36969 (phospholipid hydroperoxide glutathione peroxidase)
 344 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The GPX2 gene encodes a homologue of phospholipid hydroperoxide glutathione peroxidase in Saccharomyces cerevisiae. The GPX2 promoter contains three elements the sequence of which is completely consistent with the optimal sequence for the Yap1 response element (YRE). Here, we identify the intrinsic YRE that functions in the oxidative stress response of GPX2. In addition, we discovered a cis-acting element (5'-GGCCGGC-3') within the GPX2 promoter proximal to the functional YRE that is necessary for H(2)O(2)-induced expression of GPX2. We present evidence showing that Skn7 is necessary for the oxidative stress response of GPX2 and is able to bind to this sequence. We determine the optimal sequence for Skn7 to regulate GPX2 under conditions of oxidative stress to be 5'-GGC(C/T)GGC-3', and we designate this sequence the oxidative stress-responsive Skn7 response element.
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PMID:Regulation of the yeast phospholipid hydroperoxide glutathione peroxidase GPX2 by oxidative stress is mediated by Yap1 and Skn7. 1513 69

The GPX2 gene encodes a homologue of mammalian phospholipid hydroperoxide glutathione peroxidase in Saccharomyces cerevisiae. Previously, we have reported that the oxidative stress-induced expression of GPX2 is strictly regulated by Yap1 and Skn7 transcription factors. Here, we found that the expression of GPX2 is induced by CaCl(2) in a calcineurin (CN)/Crz1-dependent manner, and the CN-dependent response element was specified in the GPX2 promoter. Neither Yap1 nor Skn7 was required for Ca(2+)-dependent induction of GPX2, therefore, distinct regulation for the oxidative stress response and Ca(2+) signal response for GPX2 exists in yeast cells.
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PMID:Distinct regulatory mechanism of yeast GPX2 encoding phospholipid hydroperoxide glutathione peroxidase by oxidative stress and a calcineurin/Crz1-mediated Ca2+ signaling pathway. 1522 52

The oviduct plays a crucial role in mammalian reproduction by providing an optimal environment for the final maturation and transport of gametes, fertilization, and early embryonic development. It is now recognized that these reproductive events in vitro can be either negatively or positively affected by reactive oxygen species such as hydrogen peroxide and lipid hydroperoxides. In the current study, we analyzed the expression of the phospholipid hydroperoxide glutathione peroxidase (PHGPx or GPx-4), a selenoenzyme that directly reduces membrane-bound lipid hydroperoxides in the bovine oviduct. Using in situ hybridization, we demonstrated that GPx-4 expression is almost restricted to the oviductal luminal epithelium in contrast to GPx-1, which is widely distributed, and GPx-2 and -3, which are mainly detected in the epithelial cells and lamina propria. Interestingly, real-time quantitative RT-PCR analysis showed that GPx-4 expression was highest during the follicular and postovulatory phases. In addition, GPx-4 expression was highest in the isthmus proximal to the dominant follicle during the follicular stage and remained high during the postovulatory period. This increased in expression of GPx-4 corresponded to increased GPx-4 enzymatic activity. Based on intrauterine infusion of estradiol, we determined that the increase in expression and activity of GPx-4 is estrogen mediated. This work clearly demonstrates that GPx-4 gene expression is influenced by the proximity of the dominant follicle in the oviduct in vivo. We propose that GPx-4 has an important role in the physiological control of peroxide tone in the bordering cells of the oviductal lumen.
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PMID:Estrogen selectively up-regulates the phospholipid hydroperoxide glutathione peroxidase in the oviducts. 1574 55

Glutathione peroxidases (GPxs) are a family of enzymes that scavenge peroxides generated in cells. We carried out molecular cloning for cDNAs of four GPx isozymes (GPx-1 through 4) in primate species. The essential residues for the function of these isozymes were well conserved. A phylogenetic tree of GPx isozymes of primates and other mammals showed that GPx-4 diverged first, followed by GPx-3, GPx-2, and GPx-1. Expression of mRNAs for GPx-2 through 4 in various tissues of Japanese monkey was analyzed by Northern blot hybridization. GPx-2 mRNA was detected at 1.7 kb, exclusively in the stomach and small intestine. GPx-3 mRNA was detected at 1.8 kb, intensively in the kidney and adrenal gland, and weakly in the cerebellum, heart, and lung. GPx-4 mRNA was detected at 1.1 kb, very intensively in the testis and weakly in lung, heart, and cerebellum. These results showed that GPx isozymes were expressed under tissue-specific regulations.
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PMID:Structure, gene expression, and evolution of primate glutathione peroxidases. 1596 96

We have previously reported that Saccharomyces cerevisiae has three glutathione peroxidase homologues (GPX1, GPX2, and GPX3) (Inoue, Y., Matsuda, T., Sugiyama, K., Izawa, S., and Kimura, A. (1999) J. Biol. Chem. 274, 27002-27009). Of these, the GPX2 gene product (Gpx2) shows the greatest similarity to phospholipid hydroperoxide glutathione peroxidase. Here we show that GPX2 encodes an atypical 2-Cys peroxiredoxin which uses thioredoxin as an electron donor. Gpx2 was essentially in a reduced form even in mutants defective in glutathione reductase or glutaredoxin under oxidative stressed conditions. On the other hand, Gpx2 was partially oxidized in a mutant defective in cytosolic thioredoxin (trx1Deltatrx2Delta) under non-stressed conditions and completely oxidized in tert-butyl hydroperoxide-treated cells of trx1Deltatrx2Delta and thioredoxin reductase-deficient mutant cells. Alanine scanning of cysteine residues of Gpx2 revealed that an intramolecular disulfide bond was formed between Cys37 and Cys83 in vivo. Gpx2 was purified to determine whether it functions as a peroxidase that uses thioredoxin as an electron donor in vitro. Gpx2 reduced H2O2 and tert-butyl hydroperoxide in the presence of thioredoxin, thioredoxin reductase, and NADPH (for H2O2, Km= 20 microm, kcat = 9.57 x 10(2) s(-1); for tert-butyl hydroperoxide, Km= 62.5 microm, kcat = 3.68 x 10(2) s(-1)); however, it showed remarkably less activity toward these peroxides in the presence of glutathione, glutathione reductase, and NADPH. The sensitivity of yeast cells to tert-butyl hydroperoxide was found to be exacerbated by the co-existence of Ca2+, a tendency that was most obvious in gpx2Delta cells. Although the redox state of Gpx2 was not affected by Ca2+, the Gpx2 level was markedly increased in the presence of both tert-butyl hydroperoxide and Ca2+. Gpx2 is likely to play an important role in the protection of cells from oxidative stress in the presence of Ca2+.
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PMID:GPX2, encoding a phospholipid hydroperoxide glutathione peroxidase homologue, codes for an atypical 2-Cys peroxiredoxin in Saccharomyces cerevisiae. 1625 Nov 89

Analysis of the selenoproteome identified five glutathione peroxidases (GPxs) in mammals: cytosolic GPx (cGPx, GPx1), phospholipid hydroperoxide GPx (PHGPX, GPx4), plasma GPx (pGPX, GPx3), gastrointestinal GPx (GI-GPx, GPx2) and, in humans, GPx6, which is restricted to the olfactory system. GPxs reduce hydroperoxides to the corresponding alcohols by means of glutathione (GSH). They have long been considered to only act as antioxidant enzymes. Increasing evidence, however, suggests that nature has not created redundant GPxs just to detoxify hydroperoxides. cGPx clearly acts as an antioxidant, as convincingly demonstrated in GPx1-knockout mice. PHGPx specifically interferes with NF-kappaB activation by interleukin-1, reduces leukotriene and prostanoid biosynthesis, prevents COX-2 expression, and is indispensable for sperm maturation and embryogenesis. GI-GPx, which is not exclusively expressed in the gastrointestinal system, is upregulated in colon and skin cancers and in certain cultured cancer cells. GI-GPx is a target for Nrf2, and thus is part of the adaptive response by itself, while PHGPx might prevent cancer by interfering with inflammatory pathways. In conclusion, cGPx, PHGPx and GI-GPx have distinct roles, particularly in cellular defence mechanisms. Redox sensing and redox regulation of metabolic events have become attractive paradigms to unravel the specific and in part still enigmatic roles of GPxs.
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PMID:Glutathione peroxidases and redox-regulated transcription factors. 1708 Nov 3

Exogenous salicylic acid (SA) significantly improved abiotic tolerance in higher plants, and ascorbate (ASA) and glutathione (GSH) play important roles in abiotic tolerance. In this study, SA (0.5mM) markedly increased the contents of ASA and GSH in SA-treated plants during salt stress (250mM NaCl). The transcript levels of the genes encoding ASA and GSH cycle enzymes were measured using quantitative real-time PCR. The results indicated that, during salt stress, exogenous SA significantly enhanced the transcripts of glutathione peroxidase (GPX1), phospholipid hydroperoxide glutathione peroxidase (GPX2) and dehydroascorbate reductase (DHAR) genes at 12h, glutathione reductase (GR) at 24h, 48h and 72h, glutathione-S-transferase 1 (GST1), 2 (GST2), monodehydroascorbate reductase (MDHAR) and glutathione synthetase (GS) at the 48h and 72h after salt stress, respectively. The results implied that SA temporally regulated the transcript levels of the genes encoding ASA-GSH cycle enzymes, resulting in the increased contents of GSH and ASA and enhanced salt tolerance.
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PMID:Salicylic acid increases the contents of glutathione and ascorbate and temporally regulates the related gene expression in salt-stressed wheat seedlings. 2394 81

Previous studies revealed that Se was an important regulatory factor for glutathione peroxidase (GPx) genes. However, the relationship between Se concentrations and mRNA expression levels of GPxs were unclear in goats, especially the goats living in natural Se-enriched area. Thus, the aim of this study was to determine the Se concentrations and the mRNA expression levels of GPx-1, GPx-2, GPx-3, and GPx-4 in goats from Ziyang County (ZY-H and ZY-L goats) and Baoji City (BJ-P goats), which were Se-rich region and Se-poor region in China, respectively. Atomic fluorescence spectrometry was used as an essential method to determine the Se concentrations in heart, liver, spleen, lung, kidney, longissimus, biceps femoris, and serum, and the gene expressions were quantified in mRNA samples extracted from the above tissues by real-time quantitative reverse transcription-polymerase chain reaction. We found that the Se concentrations in ZY-H and ZY-L goats were higher than that in BJ-P goats significantly (P < 0.05), and the pertinence relations of Se levels between serum and heart, liver, spleen, and kidney were significant (P < 0.05). The mRNA levels of GPx-1 in ZY-H and ZY-L goats were higher than that in BJ-P goats very significantly (P < 0.01) except for longissimus (P < 0.05). Our results indicated a significant trend for GPx-2 in the direction of increasing mRNA levels with increasing Se concentrations in goats but had no statistical significance (P > 0.05) in our experimental conditions. As to GPx-3, its mRNA expression in spleen, lung, and kidney (P < 0.05) were upregulated and were consensual to high Se contents in ZY-H goats, but no significant effects were observed in heart, liver, longissimus, and biceps femoris among our three groups (P > 0.05). The mRNA levels of GPx-4 in heart, liver, lung, and kidney of ZY-H and ZY-L goats were higher than that of BJ-P goats (P < 0.05), and the difference was very significant in lung especially (P < 0.01), but no change in spleen, longissimus, and biceps femoris (P > 0.05). In summary, these data suggested that the goats living in Ziyang County were rich in Se, and the deposition Se played important roles in the mRNA expression of GPx-1, GPx-3, and GPx-4 in certain tissues of goats differentially.
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PMID:The effect of deposition Se on the mRNA expression levels of GPxs in goats from a Se-enriched county of China. 2407 70


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