Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.11.1.9 (glutathione peroxidase)
 22,002 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The complete sequence of the mouse epididymal protein (MEP24) was cloned. It contains a 663 bp open-reading frame that, after conceptual translation, shows extensive identity with proteins belonging to the glutathione peroxidase (GPX) family. However, a major difference between GPX5 (MEP24) and other known GPXs concerns a protein domain known to be critical for GPX function. To find out what could be the physiological function of such a protein in the mouse epididymis, we have used a mammalian expression system to overexpress the GPX5 protein. Cells constitutively expressing the GPX5 protein were generated and assayed for their ability to metabolize regular substrates of GPX enzymes. Data presented here show that the GPX5-expressing cells can metabolize hydrogen peroxide in a manner that is consistent with a peroxidase activity. However, the substrate preference of the GPX5-expressing cells and their apparent insensitivity to a regular inhibitor of GPX enzymes suggest that the GPX5 protein belongs to a particular class of GPX proteins. Involvement of this protein in the physiology of the mouse epididymis is discussed.
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PMID:In vitro expression of a mouse tissue specific glutathione-peroxidase-like protein lacking the selenocysteine can protect stably transfected mammalian cells against oxidative damage. 903 86

Using immunohistochemistry and Western blotting analyses, we present a detailed study of the distribution of the glutathione peroxidase protein (GPX5) within the mouse epididymis. We have shown that the expression of the epididymis-specific protein is restricted to the caput and essentially localized to the apical cell border of the caput epithelium. Secretion of the protein was detected as early as the proximal segment of the caput and GPX5 was subsequently found in the lumen of corpus and cauda epididymis duct. Within the caput, Western blot analyses have shown that equivalent quantities of GPX5 protein were found in segments I, II, and III. During ontogenesis, GPX5 appeared at 20 days postnatal, before the completion of the morphological differentiation of the caput and concomitantly with the appearance of spermatozoa within the epididymis, in agreement with what was reported earlier regarding the transcription of its corresponding gene during epididymal ontogenesis (Faure et al., 1991). Hormonal privation by castration abolished the accumulation of the GPX5 protein confirming previous data obtained on GPX5 mRNA levels. Treatments such as testosterone replacement or hemicastration led to the restriction of the protein to the caput epithelium, suggesting that protein secretion partly depends both on the presence of testicular factors and on spermatozoa. Using electron microscopy, we have shown that the secreted protein binds to spermatozoa and is found predominantly on the sperm acrosomic region. Finally, we report here that the GPX5 protein can be detected in fluids recovered from the uterine horns of freshly mated female mice. These results suggest that GPX5 might play an important role in sperm maturation from the early events up to the onset of fertilization and therefore could potentially be used as a tool to monitor sperm quality.
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PMID:Tissue and developmental distribution, dependence upon testicular factors and attachment to spermatozoa of GPX5, a murine epididymis-specific glutathione peroxidase. 911 Mar 19

An epididymis-specific, secretory glutathione peroxidase (GPX5) has been proposed previously to play a role in protecting mammalian sperm membranes from the deleterious effects of lipid peroxidation, which, if not contained, can lead to reduced fertilizing capacity. Here we report the cDNA cloning of human GPX5 and show that the majority of transcripts contain a 118 nt frame-shifting deletion, arising, most likely, from inappropriate excision of exon 3 during processing. Antisera raised against recombinant human GPX5 cross-reacted with rat and macaque (Macaca fascicularis) epididymal proteins of the size expected for full-length, active GPX5. However, no similar reactivity could be demonstrated in any of the human samples tested.
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PMID:The majority of human glutathione peroxidase type 5 (GPX5) transcripts are incorrectly spliced: implications for the role of GPX5 in the male reproductive tract. 963 55

A differential library screening procedure was used to clone a novel abundant and tissue-specific cDNA from the dog epididymis. It was tentatively named CE7 for dog epididymal gene product 7. By sequence similarity to homologous counterparts expressed in mice, rats, pigs, and macaque monkeys, it appears that the 1.5 kb dog epididymal mRNA encodes the secretory glutathione peroxidase-like protein, GPX5. This protein is very similar to the family of glutathione peroxidase enzymes, but does not contain selenocysteine. Northern blot and in situ hybridization analyses revealed that the mRNA encoding CE7/GPX5, like its species homologues, was restricted to the epididymis and transcribed by the epithelial cells in the proximal parts of the organ. While the CE7 cDNA probe cross-hybridized to epididymal mRNAs in most species included in this study, it failed to identify a human GPX5 counterpart. Northern blot analyses of epididymal RNA extracts from hemi-cryptorchid dogs suggested that testicular secretions, including androgen hormones, temperature effects, or both, were involved in the region-dependent modulation of mRNA encoding CE7 in the dog epididymis. The effect was most obvious in the caput region of the abdominal organ where the mRNA encoding CE7 was almost completely downregulated.
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PMID:Dog epididymis-specific mRNA encoding secretory glutathione peroxidase-like protein. 964 Feb 75

The mammalian epididymis is the site of expression and secretion of an abundant, tissue-specific, androgen-regulated, selenium-independent, glutathione peroxidase isoenzyme (GPX5), which has been proposed to play a role in protecting the membranes of spermatozoa from the damaging effects of lipid peroxidation and/or preventing premature acrosome reaction. Using a combination of reverse transcription-polymerase chain reaction, Northern blot analysis and Western blotting, we now describe in detail the developmental expression of GPX5 transcripts and protein in the rat epididymis and characterize the association of rat GPX5 with the sperm plasma membrane.
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PMID:Expression of extracellular glutathione peroxidase type 5 (GPX5) in the rat male reproductive tract. 978 43

We have previously characterized and cloned a secreted sperm-bound selenium-independent glutathione peroxidase protein (GPX5), the expression of which was found to be restricted to the mouse caput epididymidis. Because of the lack of selenium (Se) in the active site of this enzyme, unlike the other animal GPXs characterized to date, it was suspected that GPX5 does not function in the epididymis as a true glutathione peroxidase in vivo. In the present report, following dietary selenium deprivation which is known to reduce antioxidant defenses and favor oxidative stress in relation with depressed Se-dependent GPX activities, we show that the epididymis is still efficiently protected against increasing peroxidative conditions. In this model, the caput epididymides of selenium-deficient animals showed a limited production of lipid peroxides, a total GPX activity which was not dramatically affected by the shortage in selenium availability and an increase in GPX5 mRNA and protein levels. Altogether, these data strongly suggest that the selenium-independent GPX5 could function as a back-up system for Se-dependent GPXs.
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PMID:Selenium-independent epididymis-restricted glutathione peroxidase 5 protein (GPX5) can back up failing Se-dependent GPXs in mice subjected to selenium deficiency. 1054 76

One of the most exciting recent advances in cell biology is the possibility to use the green fluorescent protein and its various mutated forms as reporter proteins in studies carried out in vitro and in vivo. In the present study, several detection techniques for the enhanced green fluorescent protein (EGFP) were compared in transgenic mice, using fluorescence and confocal microscopy. In addition, different tissue preparation techniques (squash preparations, vibratome sections, frozen sections) were evaluated. As a model we used transgenic mice expressing EGFP under the control of a 5.0-kb fragment of the glutathione peroxidase isoenzyme 5 protein promoter (GPX5-EGFP) or under a 3.8-kb fragment of the cysteine rich protein-1 promoter (CRISP1-EGFP). In the GPX5-EGFP mice, expression of EGFP was observed in the distal part of the caput epididymis, while the CRISP1 promoter directed EGFP expression in the tubular compartment of the testis. Among the various tissue preparation procedures tested, the best morphological and histological preservation, and reproducibility in EGFP detection, were obtained using frozen sections after a slow tissue-freezing protocol developed in the present study. After slow tissue freezing, specimens of testis and epididymis could be stored at -70 degrees C for at least six weeks without any affect on EGFP fluorescence. Hence, the method developed offers the possibility to analyze EGFP fluorescence in tissues several weeks after specimen collection. The sensitivity achieved was equal to that found in immunohistochemistry, applying biotin-streptavidin-FITC detection. Confocal microscopy is known to have the advantage that fluorescence can be detected from cells in different layers. This was found to be important as regards detecting EGFP fluorescence because the fluorescence was destroyed at the cut surfaces of sections produced by either vibratome or cryomicrotome.
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PMID:Improved technique for detection of enhanced green fluorescent protein in transgenic mice. 1141 19

To investigate the function of glutathione peroxidase (GPX) in plants, we produced transgenic tomato plants overexpressing an eukaryotic selenium-independent GPX (GPX5). We show here that total GPX activity was increased by 50% in transgenic plants, when compared to control plants transformed with the binary vector without the insert (PZP111). A preliminary two-dimensional electrophoretic protein analysis of the GPX overexpressing plants showed notably a decrease in the accumulation of proteins identified as rubisco small subunit 1 and fructose-1,6-bisphosphate aldolase, two proteins involved in photosynthesis. These observations, together with the fact that in standard culture conditions, GPX-overexpressing plants were not phenotypically distinct from control plants prompted us to challenge the plants with a chilling treatment that is known to affect photosynthesis activity. We found that upon chilling treatment with low light level, photosynthesis was not affected in GPX-overexpressing plants while it was in control plants, as revealed by chlorophyll fluorescence parameters and fructose-1,6-biphosphatase activity. These results suggest that overexpression of a selenium-independent GPX in tomato plants modifies specifically gene expression and leads to modifications of photosynthetic regulation processes.
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PMID:Modification of photosynthetic regulation in tomato overexpressing glutathione peroxidase. 1592 56

When exposed to strong sunlight, photosynthetic organisms encounter photooxidative stress by the increased production of reactive oxygen species causing harmful damages to proteins and membranes. Consequently, a fast and specific induction of defense mechanisms is required to protect the organism from cell death. In Chlamydomonas reinhardtii, the glutathione peroxidase homologous gene GPXH/GPX5 was shown to be specifically upregulated by singlet oxygen formed during high light conditions presumably to prevent the accumulation of lipid hydroperoxides and membrane damage. We now showed that the GPXH protein is a thioredoxin-dependent peroxidase catalyzing the reduction of hydrogen peroxide and organic hydroperoxides.Furthermore, the GPXH gene seems to encode a dual-targeted protein, predicted to be localized both in the chloroplast and the cytoplasm, which is active with either plastidic TRXy or cytosolic TRXh1. Putative dual-targeting is achieved by alternative transcription and translation start sites expressed independently from either a TATA-box or an Initiator core promoter. Expression of both transcripts was upregulated by photooxidative stress even though with different strengths. The induction required the presence of the core promoter sequences and multiple upstream regulatory elements including a Sp1-like element and an earlier identified CRE/AP-1 homologous sequence. This element was further characterized by mutation analysis but could not be confirmed to be a consensus CRE or AP1 element. Instead, it rather seems to be another member of the large group of TGAC-transcription factor binding sites found to be involved in the response of different genes to oxidative stress.
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PMID:Function and regulation of the glutathione peroxidase homologous gene GPXH/GPX5 in Chlamydomonas reinhardtii. 1969 Sep 65

This study investigated whether specific proteins from distinct seminal plasma fractions of boars could be related to in vivo fertility. Nine boars with acceptable sperm motility and morphology for use in artificial insemination demonstrated major differences in total number born and pregnancy rate when low sperm doses (1.5 billion sperm) were used to breed a minimum of 50 gilts per boar. The 2 lowest-fertility and 2 highest-fertility boars were chosen for evaluation of specific seminal plasma proteins. On 4 occasions, semen was collected and separated into 3 fractions based on sperm concentration (Sperm-Peak, Sperm-Rich, and Sperm-Free), and the fractions were analyzed for total protein concentration and abundance of major seminal plasma glycoprotein (PSP-I), AWN-1, and osteopontin protein using Western blotting techniques. The concentrations of these seminal plasma proteins were lower in the Sperm-Peak fractions compared with the Sperm-Free fractions (P < .05). Seminal plasma from the pooled Sperm-Rich fraction used for artificial insemination was also subjected to two-dimensional gel electrophoresis to investigate novel protein markers related to in vivo fertility. Total piglets born (r = -0.76, P = .01) and sperm motility at day 7 (r = -0.74, P = .037) were again negatively correlated with a 22-kDa protein identified by mass spectrometry as PSP-I. However, fertility index and farrowing rate tended to be positively correlated (P < .10) with a 25-kDa protein, identified as glutathione peroxidase (GPX5), an antioxidant enzyme that may protect sperm membranes from oxidative damage. These candidate proteins merit further investigation as markers of fertility in boars.
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PMID:Seminal plasma proteins as potential markers of relative fertility in boars. 1971 65


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