Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:2.5.1.18 (glutathione S-transferase)
22,582 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of endosulfan, a widely used organochlorine pesticide, on cortisol secretion, cell viability, antioxidants and lipid peroxidation were investigated in enzymatically dispersed head kidney cells of rainbow trout (Oncorhynchus mykiss). ACTH- and dbcAMP-stimulated cortisol secretion, and cell viability were impaired in a dose-related manner following acute in vitro exposure to endosulfan (EC(50) 19 microM, LC(50) 366 microM) and the loss of cortisol secretion was detected even at concentrations of endosulfan that did not decrease cell viability. Stimulation with dbcAMP did not restore cortisol secretion in endosulfan exposed cells while stimulation with pregnenolone maintained cortisol secretion until viability of cells was affected. Thus endosulfan may disrupt processes between the step generating cAMP and the step where pregnenolone is used. Activity of catalase increased at concentrations of endosulfan that did not impair cortisol secretion, and decreased at higher doses. Glutathione peroxidase (GPx) activity was significantly reduced at doses of endosulfan that also reduced levels of glutathione, an essential cofactor of GPx. Exposure up to 1 x 10(-7) M endosulfan increased the activity of glutathione transferase. The present in vitro study identified endosulfan as a chemical inducing a loss of secretory responses in teleost adrenocortical steroidogenic cells and alterations in the activity of enzymes known to be involved in oxidative stress pathways. Moreover, the significant increase in lipid hydroperoxides levels provided further evidence for endosulfan-induced oxidative stress.
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PMID:Oxidative stress and loss of cortisol secretion in adrenocortical cells of rainbow trout (Oncorhynchus mykiss) exposed in vitro to endosulfan, an organochlorine pesticide. 1271 13

Cellular defense system, including glutathione, glutathione-related enzymes, and antioxidant and redox enzymes, may play crucial roles in the aging of aerobic organisms. To understand the physiological roles of these factors in the aging process, their levels were compared in the livers and brains of 5-week- and 9-month-old rats. GST activity was higher in livers and brains of 9-month-old rats than in those of 5-week-old rats, and brain catalase activity was about 2-fold higher. However, it was unchanged in the livers of the 9-month-old rats. gamma-Glutamylcysteine synthetase activity was about 2-fold higher in the brains of the older rats but again not in their livers. In contrast glutathione synthetase activity appeared to be lower in the livers of the older rats while GSH content did not change with age in livers and brains. Glutathione peroxidase activity was higher in 9-month-old rat brains, but lower in 9-month-old rat livers, while superoxide dismutase activity was higher in both tissues in the older rats. The activities of two redox enzymes, thiol-transferase and thioredoxin reductase, did not change with age, nor did that of glutathione reductase. These results indicate that levels of different cellular defense systems vary with age in an irregular manner.
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PMID:Age-related changes in the activity of antioxidant and redox enzymes in rats. 1474 15

This study assesses the antioxidant enzymes activities viz., catalase, glutathione peroxidase, glutathione S-transferase and nonenzymatic antioxidant molecule such as glutathione in Anguilla anguilla L. gill, kidney and liver in response to 8- and 48-h exposure to bleached kraft pulp mill effluent (BKPME). A. anguilla were caged and plunged at three different sites-50 (Site 1), 100 (Site 2) and 2000 m (Site 3) away from the closed BKPME outlet. A significant gill (8 and 48 h) and kidney (48 h) catalase activity decrease was observed at site 2 exposure whereas liver showed a significant increase in catalase activity after 8 and 48 h to site 1 exposure. Glutathione peroxidase (GPX) activity was significantly decreased in gill after 8-h exposure to site 1 and 48-h exposures to sites 1 and 2, respectively. Concerning gill, kidney and liver glutathione S-transferase (GST) activity, a significant gill GST activity decrease after 8 h at site 2 and 48 h at sites 1 and 2 was observed; in kidney, a significant decrease in its activity was observed after 48 h at sites 1 and 2, respectively, whereas in liver, the decrease was significant only at site 2 after 48-h exposure. The in situ BKPME exposure caused a significant total gill and kidney reduced glutathione (GSH) decrease after 8 h at site 2 exposure and after 48 h at site 1 and 2 exposures, respectively. However, a biphasic response was observed in liver, i.e. initial significant increase after 8 h at site 2 followed by a significant decrease after 48 h to the same site exposure. The enzymatic and nonenzymatic antioxidants pattern in gill and kidney, as observed in this study, was different than liver, demonstrating that the liver was more resistant to oxidative damage than gill and kidney. In addition, A. anguilla gill, kidney and liver antioxidants adaptation potentials may serve as a surrogate biomarker to BKPME exposure.
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PMID:Anguilla anguilla L. antioxidants responses to in situ bleached kraft pulp mill effluent outlet exposure. 1498 59

Glutathione peroxidase (GPx, EC 1.11.1.9) protects cells against oxidative damage by catalyzing the reduction of hydroperoxides with glutathione (GSH). Several attempts have been made to imitate its function for mechanical study and for its pharmacological development as an antioxidant. By replacing the active site serine 9 with a cysteine and then substituting it with selenocysteine in a cysteine auxotrophic system, catalytically essential residue selenocysteine was bioincorporated into GSH-specific binding scaffold, and thus, glutathione S-transferase (GST, EC 2.5.1.18) from Lucilia cuprina was converted into a selenium-containing enzyme, seleno-LuGST1-1, by genetic engineering. Taking advantage of the important structure similarities between seleno-LuGST1-1 and naturally occurring GPx in the specific GSH binding sites and the geometric conformation for the active selenocysteine in their common GSH binding domain-adopted thioredoxin fold, the as-generated selenoenzyme displayed a significantly high efficiency for catalyzing the reduction of hydrogen peroxide by glutathione, being comparable with those of natural GPxs. The catalytic behaviors of this engineered selenoenzyme were found to be similar to those of naturally occurring GPx. It exhibited pH and temperature-dependent catalytic activity and a typical ping-pong kinetic mechanism. Engineering GST into an efficient GPx-like biocatalyst provided new proof for the previous assumption that both GPx and GST were evolved from a common thioredoxin-like ancestor to accommodate different functions throughout evolution.
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PMID:Engineering glutathione transferase to a novel glutathione peroxidase mimic with high catalytic efficiency. Incorporation of selenocysteine into a glutathione-binding scaffold using an auxotrophic expression system. 1564 95

Transgenic cotton (Gossypium hirsutum L.) lines expressing the tobacco glutathione S-transferase (GST) Nt107 were evaluated for tolerance to chilling, salinity, and herbicides, antioxidant enzyme activity, antioxidant compound levels, and lipid peroxidation. Although transgenic seedlings exhibited ten-fold and five-fold higher GST activity under normal and salt-stress conditions, respectively, germinating seedlings did not show improved tolerance to salinity, chilling conditions, or herbicides. Glutathione peroxidase (GPX) activity in transgenic seedlings was 30% to 60% higher under normal conditions, but was not different than GPX activity in wild-type seedlings under salt-stress conditions. Glutathione reductase, superoxide dismutase, ascorbate peroxidase, and monodehydroascorbate reductase activities were not increased in transgenic seedlings under salt-stress conditions, while dehydroascorbate reductase activity was decreased in transgenic seedlings under salt-stress conditions. Transgenic seedlings had 50% more oxidized glutathione when exposed to salt stress. Ascorbate levels were not increased in transgenic seedlings under salt-stress conditions. Malondialdehyde content in transgenic seedlings was nearly double that of wild-type seedlings under normal conditions and did not increase under salt-stress conditions. These results show that expression of Nt107 in cotton does not provide adequate protection against oxidative stress and suggests that the endogenous antioxidant system in cotton may be disrupted by the expression of the tobacco GST.
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PMID:Transgenic cotton (Gossypium hirsutum L.) seedlings expressing a tobacco glutathione S-transferase fail to provide improved stress tolerance. 1582 6

Resveratrol is a polyphenolic chemopreventive agent that has been shown to influence cellular redox reactions. As a systematic approach to elucidating the complex effects of resveratrol on eukaryotic cells, we studied its dose-dependent effects on the transcript levels of genes and activities of enzymes related to redox metabolism, cell cycle regulation, and apoptotic cascades in the cancer cell line A549. Glutathione peroxidase (GPx)1 mRNA levels, as well as GPx and thioredoxin reductase (TrxR) activities, were significantly increased after resveratrol treatment, whereas total glutathione concentrations decreased. Increased transcript levels were also detected for selenophosphate synthetase 2 and superoxide dismutase 2. However, mRNA levels of thioredoxin, TrxR, glutathione reductase, glutathione S-transferase, superoxide dismutase 1, and catalase were not altered. Among the 12 genes studied that are related to the cell cycle, differentiation and apoptosis, mRNA levels of six genes, including P53, FAS, and BCL2, were upregulated, while the mRNA level of survivin was reduced. The results suggest that GPx and other selenoproteins are important targets of resveratrol. Furthermore, genes supporting cell survival and differentiation, as well as genes involved in proliferation inhibition and apoptosis, are induced by resveratrol, resulting in a delicate balance that is likely to contribute to the chemopreventive effects of resveratrol.
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PMID:Resveratrol modulates mRNA transcripts of genes related to redox metabolism and cell proliferation in non-small-cell lung carcinoma cells. 1726 Oct 84

The effects of intraperitoneal injection of diethyldithiocarbamate (DDC) on free radical processes were examined in brain, liver and kidney of goldfish (Carassius auratus). Levels of oxidatively modified lipids and proteins as well as the activities of antioxidant and associated enzymes were measured. Intraperitoneal injection of DDC at a concentration of 0.01 mg/g wet mass decreased SOD activities by about 30-50% after 48 and 168 h compared to corresponding sham-injected values. This treatment resulted in transient oxidative stress. Lipid peroxide content increased after DDC injection at all time points in the kidney, after 48 h in the liver and was elevated in most experimental groups in the brain. Thiobarbituric-acid reactive substances (end products of lipid peroxidation) rose within the first 48 h after injection, but returned to initial levels after 168 h. Two other indices of oxidative stress were also transiently modified: protein carbonyl levels in the brain and kidney increased 24h post-injection, and the low-molecular mass thiol content was reduced over the same period in all tissues examined. Activities of catalase, glutathione peroxidase, glutathione-S-transferase, glutathione reductase, and glucose-6-phosphate dehydrogenase showed differential responses to DDC treatment that rebounded by 168 h post-injection. Glutathione peroxidase activities were reduced by 60, 45 and 65% in the brain, liver and kidney, respectively, after 24h but rebounded thereafter. After 48 h post-injection with DDC significant decreases were also seen in liver and kidney catalase, GST activities in all three tissues, and kidney GR and G6PDH activities. In some cases, catalase, GST, GR and G6PDH activities transiently increased after 24 h. It was concluded that DDC injection depleted SOD and simultaneously stimulated lipid peroxidation, but did not require compensatory enhancement of other enzymatic defenses. Different actions of the superoxide anion in cellular metabolism and possible consequences of the impairment of superoxide dismutase are discussed.
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PMID:Diethyldithiocarbamate injection induces transient oxidative stress in goldfish tissues. 1766 2

The present study was designed to understand the oxidative stress potential of fenthion, an organophosphate (OP) pesticide and its involvement in glutathione metabolism modulated buthionine sulfoximine (BSO, 50 mg/kg) and N-acetylcysteine (NAC, 100 mg/kg) in the brain of fish, Oreochromis niloticus. A sublethal fenthion concentration (0.45 mg/L) was applied for 24, 48, and 96 h together with injection with BSO or NAC; following treatment, recovery periods for 24, 48, and 96 h were allowed. Total glutathione (tGSH), oxidized glutathione (GSSG), lipid peroxidation, protein level, and GSH-related enzyme activities were analyzed by using spectrophotometric methods. Fenthion in applied concentration did not change GSH levels, but increased GSSG levels. BSO application in fenthion exposure caused a depletion in GSH, while increasing the GSSG levels. Glutathione peroxidase (GPx; EC 1.11.1.9) specific activity increased in fenthion-applied groups at 24-h treatment. gamma-Glutamylcysteinyl synthetase (gamma-GCS; EC 6.3.2.2) was not detected in the brain. NAC injection in fenthion treatment decreased GSH and increased GSSG levels and GST activity. In conclusion, fenthion in sublethal concentration induced an oxidative stress processes in brain. BSO application provided an evidence for the involvement of fenthion in GSH metabolism. NAC elevated the fenthion-induced effects in spite of its antioxidant properties. Recovery period for 96 h was not adequate to eliminate the fenthion-induced changes.
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PMID:In vivo effects of fenthion on oxidative processes by the modulation of glutathione metabolism in the brain of Oreochromis niloticus. 1800 Aug 50

We studied the antioxidant enzyme response of the gastropoda Bittium reticulatum feeding the toxic alga Caulerpa taxifolia, and also the effects of intense herbivorism on caulerpenyne production and on the antioxidant response of C. taxifolia. B. reticulatum were maintained in two separated aquariums containing Posidonia oceanica or C. taxifolia. Glutathione peroxidase, glutathione reductase and glutathione S-transferase activities were significantly higher in B. reticulatum living in presence of C. taxifolia with respect to animals living in P. oceanica aquarium. Malondialdehyde levels in B. reticulatum showed similar values in both environments. Caulerpenyne levels were significantly higher in C. taxifolia fronds after herbivore exposure. C. taxifolia activities of catalase and glutathione reductase significantly increased in presence of B. reticulatum. B. reticulatum exposed to caulerpenyne evidenced antioxidant enzyme adaptations to prevent oxidative damage. The presence of B. reticulatum in the aquarium induces a protective adaptation in C. taxifolia in order to reduce the herbivorism.
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PMID:Reciprocal effects of caulerpenyne and intense herbivorism on the antioxidant response of Bittium reticulatum and Caulerpa taxifolia. 1823 33

Glutathione peroxidase (GPX) and glutathione S-transferase (GST) are key enzymes of cellular detoxification systems that defend cells against reactive oxygen species (ROS). In this study, we isolated the GPX and GST full-length cDNA and investigated the expression of these mRNAs from livers of olive flounder during salinity changes (35, 17.5, 8.75, 4 and 0 psu) by quantitative PCR (QPCR). GPX cDNA consists of 429 base pairs (bp) and encodes a protein of 142 amino acids. GST cDNA consists of 663 bp and encodes a protein of 220 amino acids. Both of GPX and GST mRNA expressions were the highest in 4 psu and then decreased in 0 psu. Also, the levels of Na(+) and Cl(-) decreased, and aspartate aminotransferase (AST) and alanine aminotransferase (ALT) increased during the experimental period. These findings provide molecular characterization of GPX and GST in olive flounder and suggest that GPX and GST play important roles in detoxification of ROS, thereby these maybe indicators of oxidative stress responses by salinity changes in olive flounder.
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PMID:Molecular characterization and mRNA expression of glutathione peroxidase and glutathione S-transferase during osmotic stress in olive flounder (Paralichthys olivaceus). 1830 88


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