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 effect of unilateral pneumonectomy on the drug-metabolizing capability of the remaining lung of male rabbits was studied 3, 10, and 28 days after surgery. During the period of compensatory lung growth which follows pneumonectomy, the contralateral lung had a reduced ability to metabolize some model drug substrates. The activities of 4-chloro-N-methylaniline demethylase, glutathione transferase, and 4-aminobenzoate N-acetyltransferase were significantly decreased in pneumonectomizd animals relative to shamoperated controls at 10 days. By 28 days most of these parameters of drug metabolism had returned to control levels. Lung hydroxyproline concentration, an index of collagen, did not differ in pneumonectomized and control animals at any of the time points. 3-Methylcholanthrene failed to induce the pulmonary mono-oxygenase system in pneumonectomized animals. The response of pulmonary drug-metabolizing enzymes to unilateral pneumonectomy in rabbits was temporally and qualitatively similar to the response in rat liver following partial hepatectomy.
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PMID:The effect of unilateral pneumonectomy on in vitro drug metabolism by the contralateral lung of rabbits. 3 21

Dihalomethanes are metabolized to carbon monoxide both in vivo and in vitro. The reaction is catalyzed by a hepatic microsomal cytochrome P-450 dependent mixed function oxidase system. Bioorganic mechanism studies suggest an initial oxygen insertion reaction followed by rearrangement to a formyl halide intermediate which in turn decomposes to yield carbon monoxide. In vitro studies show that 14C-dichloromethane becomes covalently bound to both microsomal protein and lipid. The similar characteristics of metabolism to carbon monoxide and covalent binding suggests that a common intermediate, perhaps the formyl halide, may be involved. Dihalomethanes are also metabolized to formaldehyde, formic acid, and inorganic halide. A glutathione transferase, located in hepatic cytosol fractions, appears to be involved. Reaction mechanism studies suggest that a S-hydroxymethyl glutathione intermediate may yield formaldehyde or be diverted via formaldehyde dehydrogenase/S-formyl glutathione hydrolase to yield formic acid. Haloforms are also metabolized in vitro to carbon monoxide by a hepatic microsomal cytochrome P-450 dependent mixed function oxidase system. This reaction is a markedly stimulated by sulfhydryl compounds.
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PMID:Metabolism of halogenated methanes and macromolecular binding. 9 15

Poly(A)-containing rat liver mRNA isolated from animals injected with phenobarbital and uninjected controls was translated efficiently in a wheat-germ system. The synthesis of ligandin (glutathione S-transferase B; glutathione transferase; RX-gluathione R-transferase, EC 2.5.1.18) was detected by immunoprecipitation with a highly purified monospecific ligandin antibody and analysis by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. The extent of incorporation of [35S]methionine into ligandin in the translation system was similar for poly(A)-containing messages from un-infected animals and those treated with phenobarbital.
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PMID:Translation in vitro of rat liver messenger RNA coding for ligandin (glutathione S-transferase B). 26 12

The reduction of linoleic acid hydroperoxide catalysed by rat liver cytosol was previously shown to be catalysed by a selenium-dependent glutathione peroxidase. In contrast, the enzyme responsible in guinea-pig liver cytosol is not selenium-dependent and appears to be a glutathione transferase.
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PMID:Lipid and steroid hydroperoxides as substrates for the non-selenium-dependent glutathione peroxidase. 43 67

Ligandin (Y protein) is an abundant cytoplasmic glutathione transferase present in liver, kidney and gut in various animals and man. Its interaction with four radiologic contrast media (Telepaque, 3-(3 amino-2,4,6, triiodophenyl -2 ethylpropanoic acid, sodium salt; Hypaque, sodium -3, 5-diacetamido-2,4,6,-triiodobenzoate; Cholografin, N,N'adipyl-bis-(3-amino-2,4,6-triiodobenzoic acid) N-methyl-glucosamine; Diodrast, 3,5-Diiodo-4-pyridone-N-acetic acid, Diethanolamine Salt was investigated by observing inhibitory effects on the enzyme-catalyzed conjugation of glutathione with 1-chloro-2, 4-dinitrobenzene. Lineweaver-Burk plots of reciprocal initial velocity versus reciprocal inhibitor concentrations at fixed glutathione and chlorodinitrobenzene concentrations demonstrate non-competitive inhibition by all contrast media except Diodrast. No conjugates of contrast media with glutathione were formed. It is postulated that intracellular accumulation of contrast media is aided by intracellular binding with ligandin. Inhibition of the GSH transferase activity of ligandin can disrupt the mercapturate formation, an important detoxification process.
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PMID:Interaction of ligandin with radiographic contrast media. 100 14

1. The alkenyl phosphate insecticide, dimethylvinphos, is rapidly metabolized and eliminated by rats and dogs. 2. Metabolism proceeds via demethylation followed by the hydrolysis of desmethyl dimethylvinphos to 2,4-dichlorophenacyl chloride which is further metabolized mainly to 2,4-dichloromandelic acid, 1-(2,4-dichlorophenyl)ethanol (glucuronide) and 2,4-dichlorphenylethanediol (glucuronide). 3. The dechlorination of 2,4-dichlorophenacyl chloride to 2,4-dichloroacetophenone proceeds via the spontaneous formation of S-(2,4-dichlorophenacyl) glutathione which is converted to the ketone by an enzyme-catalysed glutathione-dependent reaction. 4. Demethylation of dimethylvinphos occurs in liver fractions via the action of two enzymes: glutathione S-methyl transferase in the cytosol, and microsomal mono-oxygenase. The relatively high activities of both enzymes in dog liver (compared with rat liver) partly account for the observed differences in metabolism and toxicity of dimethylvinphos in the two species. 5. The glutathione transferase is enhanced twofold by pre-treatment of rats with 0-1% phenobarbital in their drinking water. This treatment also induces the microsomal demethylation 45-fold and results in a greater than 13-fold protective effect against the acute toxic effects of dimethylvinphos.
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PMID:Metabolic demethylation of the insecticide dimethylvinphos in rats, in dogs, and in vitro. 100 19

Circular dichroism methods were used to study the structure of rat ligandin and the binding of organic anions to the protein. Ligandin has a highly ordered secondary structure with about 40%alpha helix, 15% beta structure, and 45% random coil. Bilirubin binding occurred primarily at a single high affinity site on the protein. The binding constant for bilirubin (5 X 10-7 Mminus 1) was the highest among the ligands studied. The bilirubin-ligandin complex exhibited a well-defined circular dichroic spectrum with two major overlapping ellipticity bands of opposite sign in the bilirubin absorption region. This spectrum was virtually a mirror image of that of human or rat serum albumin-bilirubin complexes. Studies on the direct transfer of bilirubin from ligandin to rat serum albumin showed that sasociation constants of bilirubin-ligandin complexes were approximately tenfold less than those of the bilirubin-albumin system. Ligandin exhibited a broad specificity with respect to the typeof ligand bond. A series of organic anions inclucing dyes used clinically for liver function tests, fatty acids, hormones, heme derivatives, bile acids, and other ligands that were considered likely to interact with ligandin, were examined. Most induced ellipticity changes consistent with competitive displacement of bilirubin from ligandin and relative affinities of these compounds for ligandin were determined based on their effectiveness in desplacing the bilirubin. Some substances such as glutathione, conjugated sulfobromophthaleins and lithocholic acid bound to ligandin but induced anomalous spectral shifts, when added to ligandin-bilirubin complexes. Other compounds, including some that act as substrates for the glutathione transferase activity exhibited by ligandin, revealed no apparent competitive effects with respect to the bilitubin binding site.
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PMID:Interactions of bilirubin and other ligands with ligandin. 114 65

Male C57Bl/6 mice were treated for 5 days with 0.05% perfluorooctanoic acid (PFOA) in their diet. This treatment resulted in a potent induction of peroxisomal fatty acid beta-oxidation in the liver. In order to investigate recovery from treatment with PFOA, mice were given normal laboratory chow for up to 20 days after termination of PFOA administration. It was established that the activities of peroxisomal lauoryl-CoA oxidase and palmitoyl-CoA oxidation were still elevated 2-3 weeks after termination of treatment. The catalase activity recovered in the cytosolic fraction was also still significantly elevated after 20 days with normal laboratory chow. Furthermore, the protein content of the mitochondrial fraction was increased by PFOA and had not returned to control level at the end of the recovery period. Perfluorooctanoic acid also caused a persistent effect in omega hydroxylation of lauric acid (cytochrome P-452). The activities of cytosolic DT-diaphorase and glutathione transferase were also enhanced by PFOA. However, these two enzymes recovered relatively rapidly from the treatment (2-20 days). This study reveals two different patterns of recovery from PFOA treatment, one involving parameters that recovered completely, or almost completely, from PFOA treatment after 20 days and another involving parameters that were still elevated at the end of the recovery period.
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PMID:Perfluorooctanoic acid has persistent effects on peroxisome proliferation and related parameters in mouse liver. 129 9

The individual and combined effects of dietary toasted soybean meal (3.13-25%) and dietary licorice root extract (0.38-3.0%) on selected liver and intestinal enzyme levels and on clinical chemistry and histopathological parameters were evaluated on male F344 rats. All parameters were measured one and three months after the 50-day-old rats were started on the diets. By use of newly developed high-performance liquid chromatography-based analytic methods, measurable levels of daidzein (2.67 micrograms/ml) and glycyrrhetinic acid (7.87 micrograms/ml) were detected in the sera of rats on the 25% soybean and 3% licorice diets, respectively. Histopathological evaluations of organs and tissues yielded only nonsignificant strain-related changes. At all dosages, there were no significant soybean- or licorice-related anatomic lesions or hematologic changes. In the clinical biochemistry profile, soybean meal caused moderate but significant dose-dependent decreases in serum cholesterol and increases in alkaline phosphatase, blood urea nitrogen, and phosphorus, which remained within the normal range. Liver glutathione transferase, catalase, and protein kinase C showed significant inductions (up to 50%) in response to increasing doses of soybean meal and licorice extract, with evidence for only marginal interaction between the two additives. Their effects on the intestinal mucosa were not significant. Ornithine decarboxylase levels, an indicator of promotional activity, were unchanged or repressed by the additives. The favorable effects of up to 25% toasted soybean meal and 3% licorice root extract on the levels of the four enzymes, without unfavorable changes in clinical parameters, might account in part for the chemopreventive activities of these additives. These effects would be in addition to direct inhibitory effects of known components in these additives on these or other enzymes or modulation of hormone activity that is not evaluated in this study.
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PMID:Effect of dietary soybean and licorice on the male F344 rat: an integrated study of some parameters relevant to cancer chemoprevention. 129 95

Kinetic parameters of 9 substrates interaction with glutathione transferase (GST) from spring grain aphid and rat were studied. The most significant difference in Vmax values was noticed for 4-nitropyridine-N-oxide (6 times higher for aphid) and ethacrynic acid (7 times higher for rat). Km values were practically in all cases higher for aphid GST as compared to rat GST. New class of effectors of GST suggested by us, that is azimines (2 series), was used for the inhibitor analysis. GST interaction with these inhibitors was appreciated by three types of activity: nucleophilic replacement, thiolysis and N-deoxygenation. It has been shown that the degree of GST inhibition depended considerably both on the GST source and the substrate used. New high-effective inhibitors of GST were found among azimines and their higher specificity to rat GST as compared to aphid GST was demonstrated especially in thiolysis reaction.
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PMID:[A comparative study of the substrate and inhibitor specificity of the glutathione transferase from the spring grain aphid (Schizaphis gramina Rond.) and from rat liver]. 130 16


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