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)

We have purified two isoenzymes of glutathione S-transferase from bovine retina to apparent homogeneity through a combination of gel-filtration chromatography, affinity chromatography and isoelectric focusing. The more anionic (pI = 6.34) and less anionic (pI = 6.87) isoenzymes were comparable with respect to kinetic and structural parameters. The Km for both substrates, reduced glutathione and 1-chloro-2,4-dinitrobenzene, bilirubin inhibition of glutathione conjugation to 1-chloro-2,4-dinitrobenzene, 1-chloro-2,4-dinitrobenzene inactivation of enzyme activity and molecular weight were similar. However, pH optimum and energy of activation were found to differ considerably. Retina was found to have no selenium-dependent glutathione peroxidase activity. The total glutathione peroxidase activity fractionated with the transferases in the gel-filtration range of mol.wt. 49000 and expressed activity with only organic hydroperoxides as substrate. Only the more anionic isoenzyme expressed both transferase and peroxidase activity.
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PMID:Glutathione S-transferases of the bovine retina. Evidence that glutathione peroxidase activity is the result of glutathione S-transferase. 712 77

Sheep antibodies raised against three isoenzymes of glutathione S-transferase (EC 2.5.1.18), transferases B, C, and E, which were isolated and purified to apparent homogeneity from rat liver, have been employed to localize these enzymes at the light microscopic level within livers of untreated rats. Using these antibodies in an unlabeled antibody peroxidase-antiperoxidase staining technique, each glutathione S-transferase was detected immunohistochemically within parenchymal cells throughout the liver lobule. In addition, immunohistochemical staining for transferases C and E, but not for transferase B, was observed within bile duct epithelium. While all parenchymal cells were stained with each glutathione S-transferase antibody, the patterns of immunohistochemical staining intensity observed across the liver lobule with the three anti-transferases were not uniform: parenchymal cells within the centrilobular region were more intensely stained for each lobular region were more intensely stained for each isoenzyme than were those within the midzonal and periportal regions of the lobule. The results of this immunohistochemical study thus demonstrate that glutathione S-transferases are not distributed uniformly throughout the liver lobule and that each transferase is present in the greatest concentration within the centrilobular region of the lobule.
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PMID:Immunohistochemical localization of glutathione S-transferases in livers of untreated rats. 717 91

The number of binding sites and the dissociation constants were determined for the binding of bilirubin to human liver ligandin and to human serum albumin. Albumin has a primary bilirubin binding site (KD = 0.03 microM), measured by the peroxidase procedure, and two apparently equivalent secondary binding sites (KD = 2 microM), determined by fluorescence quenching experiments. By contrast, ligandin does not have a corresponding high affinity site. The absence of this high affinity site was shown both by the peroxidase procedure and by direct competition between albumin and ligandin for bilirubin. Bilirubin binding to ligandin, measured by fluorescence quenching, is complex. At both pH 6.5 and 7.4, two interacting sites were observed with a Hill coefficient of 1.5, K' approximately 5 microM. Bilirubin binding to ligandin is not independent of glutathione S-transferase activity. Depending upon pH and upon the order with which the reactants are added, bilirubin can markedly alter the transferase activity. The results are interpreted in terms of kinetically stable conformational isomers of ligandin induced by bilirubin or by glutathione.
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PMID:Bilirubin binding to human liver ligandin (glutathione S-transferase). 737 7

The reduction of linoleic acid hydroperoxide catalyzed by rat liver cytosol was previously shown to be catalyzed by a selenium-dependent glutathione peroxidase. In contrast, the activity in rabbit liver cytosol could also be attributed to a selenium-dependent peroxidase. The selenium-independent peroxidase copurified with glutathione transferase B and was completely inhibited by antitransferase B antiserum and transferase substrates. These results suggest that glutathione transferase B in rabbit liver cytosol is involved in the intracellular decomposition of lipid peroxide and could explain the lower selenium requirement of rabbits in comparison with other species.
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PMID:Selenium-independent glutathione peroxidase activity in rabbit liver. 745 69

The expression and localization of glutathione S-transferase (GST) isoenzymes in the epithelium of normal oral mucosa (n = 9), overlying reactive fibrous hyperplasia (n = 9), and of potentially malignant [leukoplakia (n = 25), submucous fibrosis (n = 12), verrucous hyperplasia (n = 16)] and malignant [squamous cell carcinoma (n = 36), verrucous carcinoma (n = 13)] oral lesions were examined immunohistochemically using polyclonal antibodies raised against GST isoenzymes (alpha, mu and pi) with the standard avidin-biotin-peroxidase complex (ABC) method. GST alpha, mu and pi were almost completely absent in the epithelium of normal oral mucosa and overlying benign fibrous tissues. GST alpha staining was cytoplasmic and focally positive, while GST mu staining was similar to but weaker than that seen for GST alpha. GST pi showed both cytoplasmic and nuclear staining and was expressed in 60% of leukoplakias with mild dysplasia (n = 15), 80% of leukoplakias with moderate to severe dysplasia (n = 10). 75% of submucous fibrosis samples (n = 12), 75% of verrucous hyperplasias (n = 16), 77% of verrucous carcinomas (n = 13), 81% of well-differentiated squamous cell carcinomas (n = 26) and 70% of moderate- to poorly-differentiated squamous cell carcinomas (n = 10). In addition, GST pi expression was independent of the state of differentiation of oral cancers. Since GST pi was significantly over-expressed in the oral premalignant and malignant lesions, the kinetics of GST pi-positive cells and the value of GST pi as a tumor marker in oral carcinogenesis need further investigation.
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PMID:Immunohistochemical demonstration of epithelial glutathione S-transferase isoenzymes in normal, benign, premalignant and malignant human oral mucosa. 747 69

Adult female rats subjected to exercise training in the form of swimming daily (for 20 min initially with gradual increase up to 90 min within a week) for 130 days showed a significant elevation of liver glutathione S-transferase (GST) activity when compared to controls. Electrophoresis and Western blot analysis of cytosolic as well as affinity-purified hepatic glutathione S-transferases revealed the induction of Ya-sized subunit in exercise-trained animals. Reverse-phase HPLC analysis of affinity-purified GSTs further revealed that Ya-sized subunits in control animals consisted of predominantly Ya2, whereas the trained animals displayed a dramatic 4.3-fold increase in Ya1. The GSTs of exercise-trained animals showed increased peroxidase activity when compared to corresponding controls, which is consistent with the changes in sub-unit composition. This could be a response to the physiological oxidative stress induced by physical exercise.
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PMID:Induction of Ya1 subunit of rat hepatic glutathione S-transferases by exercise-induced oxidative stress. 748 74

In this study, we have characterized quinone reductase (QR), glutathione (GSH), glutathione S-transferase (GST) and their induction by a chemoprotector, 1,2-dithiole-3-thione (D3T), in the human myeloid cell lines ML-1 and HL-60. In addition, we also examined the toxicity of hydroquinone (HQ), a benzene metabolite, to these two cell lines. Both of the cell lines contain a basal level of cellular GSH, which is similar in the two cell lines. Although ML-1 cells contain much higher QR specific activity than HL-60 cells, which are relatively QR deficient, the GST specific activity of ML-1 cells is 1.8 times less than that of HL-60 cells. Immunoblot experiments showed that the GST in these two cell lines is GST pi. In addition, HL-60 cells exhibit 4.5 times more myeloperoxidase specific activity than ML-1 cells. Inclusion of D3T in the cultures could induce significant increases in cellular GSH content and QR activity, but not GST activity in either cell line. Treatment with HQ caused both inhibition of cell proliferation and loss of cell viability in these two myeloid cell lines. HQ treatment also resulted in a significant depletion of cellular GSH, which preceded the loss of cell viability. Pretreatment of both cell lines with buthionine sulfoximine, an inhibitor of GSH biosynthesis, markedly increased HQ-induced toxicity. In contrast, the presence of dicumarol, a QR inhibitor, failed to potentiate HQ-induced toxicity in ML-1 cells. On the other hand, pretreatment of these two myeloid cell lines with D3T significantly protected against HQ-induced inhibition of cell proliferation and cell death. Therefore, the above results suggest that GSH but not QR is an important factor involved in the toxicodynamics of HQ in these myeloid cells.
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PMID:Characterization of quinone reductase, glutathione and glutathione S-transferase in human myeloid cell lines: induction by 1,2-dithiole-3-thione and effects on hydroquinone-induced cytotoxicity. 751 Dec

Recombinant proteins containing amino acid sequences from open reading frame (ORF) 2 and ORF3 of a Chinese strain of hepatitis E virus (HEV) were constructed as fusions with glutathione S-transferase (GST). Stable fusion proteins were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the proteins were transferred to nitrocellulose membranes, and the immobilized proteins were probed with sera from hepatitis E patients from various regions or from rhesus monkeys (Macaca mulatta) experimentally infected with the Chinese strain of HEV. Immunoglobulin G-class antibodies were detected with chemiluminescence and anti-human immunoglobulin G conjugated to horseradish peroxidase. Anti-ORF3 antibodies were detected in most patients and monkeys within 17 days of exposure, but this humoral response declined with time and was usually undetectable by approximately 100 days. Anti-ORF2.1 antibody was usually detected as early as anti-ORF3 but persisted in all animals and many patients, whereas reactivity to the larger GST-ORF2.2 fusion protein was more transient, even though all sequences present in GST-ORF2.1 are present in GST-ORF2.2. Rechallenge of these monkeys with HEV suggested that immunity to reinfection was incomplete, as levels of anti-ORF2.1 (but not anti-ORF2.2) were boosted after each rechallenge. The results demonstrate that the carboxy-terminal region of HEV ORF2 contains epitopes which are recognized by convalescent-phase antibody and are likely to be associated with limited immunity to infection, but these epitopes may be masked when larger portions of ORF2 are expressed as recombinant proteins.
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PMID:Persistent and transient antibody responses to hepatitis E virus detected by western immunoblot using open reading frame 2 and 3 and glutathione S-transferase fusion proteins. 752 46

In a retrospective study the expression of the resistance proteins P-170 glycoprotein (P-170), glutathione S-transferase pi (GST-pi), thymidylate-synthase (TS), dihydrofolate reductase (DHFR) and metallothionein (MT) was investigated in 111 patients with newly diagnosed acute lymphoblastic leukemia (ALL) using the streptavidin-biotin-peroxidase complex method. The expression of the resistance proteins was found in following frequency: P-170 in 39 (35%), GST-pi in 54 (49%), TS in 46 (42%), DHFR in 21 (20%) and MT in 30 (33%) cases of the investigated patients. Patients with overexpression of P-170 or GST-pi had a significant lower probability of remaining in continuous first remission (P < 0.05 for P-170 and P < 0.01 for GST-pi). The expression of TS and DHFR had no prognostic significance on the probability of first remission. Patients with MT-overexpression showed only a tendency for a lower probability of continuous first remission. Coexpression of P-170 and GST-pi was observed in leukemias of 22 patients (21%) and 38 patients (37%) showed no evidence for the expression of both markers. Combining P-170 and GST-pi improved the prognostic value. The expression of the resistance proteins was independent of age, sex, FAB-type, immunological subtype and of the initial peripheral blast cell count. The multivariate analysis indicated that only the expression of P-170 was an independent unfavorable prognostic factor for children with initial ALL. The reason for this was an minor correlation of P-170 and GST-pi (P = 0.01).
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PMID:[Expression and clinical significance of resistance proteins in initial acute lymphatic leukemia (ALL) in childhood]. 756 59

Southern armyworm, Spodoptera eridania, larvae were provided ad libitum 0.002-0.25% w/w dichlone, 2,3-dichloro-1,4-naphthoquinone (CNQ). Larval mortality occurred in a time-and-dose dependent manner, with an LC17 of 0.01% and an LC50 of 0.26% CNQ at day-5. Extracts of larvae fed control, 0.01, and 0.25% CNQ diets for 5 days were assayed for antioxidant enzymes. While 0.01% CNQ had a mild effect, 0.25% CNQ profoundly increased levels of all antioxidant enzymes that were examined. The increases as compared to control were: 5.3-, 1.9-, 3.2-, 2.6-, 2.8-, and 3.5-fold higher for superoxide dismutase, catalase, glutathione transferase and its peroxidase activity, glutathione reductase and DT-diaphorase, respectively. At 0.01% CNQ, the thiobarbituric acid reactive substances (TBARS) were similar to the control group. However, despite the induction from 0.25% CNQ of all enzymes examined, the lipid peroxidation was not attenuated; the TBARS were 29.7% over the control value. High mortalities and CNQ-induced pathologies reflected in retarded growth, wasting syndrome, and diuresis clearly indicated that the insect sustained severe oxidant-induced injuries before appropriate defenses were fully mobilized. Thus, this quinone causes an oxidative stress in a model insect species analogous to that observed in mammalian species.
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PMID:Dichlone-induced oxidative stress in a model insect species, Spodoptera eridania. 757 83


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