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)

Glutathione transferase, glyoxalase I and glyoxalase II activities were not evenly distributed among the major helminth groups. Intestinal cestodes and digeneans had higher glutathione transferase activity than parasitic nematodes. High glyoxalase II activity was found in cestodes and digeneans but no glyoxalase I was detectable. Glyoxalase I and II were both detected in nematodes. These results are discussed in relation to the enzymes' suggested role in protection against secondary lipid peroxidation products.
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PMID:Relative distribution of glutathione transferase, glyoxalase I and glyoxalase II in helminths. 233 83

Hypobaric hypoxia at 0.45 atm induced a reversible increase of mouse liver glyoxalase I. The levels of this enzyme increased after an exposure of 20 h and 20 + 20 h, whereas the activity decreased to the control values after 20 h at room pressure. Before the treatment, some animals received tritiated leucine (i.p.). Glyoxalase I was purified to homogeneity. The pure enzyme from the treated animals showed 20-times more radioactivity than the controls. Thus, the increase in specific activity is due to new protein synthesized in response to the treatment at 0.45 atm. The activities of glyoxalase II and glutathione S-transferase were not affected by the treatment.
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PMID:Induction of mouse liver glyoxalase I by hypobaric hypoxia. 236 8

A very potent competitive inhibitor of mammalian glyoxalase II activity, N,S-bis-fluorenylmethoxycarbonylglutathione (DiFMOC-G) has been synthesized and characterized. The Ki value for inhibition of glyoxalase II purified from calf liver is 0.08 microM. The Ki values for glyoxalase I inhibitions range from 285 to 500 fold higher than the values obtained for glyoxalase II inhibitions, depending on the source of the enzyme. Among other enzymes involved in glutathione metabolism, such as glutathione S-transferase, glutathione reductase, and glutathione peroxidase, only glutathione S-transferase is inhibited to a small extent by DiFMOC-G. Diesters of DiFMOC-G were prepared in order to improve transport of DiFMOC-G into mammalian tumor cells (rat adrenal pheochromocytoma, PC-12) in culture. Among the diesters synthesized, diisopropyl DiFMOC-G was found to be the most inhibitory to cell viability, with a [I]0.5 value of 3 microM.
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PMID:N,S-bis-fluorenylmethoxycarbonylglutathione: a new, very potent inhibitor of mammalian glyoxalase II. 762 27

A clone encoding glyoxalase II has been isolated from a human adult liver cDNA library. The sequence of 1011 base pairs consists of a full-length coding region of 780 base pairs, corresponding to a protein with a calculated molecular mass of 28,861 daltons. Identities (50-60%) were found to partial 5' and 3' cDNA sequences from Arabidopsis thaliana as well as within a limited region of glutathione transferase I cDNA from corn. A vector was constructed for heterologous expression of glyoxalase II in Escherichia coli. For optimal yield of enzyme, silent random mutations were introduced in the 5' coding region of the cDNA. A yield of 25 mg of glyoxalase II per liter of culture medium was obtained after affinity purification with immobilized glutathione. The recombinant enzyme had full catalytic activity and kinetic parameters indistinguishable from those of the native enzyme purified from human erythrocytes.
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PMID:Molecular cloning, heterologous expression, and characterization of human glyoxalase II. 855 May 79

Inhibitors having high specificity toward mammalian glyoxalase II, but not glyoxalase I, were sought as part of a program to study glyoxalase enzyme function in mammalian cells. The compound, S-fluorenylmethoxycarbonyl glutathione (FMOC-G), was synthesized and found to be a competitive inhibitor of purified calf liver glyoxalase II (Ki = 2.1 mumol/l). Inhibition constants (Ki values) for the other glyoxalase enzyme, glyoxalase I, and the glutathione-requiring enzyme, glutathione S-transferase, from other sources, were found to be 17 and 25 mumol/l, respectively. FMOC-G is a very poor inhibitor of glutathione reductase and glutathione peroxidase. Diesters (dimethyl, diethyl, diisopropyl) of FMCO-G were also synthesized, as proinhibitors, to improve transport of FMOC-G into mammalian tumor cells (rat adrenal pheochromocytoma, PC-12) in culture. The diesters were inhibitory to cell growth and variability; the most effective of these, diisopropyl FMOC-G, exhibited an [I]0.5 value of approximately 275 mumol/l. Diesters of FMOC-G may be useful in studies of the glyoxalase enzyme system in cultured mammalian cells.
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PMID:S-fluorenylmethoxycarbonyl glutathione and diesters: inhibition of mammalian glyoxalase II. 858 3

Levels of aldose reductase, glyoxalase I, and glyoxalase II in mononuclear and polymorphonuclear cells from insulin-dependent diabetes mellitus (IDDM) patients with long term diabetic complications were compared to levels in IDDM patients without complications and to those in nondiabetic controls. Cells were isolated from 22 asymptomatic long term IDDM patients, 22 symptomatic IDDM patients, and 16 controls, using a double gradient centrifugation procedure. Aldose reductase was determined by Western blots using polyclonal antiserum to human aldose reductase purified from skeletal muscle. Glyoxalase I and glyoxalase II were determined spectrophotometrically. Aldose reductase in mononuclear cells from symptomatic IDDM patients is significantly elevated compared to that in asymptomatic IDDM patients (mean +/- SEM, 0.96 +/- 0.20 vs. 0.46 +/- 0.08 microgram/mg protein; P < 0.02). Aldose reductase was not detected in polymorphonuclear cells. Glyoxalase I in mononuclear and polymorphonuclear cells from symptomatic IDDM patients is significantly elevated compared to that in controls [mean for mononuclear cells, 0.46 +/- 0.03 vs. 0.37 +/- 0.03 mumol/min.mg (P < 0.05); mean for polymorphonuclear cells, 0.16 +/- 0.01 vs. 0.10 +/- 0.01 mumol/min.mg (P < 0.002)]. Glyoxalase II is significantly elevated only in polymorphonuclear cells from symptomatic IDDM patients compared to controls (mean, 0.13 +/- 0.01 vs. 0.063 +/- 0.016 mumol/min.mg; P < 0.005). Glutathione peroxidase and glutathione S-transferase were not significantly different in these populations. Aldose reductase, glyoxalase I, and glyoxalase II are involved in the metabolism of methylglyoxal, suggesting that methylglyoxal may play a role in the etiology of diabetic complications.
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PMID:Increased levels of methylglyoxal-metabolizing enzymes in mononuclear and polymorphonuclear cells from insulin-dependent diabetic patients with diabetic complications: aldose reductase, glyoxalase I, and glyoxalase II--a clinical research center study. 863 55

A seasonal variability of trace metal concentrations and antioxidant enzymes was observed in gills and digestive gland of the Mediterranean mussel Mytilus galloprovincialis from both a polluted and a nonpolluted population. Trace metals (As, Cu, Fe, Mn, Pb, and Zn) exhibited, in both organs, maximum values in later winter-early spring followed by a progressive decrease during the summer. While in the gills this behavior probably reflects a different bioavailability of metals, in the digestive gland it is influenced mainly by the progressive infiltration of the organ by gonadic tissues during gametogenesis. Metals, as other pollutants, are known to influence the oxidative status of these organisms and antioxidant enzymes have been often proposed as biomarkers of exposure to contaminants. In this respect, it was of interest to compare the variations of these biochemical parameters with those of metal levels in two mussel populations from a polluted and a nonpolluted site, respectively. The biochemical parameters examined included the level of glutathione and the activity of the following glutathione dependent and antioxidant enzymes: glyoxalase I, EC 4.4.1.5; glyoxalase II, EC3.1.2.6; glutathione S-transferases, EC 2.5.1.18; glutathione reductase, EC 1.6.4.2; Se-dependent, EC 1.11.1.9 and Se-independent, EC 2.5.1.18 glutathione peroxidases; catalase, EC 1. 11.1.6; superoxide dismutase, EC 1.15.1.1. Seasonal variations of trace metals did not appear to influence those of biochemical parameters, which generally showed an opposite trend with higher enzymatic activities in summer when trace metal concentrations were lower. The effects of metals on antioxidant enzymes were more evident when the two mussel populations were compared. In particular, organisms from the polluted site showed lower levels of glutathione and higher enzymatic activities of glyoxalase I even though the magnitude of these differences was not constant during the year. Moreover, native mussels from both the polluted and control populations exhibited limited differences in the activities of glutathione reductase, glutathione peroxidases, catalase, and superoxide dismutase, suggesting the possibility of some biochemical adaptation in organisms from chronically polluted environments.
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PMID:Trace metals and antioxidant enzymes in gills and digestive gland of the Mediterranean mussel Mytilus galloprovincialis. 941 73

In the framework of an INTAS project, arctic populations of the clam Macoma balthica were collected from seven stations (Mezen, Khaypudyr, Pechora 3, Pechora 5, Dvina, Keret 1, and Keret 2) in the White Sea and Pechora Sea. The main objectives of this research were to define baseline concentrations of trace metals (As, Cd, Cr, Cu, Fe, Mn, Pb, Zn) in M. balthica and to evaluate antioxidant responses as biomarkers of anthropogenic stress in these organisms. The antioxidant parameters examined included the levels of glutathione and the activities of several glutathione-dependent and antioxidant enzymes: glyoxalase I and glyoxalase II (EC 4.4.1.5 and EC 3.1.2.6), glutathione S-transferases (EC 2.5.1.18), glutathione reductase (EC 1.6.4.2), glutathione peroxidases (EC1.11.1.9 and EC 2.5.1.18, respectively, for Se-dependent and Se-independent forms), superoxide dismutase (SOD, EC 1.15.1.1), and catalase (EC 1.11.1.6). Organisms revealed enhanced concentrations of lead in both Keret stations, Khaypudyr, and Mezen, and high levels of copper in Keret and cadmium in Khaypudyr. At the biochemical level, organisms from Pechora 3, Pechora 5, and Dvina were not statistically different, whereas those from Mezen and Khaypudyr exhibited higher activities of superoxide dismutase, glutathione peroxidase, and glyoxalase II. Catalase levels were lower in Mezen and Khaypudyr. More heterogeneous were the responses of glyoxalase I and glutathione S-transferases, while no significant differences among the stations were observed for glutathione reductase. Multiple regression analyses revealed significant positive relationships between the main antioxidant enzymes (glutathione peroxidases, superoxide dismutase, glyoxalase I, and glyoxalase II), and confirmed the exception of catalase, which, when significant, was negatively correlated with the other parameters. The results support the suitability of antioxidant responses as biomarkers of pollutant exposure and/or toxicity for arctic biomonitoring programs even though only moderately polluted sites were sampled.
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PMID:Trace metals and variations of antioxidant enzymes in Arctic bivalve populations. 977 77

gamma-L-Glutamyl-S-(benzyl)-L-cysteinyl-R-(-)-phenylglycine (TER 117) has previously been developed for selective inhibition of human glutathione S-transferase P1-1 (GST P1-1) based on the postulated contribution of this isoenzyme to the development of drug resistance in cancer cells. In the present investigation, the inhibitory effect of TER 117 on the human glyoxalase system was studied. Although designed as an inhibitor specific for GST P1-1, TER 117 also competitively inhibits glyoxalase I (K(I) = 0.56 microM). In contrast, no inhibition of glyoxalase II was detected. Reduced glyoxalase activity is expected to raise intracellular levels of toxic 2-oxoaldehydes otherwise eliminated by glyoxalase I. The resulting toxicity would accompany the potentiation of cytostatic drugs, caused by inhibition of the detoxication effected by GST P1-1. TER 117 was designed for efficient inhibition of the most abundant form GST P1-1/Ile105. Therefore, the inhibitory effect of TER 117 on a second allelic variant GST P1-1/Val105 was also studied. TER 117 was shown to competitively inhibit both GST P1-1 variants. The apparent K(I) values at glutathione concentrations relevant to the intracellular milieu were in the micromolar range for both enzyme forms. Extrapolation to free enzyme produced K(I) values of approximately 0.1 microM for both isoenzymes, reflecting the high affinity of GST P1-1 for the inhibitor. Thus, the allelic variation in position 105 of GST P1-1 does not affect the inhibitory potency of TER 117. The inhibitory effects of TER 117 on GST P1-1 and glyoxalase I activities may act in synergy in the cell and improve the effectiveness of chemotherapy.
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PMID:The human glutathione transferase P1-1 specific inhibitor TER 117 designed for overcoming cytostatic-drug resistance is also a strong inhibitor of glyoxalase I. 1069 4

To gain insight into the biochemical mechanisms of organotin toxicity, the effects of oral subchronic exposure (70 d) to triphenyltin acetate (TPTA) on hepatic and renal enzymes involved in glutathione metabolism were investigated in rabbits and lambs. Rabbits were offered a diet fortified with 15, 75 or 150 ppm TPTA, whereas lambs were daily given 1 or 7.5 mg/kg TPTA On the whole, rabbits were more susceptible than lambs and in both species hepatic enzymes were affected to a greater extent than renal enzymes. In rabbit liver, glutathione S-transferase activity toward 1,2-dichloro-4-nitrobenzene (DCNB) was enhanced at 15 ppm and depressed at 150 ppm TPTA, whereas selenium-dependent glutathione peroxidase (Se-GPX) decreased in a dose-related manner; glyoxalase II (GII) activity increased to the same extent at 15 or 75 ppm TPTA but was unaffected at 150 ppm TPTA. For renal enzyme activities in rabbits, only GPX activity was significantly inhibited at 150 ppm TPTA. The only statistically significant changes in lambs were a fall in both hepatic GST accepting DCNB as substrate at 7.5 mg/kg and Se-GPX at 1 or 7.5 mg/kg TPTA, and an increase in renal GII activity at 7.5 mg/kg TPTA. These results suggest that depression of important antioxidant enzymes such as GST and GPX are part of the complex mechanism of organotin toxicity.
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PMID:Changes in hepatic and renal glutathione-dependent enzyme activities in rabbits and lambs subchronically treated with triphenyltin acetate. 1083 20


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