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PubMedDate not supplied

Papaverine, an opium alkaloid influences hepatic and pulmonary glutathione S-transferase activity and glutathione content in rats.

The present study evaluates the effect of oral administration of papaverine at differential dosing regimens (100 mg/kg bw and 200 mg/kg bw) on the hepatic and pulmonary glutathione S-transferase (GST) activity and glutathione content (GSH) in male Wistar rats. Papaverine treatment caused a pronounced increase in GST activity and GSH content at the higher dosing level in the rat liver and lung. We conclude that papaverine, can possibly act as a chemopreventive agent against chemical carcinogenesis.

Animals↗
PubMed1994

Effects of clofibric and beclobric acid in rat and monkey hepatocyte primary culture: influence on peroxisomal and mitochondrial beta-oxidation and the activity of catalase, glutathione S-transferase and glutathione peroxidase.

The effect of hypolipidaemic compounds on peroxisomal fatty acid beta-oxidation and on peroxisome morphology in the liver differs widely between rodent and primate species. We studied the relative importance of peroxisomal and mitochondrial beta-oxidation of palmitate in primary cultures of hepatocytes isolated from rat and monkey liver in the absence or presence of clofibric acid or beclobric acid. It was demonstrated that it is possible to differentiate between peroxisomal and mitochondrial beta-oxidation activities in intact cells. Overall beta-oxidation of palmitate was ca. 30% higher in rat hepatocytes than in monkey liver cells. In both monkey and rat cell cultures the mitochondrial component was over 90% of the total palmitate beta-oxidation. In rat hepatocyte culture clofibric acid and beclobric acid caused a 5- to 8-fold stimulation of peroxisomal beta-oxidation, while in monkey cells this activity was not significantly increased. However, in cells derived from both species mitochondrial palmitate beta-oxidation was increased (rat 2.5-fold; monkey 1.5-fold). These results indicate that the species differences in the increase in peroxisomal fatty acid oxidation are not a result of an inability to metabolize fatty acids in rat liver cell mitochondria. A comparison of the activity of enzymes involved in the detoxification of hydrogen peroxide showed that catalase and glutathione-S-transferase activity is 2.9-fold higher in monkey hepatocytes than in rat liver cells, while glutathione peroxidase activity was 1.6-fold higher in rat cells.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed2000

Effects of chronic dietary cadmium on hepatic glutathione levels and glutathione peroxidase activity in starlings (Sturnus vulgaris).

The effects of chronic exposure to dietary cadmium on the levels of hepatic glutathione (GSH) and on the activity of the glutathione peroxidase enzymes (GSH-Px) were studied for the first time in starlings (Sturnus vulgaris). Thirty-three individuals (17 females and 16 males) were divided into three groups: One represented the untreated control and two were respectively fed with diets containing 10 and 50 ppm cadmium chloride (CdCl(2)). The total duration of treatment was 22 weeks. The three groups respectively accumulated mean hepatic Cd residues of 2.29, 75.71, and 208.49 ppm. Hepatic GSH increased in the treated groups respectively 24% and 52% in comparison to controls. Total GSH-Px activity in the liver was inhibited in the group fed with 50 ppm, due to inhibition of the selenium-dependent fraction of the enzyme, while the selenium-independent fraction did not change significantly. During the treatment, after 14 weeks of exposure to cadmium, the 50 ppm-treated group showed a 47% decrease of the activity of the selenium-dependent GSH-Px and a 50% increase of the somatic liver index in comparison with controls.

Animals↗
PubMed1996

Glutathione S-transferase and glutathione peroxidase are essential in the early stage of adriamycin resistance before P-glycoprotein overexpression in HOB1 lymphoma cells.

We have previously established Adriamycin-resistant HOB1 cell lines showing the multidrug resistance (MDR) phenotype. For further study, we analyzed the free-radical scavengers glutathione S-transferase (GST) and glutathione peroxidase (GPX) by enzyme assays and Northern blots. Three cell lines, HOB1/ADR0.1, HOB1/ADR1.0, and HOB1/ADR5.0, represented HOB1 cells resistant to 0.1, 1.0, and 5.0 microM Adriamycin, respectively. The mdr1 transcript was overexpressed in HOB1/ADR0.1 cells, and the amount of its expression reached a maximum between HOB1/ADR1.0 and HOB1/ADR5.0 cell lines. The increases in GST activity and GST-pi expression were observed only in high-level-resistant cell line (HOB1/ADR1.0 and HOB1/ADR5.0), which also showed increased GPX activity and expression. For investigation of the cytotoxic effect of Adriamycin on HOB1 cells prior to the mdr1 overexpression, an appropriate number of parental HOB1 cells were treated with 0.1 microM Adriamycin for 7 days, and the viable cells (HOB1/ADR) were isolated and subjected to analyses for mdr1, GST-pi, and GPX expression and for GST and GPX activity. In comparison with HOB1/ADR0.1 cells, HOB1/ADR cells did not show mdr1 overexpression but had significant increases in the activity and expression of GST and GPX. The current study suggests that in the early phase of Adriamycin treatment, GST and GPX are more important than P-glycoprotein for the development in HOB1 cells of resistance against Adriamycin.

ATP Binding Cassette Transporter, Subfamily B, Mem↗
PubMed2005

Genotype, enzyme activity, glutathione level, and clinical phenotype in patients with glutathione synthetase deficiency.

Glutathione synthetase (GS) deficiency is a rare autosomal recessive disorder. The clinical phenotype varies widely, and nearly 30 different mutations in the GSS gene have been identified. In the present study, genotype, enzyme activity, metabolite levels and clinical phenotype were evaluated in 41 patients from 33 families. From some of the patients, data on glutathione (GSH) levels and gamma-glutamylcysteine levels in cultured fibroblasts were also available. Twenty-seven different mutations were found: 14 missense, 9 splice, 2 deletions, 1 insertion and 1 nonsense mutation. Twenty-three patients were homozygous and 18 were compound heterozygous. The moderate and severe clinical phenotypes could not be distinguished based on enzyme activity, GSH or gamma-glutamylcysteine levels in cultured fibroblasts. However, in fibroblasts, the residual GS activity was correlated with the GSH level. All mutations causing frameshifts, premature stop codons or aberrant splicing were associated with moderate or severe clinical phenotypes including haemolytic anaemia, 5-oxoprolinuria, and (in several forms) neurodevelopmental signs. The data indicate that additional genetic or environmental factors modify at least the moderate and severe phenotypes and that the clinical classification given to the patients may be influenced by variation in follow-up. The type of mutation involved can, to some extent, predict a mild versus a more severe phenotype.

Cells, Cultured↗
PubMed2006

Identification of a glutathione S-transferase without affinity for glutathione sepharose in human kidney.

To identify kidney glutathione S-transferase (GST) isoenzyme, which does not bind to glutathione affinity column, biochemical characterization was performed by using an array of substrates and by measuring sensitivity to inhibitors. Immunological characterization was done by immunoblotting. Affinity flow-through GST exhibited activity towards 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole and cumene hydroperoxide, typical class alpha substrates and high sensitivity towards hematin, an alpha class inhibitor. It cross-reacted with antibodies against alpha class GST. Affinity flow-through GST in human kidney is an alpha class member.

Chemical Phenomena↗
PubMed1992

Roles of glutathione and glutathione peroxidase in the protection against endothelial cell injury induced by 15-hydroperoxyeicosatetraenoic acid.

We investigated the role of the glutathione redox cycle in endothelial cell injury induced by 15(S)-hydroperoxyeicosatetraenoic acid (15-HPETE), an arachidonate lipoxygenase product. Pretreatment of endothelial monolayers with reduced glutathione (GSH) markedly suppressed 15-HPETE-induced cellular injury, which was determined by the 51Cr-release assay. 15-HPETE-induced cytotoxicity was modified by several GSH-modulating agents such as buthionine sulfoximine and 2-oxothiazolidine-4-carboxylate, indicating that this cyto-protective action of GSH was correlated with the intracellular GSH level. These GSH-modulating agents also modified the conversion of 15-HPETE to 15(S)-hydroxyeicosatetraenoic acid by endothelial cells. On the other hand, the exposure of endothelial cell monolayers to 15-HPETE did not deplete intracellular GSH levels but decreased GSH peroxidase activity. In addition, sodium selenite and ebselen, a stimulator and mimic of GSH peroxidase activity, respectively, displayed remarkable protective effects against 15-HPETE-induced cytotoxicity. These results suggest that intracellular GSH plays a pivotal role in the protection against 15-HPETE-induced endothelial cell injury, and that the decreased activity of GSH peroxidase activity is involved in 15-HPETE-induced cytotoxicity.

Animals↗
PubMed1980

The glutathione peroxidase activity of glutathione S-transferases.

Glutatione transferases (RX:glutathione R-transferases, EC 2.5.1.18) B and AA were purified from rat liver to investigate the mechanism for their apparent GSH peroxidase activity (GSSG formation). Both transferases catalyze an overall reaction in which loss of cumene hydroperoxide is accompanied by a stoichiometric increase in GSSG. Inclusion of cysteamine, a thiol, results in a reduction of GSSG formation but has no effect on hydroperoxide loss. Cysteamine does not inhibit the transferase-catalyzed conjugation of GSH and 1-chloro-2,4-dinitrobenzene. Peroxidase reactions carried out in the presence of cyanide, another nucleophile, also result in a reduction of GSSG formation without altering the rate of cumene hydroperoxide loss; cyanide does not inhibit transferase activity with 1-chloro-2,4-dinitrobenzene. Both cysteamine and cyanide are capable of blocking GSSG formation in the non-enzymic oxidation of GSH by hydrogen peroxide without blocking H2O2 loss. These results are consistent with a mechanism for GSH transferases in which nucleophilic attack by GS- on hydroperoxide results in a reactive intermediate, presumably the sulfenic acid of glutathione, GSOH. GSH + ROOH in equilibrium GSHO + ROH (1) This sulfenic acid then reacts non-enzymically with GSH to produce GSSG. GSOH + GSH in equilibrium GSSG + H2O (2) The summing of Reactions 1 and 2 explains the observed stoichiometry. Cysteamine and cyanide can compete with GSH for the sulfenic acid in Reaction 2, thus reducing GSSG formation. Thios.

Animals↗
PubMed1985

Enantioselectivity in glutathione conjugation of 1,2-epoxy-1,2,3,4-tetrahydronaphthalene by hepatic glutathione S-transferase.

Enantiomers of 1,2-epoxy-1,2,3,4-tetrahydronaphthalene (ETN) were conjugated with glutathione (GSH) specifically at their benzylic oxiran carbons, with a marked difference in rate [(1R,2S)-(+)- less than (1S,2R)-(-)-ETNs] as well as in affinity for GSH S-transferase [Km: (1S,2R)-(-)- less than (1R, 2S)-(+)-ETNs], in rat liver cytosol to yield two diastereomeric S-(2-hydroxy-1,2,3,4-tetrahydronaphth-1-yl)glutathiones which were separable by reverse partition hplc. Enzymatic GSH conjugation of racemic ETN occurred preferentially with the (1S,2R)-(-)-component as a result of its retarding effect on the conjugation of the (1R,2S)-(+)-counterpart, one half of which remained in enantiomerically pure form in the incubation medium when the (1S,2R)-(-)-component had been completely conjugated.

Animals↗
PubMed1987

Conjugation of model substrates or microsomally-activated aflatoxin B1 with reduced glutathione, catalysed by cytosolic glutathione-S-transferases in livers of rats, mice and guinea pigs.

Glutathione-S-transferase (GST) activity has been examined in liver cytosol fractions from guinea pigs, mice, control fed rats or rats with pre-neoplastic nodular liver lesions. The levels of activity in unfractionated cytosols have been assayed using the model substrates 1-chloro-2,4-dinitrobenzene (CDNB), 3,4-dichloronitrobenzene (DCNB) and monobromobimane (mBrB) with reduced glutathione (GSH). The order of activities in the various liver fractions using CDNB as substrate were: mouse greater than pre-neoplastic nodular rat greater than guinea pig greater than control rat and paralleled the capacities of the cytosols to catalyse the formation of aflatoxin B1-GSH from microsomally-activated aflatoxin B1 (AFB1) and GSH. Quantitative differences between the activities of the cytosols using the three model substrates were observed. In the mouse fractionation of GST activity by isoelectric focusing (I.E.F.) on preparative granular gels showed that the most basic component (isoelectric point pH 9.4) with the highest conjugating activity with respect to microsomally-activated AFB1 did not correspond with the peak of most activity for conjugating CDNB. In the pre-neoplastic nodular rat liver the CDNB conjugating activities of all fractions separated on granular I.E.F. gels, were higher than the corresponding fractions isolated from control rat liver, with particular enhancement of the peak containing the 3:3 isoenzyme. In contrast to control rat liver the 7:7 isoenzyme was detected in pre-neoplastic nodular liver preparations. These isoenzymes (3:3 and 7:7) did not contribute significantly to the enhanced level of AFB1-GSH formation catalysed by cytosol fractions prepared from pre-neoplastic nodular rat liver. The microsomally-activated AFB1-conjugating activity of unfractionated rat liver cytosols was increased to a relatively greater extent than CDNB conjugating activity during the induction of pre-neoplastic nodular liver lesions, and the elevated level of the activated AFB1-conjugating activity was found to be associated with the most basic fraction (isoelectric point pH 9.0). Analytical isoelectric focusing gels using mBrB as substrate demonstrated the presence of a basic GST isoenzyme in the pre-neoplastic nodular rat liver, not detected in preparations from the livers of control rats. The low level of activated AFB1-conjugating activity present in unfractionated guinea-pig cytosol was found to correspond with the fraction containing the peak of CDNB conjugating activity on preparative isoelectric focusing (isoelectric point pH 7.5). The lack of correlation between the conjugation of model substrates and the conjugation of xenobiotics could be of import

Aflatoxin B1↗
PubMed1988

The Meisenheimer complex of glutathione and trinitrobenzene. A potent inhibitor of the glutathione S-transferase from Galleria mellonella.

1. The Meisenheimer complex formed between reduced glutathione and 1,3,5-trinitrobenzene is characterised by an extinction coefficient at 470 nm of 20400 and by an association constant at pH 9.18 of 42 l.mol-1. 2. Trinitrobenzene is a moderately good inhibitor of the glutathione S-transferase from larvae of the moth Galleria mellonella. It acts by competition with the electrophilic substrate. At pH 7.4, it has a Ki value of 10 microM. Its mode of inhibition with respect to GSH appears to be non-competitive. 3. At pH values below 9.0, the Meisenheimer complex does not appear to be formed in sufficient quantity to give significant inhibition of the enzyme. At pH 9.0 and at GSH concentrations greater than 1 mM, the inhibition of the enzyme became markedly non-hyperbolic. This was attributed to the inhibitory action of the Meisenheimer complex. The complex appears to act also by competition with the electrophilic substrate and its Ki is calculated to be 1.7 X 10(-7) M.

Animals↗
PubMed1992

Correlation between trans-stilbene oxide-glutathione conjugation activity and the deletion mutation in the glutathione S-transferase class mu gene detected by polymerase chain reaction.

Glutathione S-transferase (GST) class Mu activity was determined in 145 unrelated hospital patients in Berlin by measuring their conjugation activity towards the specific substrate trans-stilbene oxide (TSO) with two substrate concentrations (50 and 250 microM) in homogenates prepared from lymphocytes. Eighty individuals (55.2%) had an activity lower than 10 pmol/min/10(6) lymphocytes and were classified as GST class Mu deficient. In 142 of 145 cases, phenotype was confirmed by the results of a genotyping procedure using the polymerase chain reaction technique. Two fragments of 273 and about 650 bp including one and two introns, respectively, could always be amplified from genomic DNA in individuals with high GST class Mu activity and could not be amplified in persons with impaired glutathione-TSO conjugation activity. This indicates that persons with low activity carry a large deletion mutation within the GST class Mu gene. The enzymatically determined antimode between low and high activity determined as 10 pmol/min/1 million lymphocytes in the assay with 50 microM TSO could be clearly confirmed by genotyping.

Adult↗
PubMed1993

Interindividual differences in the in vitro conjugation of methylene chloride with glutathione by cytosolic glutathione S-transferase in 22 human liver samples.

The interindividual variation in the in vitro conjugation of methylene chloride with glutathione by cytosolic glutathione S-transferase (GST) was investigated with 22 human liver samples. In three of the samples no activity towards methylene chloride was observed. Eleven samples showed an activity ranging from 0.20 to 0.41 (0.31 +/- 0.08) nmol/min/mg protein, and eight samples an activity of 0.82-1.23 (1.03 +/- 0.14) nmol/min/mg protein. The activities towards 1-chloro-2,4-dinitrobenzene (CDNB) of these three groups were 1.17 +/- 0.25, 1.12 +/- 0.35 and 1.20 +/- 0.53 mumol/min/mg protein, respectively. In nine of the liver samples, the alpha-, mu- and pi-class GST subunits were quantified. In two of these samples, no activity was observed towards methylene chloride, while alpha-, mu- and pi-class subunits were expressed in these human liver cytosolic samples. As the highest activity towards methylene chloride was still 1.4 times lower than the activity in rat cytosol, the existence of the three populations seems to be of little importance for human risk assessment.

Cytosol↗
PubMed1995

A glutathione depletion selectively imposed on mu glutathione S-transferase overproducing cells increases nitrogen mustard toxicity.

Glutathione (GSH) contributes to the detoxification of anticancer drugs through the operation of specific glutathione S-transferases (GST) and innate, or acquired, overexpression of this enzyme family has been frequently observed in tumor cell lines. In the GMA32 line of Chinese hamster fibroblasts, we showed that GSH starvation produced by exposing cells to buthionine sulfoximine (BSO) increased the toxicity of chlorambucil and melphalan, but not that of N,N'-bis(2-chloroethyl)-N-nitrosourea (BCNU), cisplatine and doxorubicin. This indicates that efficient mechanisms of detoxification using GSH operate for chlorambucil and melphalan, but not for the other drugs in these cells. We then showed that GSH depletion could be selectively and transiently induced in the mu GST overexpressing cell line derived from GMA32, HC474, by exposing cells to substrates specific to the overexpressed isozyme. Exposing cells to such a substrate, trans-stilbene oxide, does not alter the sensibility of GMA32 cells to melphalan and chlorambucil, but increases that of HC474 cells to these drugs, to an extent comparable to that obtained with BSO. This observation highlights the possibility of exploiting GST overexpression, a frequent feature of tumor cells, to selectively sensitize these undesirable cells to anticancer drugs.

Animals↗
PubMed1994

Status of glutathione and glutathione-metabolizing enzymes in menadione-resistant human cancer cells.

Cloned menadione (MD)-resistant human breast cancer cell lines have been developed and characterized with respect to glutathione (GSH) content and GSH-metabolizing enzymes. Increases in the activities of gamma-glutamyltranspeptidase and glutathione-S-transferase were demonstrated in the absence of alterations in the GSH content of two cloned MD-resistant cell lines. The MD-resistant cells also displayed alterations in their growth kinetics, possessing longer doubling times and increased fractions in the G1/O phase of the cell cycle as compared to parental MD-sensitive cells. The possible mechanisms for the resistance to MD, including an increase in repair of MD-induced DNA damage, are discussed.

Cell Cycle↗
PubMed1994

Role of cellular glutathione and glutathione S-transferase in the expression of alkylating agent cytotoxicity in human breast cancer cells.

Glutathione (GSH) and glutathione S-transferases (GSTs) play an important role in the protection of cells against toxic effects of many electrophilic drugs and chemicals. Modulation of cellular GSH and/or GST activity levels provides a potentially useful approach to sensitizing tumor cells to electrophilic anti-cancer drugs. In this study, we describe the interactions of four representative alkylating agents (AAs), melphalan, 4-hydroperoxy-cyclophosphamide (4HC), an an activated form of cyclophosphamide, 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU), and cisplatin, with GSH and GST in the human breast cancer cell line MCF-7. Depletion of cellular GSH pools by approximately 80% by treatment of the cells with the GSH synthesis inhibitor buthionine sulfoximine (BSO) sensitized the tumor cells to each AA to a different extent, with dose-modifying factors of 2.39, 2.21, 1.64, and 1.27 observed for melphalan, 4HC, cisplatin, and BCNU, respectively. Treatment of the cells with the GST inhibitor ethacrynic acid (EA) failed to show any significant effects on the cytotoxicity of these AAs. However, EA did potentiate the cytotoxicity of melphalan when given in combination with BSO, an effect that may be due to a more complete depletion of cellular GSH levels by the combined modulator treatment. Following a 1-hr exposure to cytotoxic-equivalent concentrations of these AAs, GSH levels decreased substantially in the case of 4HC and BCNU, but increased by 30-50% in the case of cisplatin and melphalan. BSO pretreatment largely blocked this effect of cisplatin and melphalan on cellular GSH, while it further enhanced the GSH-depleting activity of both 4HC and BCNU. On the basis of these results, it is concluded that (a) GSH affects the cytotoxicity of different AAs to different extents, (b) basal GST expression in MCF-7 cells does not play a major role in AA metabolism, (c) EA can potentiate the enhancing effect of BSO on melphalan cytotoxicity in MCF-7 cells, and (d) depletion of cellular GSH by pretreatment with BCNU or cyclophosphamide may correspond to a useful strategy for enhancing the anti-tumor activity of other AAs given in a sequential combination.

Alkylating Agents↗
PubMed1996

Glutathione and glutathione S-transferase in benign and malignant prostate cell lines and prostate tissues.

Metastatic prostate adenocarcinoma is unresponsive to alkylator chemotherapy with virtually no prolonged remissions. Glutathione (GSH) and glutathione S-transferase (GST) have been reported to play a role in tumor resistance to alkylator therapy; however, there are no baseline studies that have investigated and compared GSH and GST in human prostate cell lines and tissues. Thus, we determined the GSH content and GST activity in benign prostate, in primary and metastatic prostate adenocarcinoma tissues, in immortal adenocarcinoma cell lines, and in primary cell cultures derived from both benign prostate and primary prostatic carcinoma tissue. The GSH content was higher in the immortal cell lines than in the fresh tissues and primary cultures. Conversely, the GST activity was significantly higher in the tissues and primary cultures than in the cell lines. The GSH content and GST activity of the primary cultured prostatic cells were similar to those of the prostate tissues. The differences between the immortal prostate cancer cell lines and prostate tissue are of sufficient magnitude to suggest that in vitro results with cell lines may not extrapolate to prostate cancer in vivo. The GSH content and GST activity in a prostate specific antigen-secreting human prostate tumor xenograft, LuCaP23, maintained in nude mice were similar to those of human prostate tissue and primary cultures. Both the xenograft and primary cultures from patients with prostate cancer may be more appropriate models than established cell lines for investigating techniques to increase the effectiveness of alkylators in prostate cancer.

Adenocarcinoma↗
PubMed1980

Formation of 3-(glutathion-S-YL)-N-methyl-4-aminoazobenzene and inhibition of aminoazo dye-nucleic acid binding in vitro by reaction of glutathione with metabolically-generated N-methyl-4-aminoazobenzene-N-sulfate.

The reaction of glutathione (GSH) with metabolically-formed N-methyl-4-aminoazobenzene-N-sulfate (MAB-N-sulfate), a presumed ultimate carcinogenic metabolite of N,N-dimethyl-4-aminoazobenzene (DAB), was investigated using a hepatic sulfotransferase incubation mixture containing GSH and the proximate carcinogen, N-hydroxy-N-methyl-4-aminoazobenzene (N-HO-MAB). Under these conditions, 6--16% of the MAB-N-sulfate formed could be trapped as an aminoazo dye-GSH adduct. Upon subsequent purification, the adduct was shown to be chromatographically and spectrally identical to 3-(glutathion-S-yl)-N-methyl-4-aminoazobenzene (3-GS-MAB), a known biliary metabolite of DAB and a product of the reaction of the synthetic ultimate carcinogen, N-benzoyloxy-N-methyl-4-aminoazobenzene(N-BzO-MAB), with GSH. Neither 2'- nor 4'-GS-MAB, both products of the latter reaction, were detected in the sulfotransferase incubation mixture. GSH-S-transferases did not appear to be involved in the reaction of MAB-N-sulfate of N-BzO-MAB with GSH. The addition of triethyltin, a potent GSH-S-transferase inhibitor, had no effect on the yield of 3-GS-MAB in (N-HO-MAB sulfotransferase)-GSH incubations; and the addition of cytosol or purified GSH transferases A and B to a (N-BzO-MAB)-GSH reaction mixture did not increase the amount of 3-GS-MAB formed.

Animals↗