Glutathione transferases in rat lung: the presence of transferase 7-7, highly efficient in the conjugation of glutathione with the carcinogenic (+)-7β,8α-dihydroxy-9α,10α-oxy-7,8,9,10-tetrahydrobenzo[a]pyrene

Robertson, Ian; Jensson, Helgi; Mannervik, Bengt; Jernström, Bengt

doi:10.1093/carcin/7.2.295

Cited by 120 publications

(53 citation statements)

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“…The doublereciprocal plots were also linear for each GST isoenzyme when the concentration of GSH was varied (plots not shown). This is in contrast to the results obtained with purified rat liver GST isoenzymes where a nonlinear relationship was observed (14,15). The V max value for forestomach GST 9.5 was about 7-159-fold higher as compared with other GST isoenzymes.…”

Section: Table I Kinetic Parameters For Mouse Gst Isoenzymes With (ϩ)contrasting

confidence: 95%

“…The results of the present study indicate that the kinetic properties of the pi class GST isoenzymes of rat (rGSTP1-1; Ref. 15), human (hGSTP1-1, Ref. 16), and mouse (present study) in the conjugation of GSH with anti-BPDE are different.…”

Section: Table I Kinetic Parameters For Mouse Gst Isoenzymes With (ϩ)mentioning

confidence: 53%

“…The activity of rGSTP1-1 toward (Ϫ)-enantiomer of anti-BPDE has not been investigated. Finally, the rGSTP1-1, but not hGSTP1-1 or mGSTP1-1, shows a biphasic kinetics with GSH as the variable substrate (15).…”

Section: Table I Kinetic Parameters For Mouse Gst Isoenzymes With (ϩ)mentioning

confidence: 90%

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An Alpha Class Mouse Glutathione S-Transferase with Exceptional Catalytic Efficiency in the Conjugation of Glutathione with 7β,8α-Dihydroxy-9α,10α-oxy-7,8,9,10-tetrahydrobenzo(a)pyrene

Srivastava

Xia

et al. 1996

Journal of Biological Chemistry

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The kinetics of the conjugation of glutathione (GSH) with anti-7␤,8␣-dihydroxy-9␣,10␣-oxy-7,8,9,10-tetrahydrobenzo(a)pyrene (anti-BPDE) catalyzed by GSH S-transferase (GST) isoenzymes purified from the liver and forestomach of female A/J mouse has been investigated. The GST isoenzymes studied included an alpha class isoenzyme of forestomach (GST 9.5), alpha class hepatic isoenzymes mGSTA3-3 and mGSTA4-4, pi class hepatic isoenzyme mGSTP1-1, and mu class hepatic isoenzyme mGSTM1-1. When the concentration of (؉)-anti-BPDE was varied (5-120 M) at a fixed GSH concentration (2 mM), linear Lineweaver-Burk plots were observed for each isoenzyme. The k cat values for GST 9.5, mGSTA3-3, mGSTP1-1, mGSTM1-1, and mGSTA4-4 were 2.0, 0.02, 0.40, 0.05, and 0.01 s ؊1, respectively, with corresponding K m values of 16, 12, 29, 27, and 49 M. The catalytic efficiency (k cat /K m ) of GST 9.5 in the conjugation of GSH with (؉)-anti-BPDE, which is believed to be the ultimate carcinogenic metabolite of benzo(a)pyrene, was about 9 -625-fold higher as compared with other mouse GST isoenzymes. These results indicate that GST 9.5 of forestomach is different among mammalian alpha class GSTs because (؉)-anti-BPDE has been shown to be a poor substrate for alpha class rat or human GST isoenzymes. The catalytic efficiency of GST 9.5 was approximately 4.5-fold higher than that of pi class human isoenzyme (hGSTP1-1), which among human GSTs is reported to be most efficient in the detoxification of (؉)-anti-BPDE. Unlike rat GST isoenzymes, linear LineweaverBurk plots were observed for mouse GSTs when GSH was used as a variable substrate. The catalytic efficiencies of the mouse GSTs toward (؉)-anti-BPDE were about 2-20-fold higher as compared with the (؊)-enantiomer of anti-BPDE. The results of the present study suggest that GST 9.5 may play an important role in the detoxification of (؉)-anti-BPDE.

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Section: Table I Kinetic Parameters For Mouse Gst Isoenzymes With (ϩ)contrasting

confidence: 95%

Section: Table I Kinetic Parameters For Mouse Gst Isoenzymes With (ϩ)mentioning

confidence: 53%

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An Alpha Class Mouse Glutathione S-Transferase with Exceptional Catalytic Efficiency in the Conjugation of Glutathione with 7β,8α-Dihydroxy-9α,10α-oxy-7,8,9,10-tetrahydrobenzo(a)pyrene

Srivastava

Xia

et al. 1996

Journal of Biological Chemistry

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“…It is possible that GST Yp would be helpful in the detoxification of carcinogens because of its ability to catalyze conjugation reactions for carcinogens or peroxides [33][34][35] . Se-enriched JRS inhibited 80% of rat mammary carcinogenesis induced by 7,12-dimethylbenz[a]anthracene at a Se dose of 8.8 ppm in the diet 21) .…”

Section: Discussionmentioning

confidence: 99%

Selenium‐enriched Japanese Radish Sprouts Influence Glutathione Peroxidase and Glutathione S‐Transferase in an Organ‐specific Manner in Rats

Hama

Yamanoshita

Chiba

et al. 2008

Journal of Occupational Health

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Selenium-enriched Japanese Radish Sprouts Influence Glutathione Peroxidase and Glutathione S-Transferase in an Organ-specific Manner in Rats: Hidetoshi HAMA, et al. Department of Preventive Medicine, Shinshu University School of Medicine-Selenium-enriched Japanese radish s p r o u t s ( S e -e n r i c h e d J R S ) , i n w h i c h S emethylselenocysteine accounted for 80% of Se compounds, inhibited mammary tumorigenesis induced by 7,12-dimethylbenz[a]anthracene in rats. The effects of Se-enriched JRS on the oxidative stress-scavenging enzymes were investigated in rats. F344 female rats were fed test diets, in which Se-enriched JRS was added at 0, 2.4, 5.0, 8.8 or 12.5 ppm Se to commercial rodent chow for 3 wk. Glutathione peroxidase (GPx) and glutathione S-transferase (GST) in rat livers, kidneys and lungs were measured. Tissue Se concentrations at the highest Se dose (12.5 ppm) were high in order as follows: kidney > liver > lung. The diet at 12.5 ppm Se reduced the increase in body weight and, conversely, increased the liver weight. The Se test diets decreased hepatic and renal GPx activity at more than 2.4 ppm and 5.0 ppm, respectively. In contrast, the test diets increased pulmonary GPx activity at more than 2.4 ppm Se. The diets increased hepatic GST activity at more than 2.4 ppm Se dose dependently, whereas they reduced pulmonary GST activity at more than 2.4 ppm. The diet of 12.5 ppm Se induced GST Yp in all 3 organs and GST Yb1 in the liver. Thus, Se-enriched JRS influenced GPx and GST activity in a symmetrical manner in the livers and lungs of rats, with hepatic GST possibly affected, in part, by the induction of GST Yb1. (J Occup Health 2008; 50: 147-154)

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“…GSTT1 is involved in the biotransformation of a subset of low molecular weight toxins such as methyl-halogenids or ethylene oxide pyrene. 8 GSTP1, which is active against many polycyclic aromatic hydrocarbon (PAH) epoxides 9 such as (ϩ)anti-BPDE 10,11 or 5 methylchrysene, 12 is overexpressed in numerous human cancerous lesions 13,14 including head and neck cancers. 15 Genetic polymorphisms for GSTM1, GSTT1 and more recently allelic variants for GSTP1 have been found in human populations.…”

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confidence: 99%

Glutathione-associated enzymes in head and neck squamous cell carcinoma and response to cisplatin-based neoadjuvant chemotherapy

et al. 2001

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Glutathione S-transferases (GSTs) are metabolic phase II enzymes that promote reactive metabolite elimination by conjugating them to glutathione (GSH). Because of their important role in xenobiotic metabolism and detoxification, they have been implicated in carcinogenesis processes, especially epithelium transformation. Moreover, their influence on response to chemotherapy in cancer patients has been demonstrated. Genetic polymorphisms for GSTM1, GSTT1 and GSTP1 have been found in human populations and have been shown to have phenotypic consequences. To investigate the role of GST enzymes in carcinogenesis and in response to chemotherapy in patients with head and neck squamous cell carcinoma (HNSCC), GSTP1, GSTM1 and GSTT1 were studied prospectively in a large series of HNSCC patients. Correlations between GST alterations, p53 mutation status and clinical response to chemotherapy were investigated. We showed that the risk of developing laryngeal cancer was increased by 2.6-fold [95% CI 1.6 -6.1] in patients with the GSTM1 null genotype and by 2.8-fold [95% CI 0.9 -8.1] in patients with the homozygous GSTP1 val105 genotype. Furthermore, individuals with this latter genotype were overrepresented in the p53 mutation group (p ‫؍‬ 0.05). After storage duration and hemolysis adjustement, a significantly lower plasmatic GSTP1 level was observed in complete responders compared with partial and non-responders (mean: 4.4 ؎ 0.06 g/l, 4.7 ؎ 0.06 g/l and 4.7 ؎ 0.07 g/l; p ‫؍‬ 0.05), respectively. The prevalence of p53-mutated tumors was significantly higher in the group of non-responders (81%) compared with partial (60%) and complete responders (64%) (p ‫؍‬ 0.05). Two types of multivariate analysis were performed including parameters that have been shown to influence response to chemotherapy significantly in univariate analysis. p53 mutations and high tumor stage are independent factors of non-response to chemotherapy, whereas plasmatic GSTP1 levels and low tumor stage are independent factors of complete response. Our data suggest that GST enzymes are associated with larynx cancer and that their use as predictive factors and treatment targets should be further explored. Head and neck squamous cell carcinoma (HNSCC) is the sixth most common solid tumor worldwide, accounting for about 2% of all neoplasms in the western world. 1 This type of cancer appears to be mainly related to smoking and alcohol consumption. 2,3 Many of the chemical compounds contained in tobacco smoke are oxidized by phase I enzymes, such as cytochrome CYP450, into reactive metabolites, which can then be conjugated by phase II enzymes into reductive compounds and eliminated. 4,5 If they are not efficiently eliminated, reactive metabolites can form DNA adducts that, as demonstrated for p53 initiate mutations in genes implicated in tumor initiation or progression. 6 Glutathione S-transferases (GSTs) are phase II metabolic enzymes that conjugate reactive metabolites to glutathione (GSH) and lead to their elimination. Normal human tissues express 4 different s...

show abstract

Glutathione transferases in rat lung: the presence of transferase 7-7, highly efficient in the conjugation of glutathione with the carcinogenic (+)-7β,8α-dihydroxy-9α,10α-oxy-7,8,9,10-tetrahydrobenzo[a]pyrene

Cited by 120 publications

References 0 publications

An Alpha Class Mouse Glutathione S-Transferase with Exceptional Catalytic Efficiency in the Conjugation of Glutathione with 7β,8α-Dihydroxy-9α,10α-oxy-7,8,9,10-tetrahydrobenzo(a)pyrene

An Alpha Class Mouse Glutathione S-Transferase with Exceptional Catalytic Efficiency in the Conjugation of Glutathione with 7β,8α-Dihydroxy-9α,10α-oxy-7,8,9,10-tetrahydrobenzo(a)pyrene

Selenium‐enriched Japanese Radish Sprouts Influence Glutathione Peroxidase and Glutathione S‐Transferase in an Organ‐specific Manner in Rats

Glutathione-associated enzymes in head and neck squamous cell carcinoma and response to cisplatin-based neoadjuvant chemotherapy

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