Differential induction of glutathione transferase isoenzymes of mice stomach by diallyl sulfide, a naturally occurring anticarcinogen

Maurya, Akhilendra Kumar; Singh, S.V.

doi:10.1016/0304-3835(91)90205-v

Cited by 46 publications

(17 citation statements)

References 22 publications

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“…This reciprocal behavior suggests that after a certain threshold value for GST activity saturation with fluorodifen, other GST isoenzymes are activated linearly in the cytosol to protect cells from damage due to accumulation of reactive substances under stress conditions. The observed strong stimulation of microsomal and cytosolic GST activities with CDNB and fluorodifen in EH5 by STS is consistent with the activation of microsomal and cytosolic GST activities in biofilms (Table 3) by various stress factors (see above), sulfhydryl reagents (37), sulforaphane (12,29), and diallyl sulfide (34). However, the low toxicity of STS, the high sensitivity of induction of GST by STS (Fig.…”

Section: Discussionsupporting

confidence: 85%

“…Most of our knowledge of the function of GSTs has come from studies of animals and plants, and there have been relatively few studies of microbes (34,40,50). The resultant glutathione conjugates are less toxic and more polar than the parent compounds and can be stored in vacuoles or excreted from the biological system, helping the organism regain normal cellular functions and reducing the cellular toxicity of reactive parent or organic intermediates.…”

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confidence: 99%

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Induction of Glutathione S -Transferase in Biofilms and Germinating Spores of Mucor hiemalis Strain EH5 from Cold Sulfidic Spring Waters

Hoque

Pflugmacher

Fritscher

et al. 2007

Appl Environ Microbiol

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The occurrence and activation of glutathione S-transferase (GST) and the GST activities in biofilms in cold sulfidic spring waters were compared to the occurrence and activation of GST and the GST activities of the aquatic fungal strains EH5 and EH7 of Mucor hiemalis isolated for the first time from such waters. Using fluorescently labeled polyclonal anti-GST antibodies and GST activity measurements, we demonstrated that a high level of GST occurred in situ in natural biofilms and pure cultures of strain EH5. Measurement of microsomal and cytosolic soluble GST activities using different xenobiotic substrates, including 1-chloro-2,4-dinitrobenzene (CDNB), 1,2-dichloro-4-nitrobenzene, 1,2-epoxy-3-(4-nitrophenoxy)propane, 1-iodo-2,4-dinitrobenzene, and fluorodifen, showed that the overall biotransforming abilities of biofilms were at least sixfold greater than that of strain EH5 alone. Increasing the level of sodium thiosulfate (STS) in the medium stimulated the microsomal and cytosolic GST activities with CDNB of strain EH5 about 44-and 94-fold, respectively, compared to the activities in the control. The induction of microsomal GST activity with fluorodifen by STS was strongly linear, but the initial strong linear increase in cytosolic GST activity with fluorodifen showed saturation-like effects at STS concentrations higher than approximately 1 mM. Using laser scanning confocal and conventional fluorescence microscopy, abundant fluorescently labeled GST proteins were identified in germinating sporangiospores of strain EH5 after activation by STS. High-performance size exclusion chromatography and sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed the presence of at least two main GSTs (ϳ27.8-and ϳ25.6-kDa subunits) in the cytosol of EH5, whereas the major 27.8-kDa subunit was the only GST in microsomes. We suggest that differential cellular GST expression takes place in strain EH5 depending on spore and hyphal development. Our results may contribute to our understanding of induction of GST by sulfurous compounds, as well as to the immunofluorescence visualization of GST in aquatic fungus and fungus-bacterium biofilms.The glutathione S-transferases (GSTs) (EC 2.5.1.18) are a family of multifunctional cytosolic (38) and membrane-associated microsomal (10, 36) proteins that can catalyze the conjugation of many electrophilic endogenous and xenobiotic compounds to glutathione. Most of our knowledge of the function of GSTs has come from studies of animals and plants, and there have been relatively few studies of microbes (34,40,50). The resultant glutathione conjugates are less toxic and more polar than the parent compounds and can be stored in vacuoles or excreted from the biological system, helping the organism regain normal cellular functions and reducing the cellular toxicity of reactive parent or organic intermediates. The existence of a variety of different GST isoenzymes suggests that there is a wide range of substrate specificity (17). GSTs are grouped into seven distinct classes, including the ...

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Section: Discussionsupporting

confidence: 85%

mentioning

confidence: 99%

Induction of Glutathione S -Transferase in Biofilms and Germinating Spores of Mucor hiemalis Strain EH5 from Cold Sulfidic Spring Waters

Hoque

Pflugmacher

Fritscher

et al. 2007

Appl Environ Microbiol

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“…[23][24][25] In the study by Boeing et shown to inhibit mutagenesis, initiation, and promotion al., 27 onion consumption was no longer significantly assobut also to induce enzymes important in the detoxificaciated with a lower stomach cancer risk after additional tion of carcinogens. 8, 51,52 However, because the evidence adjustment for vegetables and fruit.…”

Section: / M4433f0014mentioning

confidence: 99%

Consumption of onions and a reduced risk of stomach carcinoma

Dorant¹,

Brandt²,

Goldbohm³

et al. 1996

Gastroenterology

199

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“…Induction of phase II detoxification enzymes by DAS (2,19,20), could limit the mutagenicity of a wide range of carcinogens by stimulating conjugation and excretion of reactive intermediates. In the present study, formation of urinary metabolites from NMBzA was not significantly altered by an acute dose of DAS administered either 3 or 18 h earlier.…”

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Modulation of N-nitrosomethylbenzylamine bioactivation by diallyl sulfide in vivo

et al. 1992

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Diallyl sulfide (DAS*), a major flavour and fragrance component of garlic oil (1), has been shown to be an effective inhibitor of tumorigenesis by diverse metabolically activated chemical carcinogens <2-5). In the most striking example of chemoprevention, Wargovich and co-workers reported (4) that pretreatment with DAS completely prevented the formation in rat oesophagus of both malignant and premalignant lesions by /V-nitrosomethylbenzylamine (NMBzA), an exceptionally potent and selective oesophageal carcinogen in this species (6). After preadministration of DAS, a significant reduction has been observed in nuclear aberrations induced by NMBzA and dimethylhydrazine (4,7) but not in the nucleotoxicity of the direct-acting methylating•Abbreviations: DAS, diallyl sulfide; NMBzA, N-nitrosomethylbenzylamine; O^-MEdG, C^-methyldeoxyguanosine, 7-MEdG, 7-methyldeoxyguanosine.© Oxford University Press carcinogens /V-nitrosomethylurea and /V-methyl-/V'-nitro-/Vnitrosoguanidine (7). Studies in vitro have shown that DAS also is an inhibitor of oxidative metabolism by cytochrome P450 enzymes of a number of carcinogenic nitrosamines, including NMBzA, /V-nitrosodimethylamine, /V-nitrosodiethylamine and 4-(A'-memyl-A^-nirjosarnino)-l-(3-pyridyl)-l-butanone (4,(8)(9)(10). These findings suggested that DAS may block nitrosamineinduced tumorigenesis by inhibiting nitrosamine bioactivation in situ. In the present investigation, we have examined this possibility by assessing the effects of DAS on the overall metabolism of NMBzA and on DNA methylation by NMBzA in vivo.In the protocol developed by Wargovich and co-workers (4), rats received five weekly treatments consisting of an i.g. dose of 200 mg/kg of DAS followed 3 h later by a s.c. injection of 3.5 mg/kg of NMBzA. However, in vitro demethylation of NMBzA was significantly lower by hepatic microsomes prepared 18 h after a similar dose of DAS than by microsomes collected 3 h post-treatment (8). In order to determine whether there is a similar difference in vivo between immediate and delayed effects of DAS on overall NMBzA metabolism, we monitored the formation of 14 CO 2 and radioactive urinary metabolites from [methyll4

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Differential induction of glutathione transferase isoenzymes of mice stomach by diallyl sulfide, a naturally occurring anticarcinogen

Cited by 46 publications

References 22 publications

Induction of Glutathione S -Transferase in Biofilms and Germinating Spores of Mucor hiemalis Strain EH5 from Cold Sulfidic Spring Waters

Induction of Glutathione S -Transferase in Biofilms and Germinating Spores of Mucor hiemalis Strain EH5 from Cold Sulfidic Spring Waters

Consumption of onions and a reduced risk of stomach carcinoma

Modulation of N-nitrosomethylbenzylamine bioactivation by diallyl sulfide in vivo

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