Drug induction of hepatic glutathione S-transferases in male and female rats

Kaplowitz, Neil; Kuhlekamp, J; Clifton, Gil

doi:10.1042/bj1460351

Cited by 154 publications

(32 citation statements)

References 26 publications

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“…Treating rats with phenobarbital caused an 80% increase in GST activity measured with aralkyl substrates but only a 30% increase in GST activity measured with epoxides as substrates (17). As compared to phenobarbital, treatment with 3-methylcholanthrene caused a smaller increase in GST activity with aralkyl substrates but an equivalent induction of GST activity with epoxides as substrates ( 17). In recent studies, it has been found that different xenobiotics cause differential induction of GST isozymes in rat liver (13,21,22).…”

Section: Discussionmentioning

confidence: 99%

“…2-4) may be analogous to the effect of various xenobiotics on GST isozymes in mammalian tissues. Administering xenobiotics such as phenobarbital and 3-methylcholanthrene to rats induces GST isozymes in the cytosol of rat liver (17). Recent studies have demonstrated that the induction is due to the ability of the xenobiotics to activate transcription of genes coding for the subunits of GST (5).…”

Section: Discussionmentioning

confidence: 99%

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Induction of Glutathione S-Transferase Isozymes in Sorghum by Herbicide Antidotes

Dean

Gronwald²,

Eberlein³

1990

Plant Physiol.

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Certain chemicals referred to as herbicide antidotes protect sorghum from injury by chloroacetanilide herbicides such as metolachlor. The effect of herbicide antidotes on the glutathione S-transferase isozyme complement of etiolated sorghum (Sorghum bicolor [L.] Moench) shoots was examined. Elution profiles of glutathione S-transferase isozymes from untreated and antidote-treated seedlings were generated by fast protein liquid chromatography utilizing an anion exchange (Mono Q) column. In untreated seedlings, there were two glutathione Stransferase isozymes, a major isozyme which exhibited activity toward 1-chloro-2,4-dinitrobenzene and a minor isozyme which exhibited activity toward metolachlor. Treating sorghum seedlings with various antidotes (flurazole, oxabetrinil, CGA-133205, naphthalic anhydride, dichlormid) resulted in the appearance of four to five additional glutathione S-transferase isozymes (depending on the particular antidote) which exhibited activity toward metolachlor as a substrate and little or no activity with 1-chloro-2,4-dinitrobenzene. Treating etiolated sorghum shoots with metolachlor was also found to induce at least four isozymes which exhibited activity toward the herbicide. An increase in glutathione S-transferase activity, measured with metolachlor as substrate, was detected within 4 h after treatment with 30 micromolar oxabetrinil, but 36 hours were required for maximum expression of activity. Addition of either the transcription inhibitor cordycepin or the translation inhibitor cycloheximide inhibited the appearance of glutathione S-transferase activity measured with metolachlor as substrate. The results are consistent with the hypothesis that antidotes confer protection against metolachlor injury in sorghum by inducing the de novo synthesis of glutathione Stransferase isozymes which catalyze the detoxification of the herbicide.Herbicide antidotes are chemical compounds used to protect certain grasses, in particular corn and sorghum, from injury by selected herbicides (4,14). Antidotes that provide varying degrees of protection to sorghum against injury by chloroacetanilide herbicides such as metolachlor or alachlor 'Cooperative investigation of the Minnesota Agricultural Experiment Station and the U.S.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Induction of Glutathione S-Transferase Isozymes in Sorghum by Herbicide Antidotes

Dean

Gronwald²,

Eberlein³

1990

Plant Physiol.

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“…It is well-known that treatment with phenobarbital, polychlorinated biphenyls or 3-methylcholanthrene enhances the acti vity of enzymes , such as glucuronyl transferase and glutathione-Sstransferase, involved in phase 2 reactions (5,24,60,64). However, neither food deprivation nor restricted carbohydrate intake nor ethanol consumption produced any significant effect on the activity of these enzymes (50).…”

Section: Phenobarbital As a Clue To The Underlying Mechanism Of The Dmentioning

confidence: 94%

Pharmacokinetics of organic solvent vapors in relation to their toxicity.

Sato¹,

Nakajima²

1987

Scand J Work Environ Health

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SATO A, NAKAJIMA T. Pharmacokinetics of organic solvent vapors in relation to their toxicit y. Scand J Work Environ Health 13 (1987) 81-93 . The volatility and Iipophilicity by which organi c solvents are distinct from other chemicals constitut e a characteristic pharmacokinetic feature . They enter a living body by inhalation, preferentially distribute in the adipose tissue, and are eliminated by both expirat ion and metabolic degradation. Th is review article is centered on experiment al studies conducted by the authors and their co-workers, and it deals with (i) pharmacokinetic principl es, (ii) partition coefficients in relation to toxicity, (iii) significance of metabolism in the developmen t of organic solvent toxicity, and (iv) environmental factors that alt er the metabolism and toxicity of solvents.

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“…This type of combination of subunits in GST may occur due to the exchange of gene product at the level of transcription and translation and may offer protection from various xenobiotics (Kaplowitz et al, 1975) and even with slightly modified xenobiotics. Gene conversion may be an important mechanism for generating sequence diversity in the GST multigene family.…”

Section: Disscussionmentioning

confidence: 99%

Comparative study on glutathione transferases of rat brain and testis under the stress of phenobarbitol and β-methylcholanthrene

Thyagaraju¹,

Hemavathi²,

Vasundhara³

et al. 2005

J. Zhejiang Univ. Sci.

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Abstract:A comparative study was made on the tissue specific expression of glutathione transferases (GST) in brain and testis after exposure of rat to phenobarbitol (PB) and β-methylcholanthrene (MC). Glutathione transferases, a family of multifunctional proteins are involved in intracellular transport processes and in detoxication of electrophilic xenobiotics by catalyzing reactions such as conjugation, isomerization, reduction and thiolysis. On purification, the yield of GST proteins by affinity chromatography was 39% in testis and 32% in brain. The affinity purified testis GSTs were resolved by chromatofocusing into six anionic and four cationic isozymes, and in brain glutathione transferases were resolved into four anionic and three cationic isozymes, suggesting the presence of multiple isozymes with Yc, Yb, Yβ and Yδ in both of them. In testis and brain, these isozymes at identical pI values showed variable functions with a battery of substrates and the cationic isozymes of brain and testis showed identical properties in CHP (cumene hydroperoxide) at pH values of above 7.0. Substrate specificity studies and immunoblot analysis of testis and brain proteins revealed that they play a predominant role in the detoxication of phenobarbitol or β-methylcholanthrene. Expression of the isozymes in testis and brain on exposure to PB and MC indicated elevated subunit variation. In both testis and brain, Yδ of π class was expressed on PB treatment and Yc of α class and Yβ of µ class was expressed in MC treated testis and only Yc was predominantly expressed in MC treated brain. Thus these subunits expression is considered as markers for carcinogenesis and specific to chemical toxicity under phenobarbitol and β-methylcholanthrene stress.

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Drug induction of hepatic glutathione S-transferases in male and female rats

Cited by 154 publications

References 26 publications

Induction of Glutathione S-Transferase Isozymes in Sorghum by Herbicide Antidotes

Induction of Glutathione S-Transferase Isozymes in Sorghum by Herbicide Antidotes

Pharmacokinetics of organic solvent vapors in relation to their toxicity.

Comparative study on glutathione transferases of rat brain and testis under the stress of phenobarbitol and β-methylcholanthrene

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