Effect of dietary phenobarbital, 3,4-benzo(α)pyrene and 3-methyl-cholanthrene on hepatic, intestinal and renal glutathione S-transferase activities in the rat

Clifton, Gil; Kaplowitz, Neil

doi:10.1016/0006-2952(78)90465-3

Cited by 61 publications

(6 citation statements)

References 18 publications

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“…In this study the activity levels of GST and the GSH-mediated peroxidases, were increased significantly in both brain and testis on exposure to PB and MC in multiple doses. This result accords with earlier reports that GST levels were induced in liver, small intestine and kidney by intraperitoneal administration of Polynuclear Aromatic Hydrocarbons (PAH) and PB (Clifton and Kaplowitz, 1978). Therefore the induction of GST serves to overcome the deleterious effects caused by PB and MC.…”

Section: Disscussionsupporting

confidence: 82%

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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Section: Disscussionsupporting

confidence: 82%

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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“…hypoxic) condition of reference site fish following the transport of these fish to the laboratory; later samples were transported in oxygenated rather than aerated containers and arrived in better condition. Although intestinal glutathione S-transferases are known to be sensitive to dietary pollutants including polycyclic aromatic hydrocarbons (Clifton & Kaplowitz 1978), results from the present study indicate that intestinal glutathione S-transferase activity may not be a sensitive indicator of pollution exposure in the field. Under controlled laboratory conditions we routinely observe an approximate 2-fold increase in glutathione S-transferase activity in fish intestines following administration of PAH contaminated diets.…”

Section: Resultsmentioning

confidence: 52%

“…In mammals, the activity of these enzymes in several organs is sensitive to dietary inducing agents such as polycyclic aromatic hydrocarbons (PAH) and phenobarbital (Clifton & Kaplowitz 1978). In laboratory studies with fish, we have observed enhanced activity of hepatic and intesti- ).…”

Section: Introductionmentioning

confidence: 77%

Intestinal glutathione S-transferase activity in flounder Platichthys flesus collected from contaminated and reference sites

Veld¹,

Lee²

1988

Mar. Ecol. Prog. Ser.

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Intestinal glutathione S-transferase activities were measured during the GEEP Workshop in flounder Platichthys flesus collected from Langesundfjord, Norway. Though enzyme activities were generally higher in fish collected from 3 polluted sites by comparison with a reference site, the only significant differences in activities between the 3 sites ran counter to the anticipated pollution gradient. The results suggest that intestinal glutathione S-transferase activity may not be a sensitive indicator of pollution exposure under field conditions.

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“…Induction of specific forms of GSH transferase and of associated activities has been demonstrated following treatment of mammals with various xenobiotics including polycyclic aromatic hydrocarbons (PAH) (Ding and Pickett 1985;Hammock and Ota 1983;Clifton and Kaplowitz 1978). In addition, certain forms are expressed at high levels in preneoplastic and neoplastic mammalian tissues (Kitahara et at.…”

Section: )+ Multiple Forms Of Gsh Transferase Arise Frommentioning

confidence: 99%

Glutathione S-transferase in intestine, liver and hepatic lesions of mummichog (Fundulus heteroclitus) from a creosote-contaminated environment

et al. 1991

Fish Physiol Biochem

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Cytosolic glutathione S-transferase (GSH transferase) activity towards 1-chloro-2,4-dinitrobenzene (CDNB) was elevated approximately three to four-fold in intestine and liver of mummichog (Fundulus heteroclitus) collected from a creosote-contaminated site in the Elizabeth River, Virginia. Intestinal GSH transferase activity at the most heavily contaminated site, at a moderately contaminated site and at a relatively clean site averaged 3.64, 2.83 and 1.11µmoles/min/mg respectively, while values for liver at these sites averaged 2.84, 1.75 and 0.93µmoles/min/mg. In addition, densitometric tracings of sodium dodecylsulfate-polyacrylamide gels of intestine and liver cytosol revealed a similar trend in the staining intensity of a 25.8 kD protein band, which lies within the molecular weight range of GSH transferase subunits. Activity in putative preneoplastic and neoplastic hepatic lesions of fish collected from the creosote-contaminated site was not significantly different from that of adjacent normal tissue. In the laboratory, dietary betanaphthoflavone (ßNF) treatment resulted in a three-fold increase in intestinal GSH transferase. Hepatic GSH transferase activity in the same fish was not affected by dietary ßNF although hepatic monooxygenase activity, measured as ethoxyresorufin O-deethylase (EROD), was. The results of this study indicate a response of the intestinal detoxification system to environmental contaminants and supports previous studies on the importance of intestinal metabolism of foreign compounds. Further, our results indicate the trend towards elevated GSH transferase in liver of feral fish could not be attributed to a cancerous disease state in these fish but indicates chemical induction in this organ as well.

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Effect of dietary phenobarbital, 3,4-benzo(α)pyrene and 3-methyl-cholanthrene on hepatic, intestinal and renal glutathione S-transferase activities in the rat

Cited by 61 publications

References 18 publications

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

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

Intestinal glutathione S-transferase activity in flounder Platichthys flesus collected from contaminated and reference sites

Glutathione S-transferase in intestine, liver and hepatic lesions of mummichog (Fundulus heteroclitus) from a creosote-contaminated environment

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