Induction of cytochromes P450 1A, 2B and 2E in hamster tissues by acetone

Chen, Ruei Ming; Ueng, Tzuu‐Huei

doi:10.1007/s002040050417

Cited by 12 publications

(2 citation statements)

References 28 publications

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“…Although these studies suggest a role for CYP2E1 in the -1-hydroxylation of fatty acids, many of the inducers used have been shown to induce multiple P450 isoforms. Acetone has been reported to induce multiple P450 isoforms, including 1A, 2B, and 2E (Chen and Ueng, 1997). Similarly, pyridine has been shown to induce 1A1 (Iba et al, 2002) and 2B1/2B2 (Kim et al, 1993), as well as CYP2E1.…”

Section: Poloyac Et Almentioning

confidence: 99%

The Effect of Isoniazid on Cyp2e1- And Cyp4a-Mediated Hydroxylation of Arachidonic Acid in the Rat Liver and Kidney

Poloyac¹,

Tortorici²,

Przychodzin³

et al. 2004

Drug Metab Dispos

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ABSTRACT:Cytochrome P450 (P450) bioactivation of arachidonic acid to hydroxyeicosatetraenoic acids (HETEs) has been reported to be isoform-and tissue-specific. To determine whether altered P450 expression affects the production of these metabolites, the formation of HETEs after isoniazid-mediated CYP2E1 induction was evaluated in the rat liver and kidney. Male Sprague-Dawley rats received isoniazid (200 mg/kg) or saline intraperitoneally once daily for 5 days. Chlorzoxazone, lauric acid, and arachidonic acid hydroxylation was measured in liver and kidney microsomes with and without preincubation with the specific CYP2E1 inhibitor, trans-1,2-dichloroethylene (DCE). P450 isoform content and tissue HETE metabolite concentrations were also determined. Isoniazid increased CYP2E1 protein, and the 6-hydroxychlorzoxazone formation rate was increased by 2.7 ؎ 0.3-and 2.2 ؎ 0.5-fold in liver and kidney, respectively. Formation of 19-HETE and 11-hydroxylauric acid was induced 2.3 ؎ 0.6-fold and 2.2 ؎ 0.4-fold in the liver, respectively, with no difference in the kidney. All of the induced activities were attenuated by DCE. An unanticipated decrease in liver CYP4A expression and in vitro 20-HETE formation rate was observed after isoniazid administration. Isoniazid decreased liver and kidney 20-HETE content to 34 ؎ 10% and 15.6 ؎ 5.3% of control, respectively, without significantly altering tissue 19-HETE concentration. Based on these findings, we conclude that under induced conditions, CYP2E1 is a primary enzyme involved in liver, but not kidney, formation of 19-HETE. In addition, formation of both CYP4A and 20-HETE is reduced in the liver by isoniazid. It was also demonstrated that tissue concentrations parallel in vitro inhibited formation rates for 20-HETE, but not the induced 19-HETE formation in the liver.

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Section: Poloyac Et Almentioning

confidence: 99%

The Effect of Isoniazid on Cyp2e1- And Cyp4a-Mediated Hydroxylation of Arachidonic Acid in the Rat Liver and Kidney

Poloyac¹,

Tortorici²,

Przychodzin³

et al. 2004

Drug Metab Dispos

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show abstract

“…The cytochrome P-450 1B1-specific blotting antibody kit and cell microsomes containing recombinant human cytochrome P-450 1B1 were purchased from Gentest Corporation, Woburn, MA. Intensities of the immunoreactive bands were determined using an IS-1000 digital imaging system (Alpha Innotech Corporation, San Leandro, CA) as described previously (Chen & Ueng, 1997).…”

Section: Gel Electrophoresis and Immunoblottingmentioning

confidence: 99%

Induction of Cytochromes P-450 1A1 and 1B1 by Motorcycle Exhaust Particulate In Human Breast Cancer MCF-7 Cells

Wang

Chen

Ueng

2002

Journal of Toxicology and Environmental Health, Part A

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The effects of motorcycle exhaust particulate (MEP) on cytochrome P-450-dependent monooxygenases were determined using MCF-7 human breast cancer cells treated with organic extracts of MEP. Treatment with MEP extract produced concentration- and time-dependent increases of monooxygenase activity in S9 fractions. Treatment with 50 microg/ml MEP extract for 24 h increased benzo[a]pyrene hydroxylase and 7-ethoxycoumarin, 7-ethoxyresorufin, and methoxyresorufin O-dealkylases activities in S9. Treatments with 1 and 10 microg/ml MEP extract for 24 h markedly enhanced catabolism of 17beta-estradiol in MCF-7 cells. Cotreatment of the cells with 2 microM alpha-naphthoflavone, a cytochrome P-450 inhibitor and arylhydrocarbon receptor antagonist, blocked the increase of benzo[a]pyrene hydroxylase activity induced by treatment with MEP extract alone. Immunoblot analyses of S9 proteins using a mouse monoclonal antibody 1-12-3 against rat cytochrome P-450 1A1 and a rabbit polyclonal antibody against human cytochrome P-450 1B1 revealed that MEP extract induced proteins immunorelated to cytochromes P-450 1A1 and 1B1. RNA blot analysis of total RNA using human cytochrome P-450 (CYP)1A1 3'-end and human CYP1B1 RT-PCR product cDNA probes showed that MEP extract increased the levels of cytochromes P-450 1A1 and 1B1 mRNA hybridizable to the respective cDNA probes. Treatment with 10 micro M benzo[a]pyrene, a component of MEP extract, for 24 h induced catalytic activity, protein, and mRNA of cytochromes P-450 1A1 and 1B1 in MCF-7 cells. Treatment with MEP extract increased cytochromes P-450 1A1 and 1B1 proteins and mRNA levels in NCI-H322 human lung carcinoma and CL5 human lung adenocarcinoma cells. The extract also increased cytochrome P-450 1A1, but not cytochrome P-450 1B1, protein, and mRNA, in HepG2 human hepatoma cells. The present findings demonstrate that MEP extract has the ability to induce cytochromes P-450 1A1 and 1B1 in the estrogen-responsive MCF-7 cells. Induction of the carcinogen- and estrogen-metabolizing cytochromes P-450 1A1 and 1B1 may be an important factor to consider in assessing the potential health effects associated with human exposure to MEP.

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Induction of cytochrome P450 1A in hamster liver and lung by 6-nitrochrysene

Chen

Chou

Ueng

1998

Archives of Toxicology

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The present study has determined the effect of 6-nitrochrysene (6-NC) on hepatic and pulmonary cytochrome P450 (P450)-dependent monooxygenases using hamsters pretreated with the nitrated polycyclic aromatic hydrocarbon (nitro-PAH) at 5 mg/kg per day for 3 days. Pretreatment with 6-NC elevated serum gamma-glutamyltranspeptidase, lactate dehydrogenase, and bilirubin levels. Liver S9 fractions prepared from controls and hamsters pretreated with 6-NC markedly increased mutagenicity of the nitro-PAH in Salmonella typhimurium tester strains TA98, TA100, and TA102. The pretreatment selectively increased 1-nitropyrene reductase activities of lung cytosol and liver and lung microsomes. Pretreatment with 6-NC resulted in increases of microsomal 7-ethoxyresorufin and methoxyresorufin O-dealkylases activities in liver and lung without affecting the monooxygenase activities in kidney. Immunoblot analysis of microsomal proteins using mouse monoclonal antibody 1-12-3 to rat P450 1A1 revealed that 6-NC induced P450 1A-immunorelated proteins in liver and lung. RNA blot analysis using mouse P450 1A1 cDNA showed that 6-NC increased liver and lung P450 1A mRNA. 6-NC had no effect on the kidney P450 protein and mRNA. The present study demonstrates that the hamster enzymes can support 6-NC metabolic activation and the nitro-PAH induces liver and lung P4501A via a pretranslational mechanism.

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Induction of cytochromes P450 1A, 2B and 2E in hamster tissues by acetone

Cited by 12 publications

References 28 publications

The Effect of Isoniazid on Cyp2e1- And Cyp4a-Mediated Hydroxylation of Arachidonic Acid in the Rat Liver and Kidney

The Effect of Isoniazid on Cyp2e1- And Cyp4a-Mediated Hydroxylation of Arachidonic Acid in the Rat Liver and Kidney

Induction of Cytochromes P-450 1A1 and 1B1 by Motorcycle Exhaust Particulate In Human Breast Cancer MCF-7 Cells

Induction of cytochrome P450 1A in hamster liver and lung by 6-nitrochrysene

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