A modified method for the assay of benzo[a]pyrene hydroxylase

Dehnen, Walter; Tomingas, R.; Roos, Joachim

doi:10.1016/0003-2697(73)90083-3

Cited by 294 publications

(45 citation statements)

References 7 publications

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“…Nevertheless, the test does not appear very reproducible either in a single laboratory or between laboratories (Paigen et al, 1977;Cantelli Forti et al, 1977). Hence, many variants of the original fluorimetric method of Wattenberg et al (1968) and Nebert and Gelboin (1968) have been published by different workers in an attempt to improve its reproducibility and accuracy (Whitlock et al, 1972;Busbee et al, 1972;Kellermann et al, 1973a, band c;Dehnen et al, 1973;Gurtoo et al, 1975;Cantrell et al, 1976;Bast et al, 1976;Paigen et al, 1977 ([G-3H] BP) (Amersham/Searle Co; sp. act.…”

Section: Aryl Hydrocarbon Hydroxylase (Ahh)mentioning

confidence: 99%

Appraisal of fluorimetric assay of aryl hydrocarbon (benzo(α)pyrene) hydroxylase in cultured human lymphocytes

Trieff¹,

Forti²,

Smart³

et al. 1978

Br J Cancer

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Section: Aryl Hydrocarbon Hydroxylase (Ahh)mentioning

confidence: 99%

Appraisal of fluorimetric assay of aryl hydrocarbon (benzo(α)pyrene) hydroxylase in cultured human lymphocytes

Trieff¹,

Forti²,

Smart³

et al. 1978

Br J Cancer

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“…Because kerosene soot has both aliphatic and aromatic hydrocarbons (3,5), these hydrocarbons, which would be metabolized by cytochrome P450 dependent monooxygenase, may metabolize in the presence of asbestos, so that their persistence, and hence, toxic responses in the system may be affected. In this article, we report the effect of coexposure to Indian chrysotile asbestos and kerosene soot on the pulmonary phase I and phase II drug-metabolizing enzymes after 1,4,8,16,30,90, and 150 days of exposure. (8), epoxide hydrase (9), glutathione S-transferase (GST) (10) and protein (11) were assayed by standardized methods.…”

Section: Introductionmentioning

confidence: 99%

“…In this article, we report the effect of coexposure to Indian chrysotile asbestos and kerosene soot on the pulmonary phase I and phase II drug-metabolizing enzymes after 1,4,8,16,30,90, and 150 days of exposure. (8), epoxide hydrase (9), glutathione S-transferase (GST) (10) and protein (11) were assayed by standardized methods. The results were presented as mean ± standard error (SE) of six animals.…”

Section: Introductionmentioning

confidence: 99%

“…

…”

mentioning

confidence: 99%

“…Exposure to soot resulted in a significant induction of the pulmonary microsomal cytochrome P450 and the activity of dependent monooxygenase, benzo[alpyrene (B[a]P) hydroxylase, and epoxide hydrase at all time intervals. On the other hand, the cytosolic glutathione S-transferase (GST) activity was induced at days 1, 4,8,16, and 30 after exposure, followed by inhibition in the enzyme activity. In contrast, chrysotile exposure depleted cytochrome P450, B[aiP hydroxylase, epoxide hydrase, and GST at initial stages, while all these parameters except GST were induced at later stages.…”

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confidence: 99%

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Effect of Coexposure to Asbestos and Kerosene Soot on Pulmonary Drug-Metabolizing Enzyme System

Arif¹

1994

Environmental Health Perspectives

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This article reports the effect of coexposure to Indian chrysotile asbestos (5 mg/rat) and kerosene soot (5 mg/rat) on the pulmonary phase and phase 11 drug-metabolizing enzymes 1,4,8,16, 30, 90, and 150 days after a single intratracheal inoculation. Exposure to soot resulted in a significant induction of the pulmonary microsomal cytochrome P450 and the activity of dependent monooxygenase, benzo[alpyrene (B[a]P) hydroxylase, and epoxide hydrase at all time intervals. On the other hand, the cytosolic glutathione S-transferase (GST) activity was induced at days 1, 4,8,16, and 30 after exposure, followed by inhibition in the enzyme activity. In contrast, chrysotile exposure depleted cytochrome P450, B[aiP hydroxylase, epoxide hydrase, and GST at initial stages, while all these parameters except GST were induced at later stages. However, coexposure to chrysotile and soot led to a significant inhibition in the cytochrome P450 levels, activities of B[a]P hydroxylase, epoxide hydrase, and GST at initial stages of exposure. At advanced stages, however, an additional increase in cytochrome P450, B[a]P hydroxylase, and epoxide hydrase but a decrease in GST was observed. These results clearly show that the intratracheal coexposure to high levels of asbestos and kerosene soot alters the metabolic activity of the lung, which in turn may retain toxins in the system for a longer period, resulting in adverse pathological disorders. -Environ Health Perspect 102 (Suppl 5):181 -183 (1994)

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Mutagenic activation of arylamines by subcellular fractions of Chamaelea gallina clams exposed to environmental pollutants

Rodríguez-Ortega

Rodríguez‐Ariza

Amezcua³

et al. 2003

Environ and Mol Mutagen

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Biochemical measurements in the sentinel clam Chamaelea gallina have been used as biomarkers of marine pollution. In this study, S9, cytosolic fractions (CF), and microsomal fractions (MF) prepared from unexposed clams and clams exposed to model pollutants were used to activate 2-aminoanthracene (2-AA) and 2-acetylaminofluorene (AAF) to mutagens in Salmonella typhimurium strain BA149, which overexpresses O-acetyltransferase. Arylamine activation was similar with subcellular fractions from unexposed and Aroclor 1254-exposed clams, but decreased with fractions from As(III)- and Cu(II)-exposed clams. Bioactivation of arylamines by CF was higher than by MF, and higher with NADH than with NADPH as the reducing agent. alpha-Naphthoflavone inhibited AAF activation by CF and MF, but increased 2-AA activation nearly twofold. In contrast to the results with arylamine activation, benzo[a]pyrene hydroxylase (BPH) activity increased twofold in fractions from Aroclor 1254- and Cu(II)-exposed clams. Activation of 2-AA was also evaluated using S9 fractions from clams sampled at littoral sites with different pollutant levels. Compared to a reference site, lower 2-AA bioactivation and higher BPH activity were found in clams containing high levels of copper and organic contaminants, although the differences were not statistically significant. While these findings agree with the results of the model Cu(II) exposure, the effects of other pollutants cannot be ruled out. The results of the study demonstrate that arylamine activation by clams is not preferentially catalyzed by microsomal monooxygenases but by unknown cytosolic system(s), and that bioactivation of 2-AA and AAF appears to occur by different pathways.

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A modified method for the assay of benzo[a]pyrene hydroxylase

Cited by 294 publications

References 7 publications

Appraisal of fluorimetric assay of aryl hydrocarbon (benzo(α)pyrene) hydroxylase in cultured human lymphocytes

Appraisal of fluorimetric assay of aryl hydrocarbon (benzo(α)pyrene) hydroxylase in cultured human lymphocytes

Effect of Coexposure to Asbestos and Kerosene Soot on Pulmonary Drug-Metabolizing Enzyme System

Mutagenic activation of arylamines by subcellular fractions of Chamaelea gallina clams exposed to environmental pollutants

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