Search results for "Benzopyrenes"

showing 5 items of 35 documents

Prevention of benzo(a)pyrene-induced mutagenicity by homogeneous epoxide hydratase

1976

Benzo(a)pyrene and benz(a)anthrancene which, in contrast to the K-region epoxides benzo(a)pyrene 4,5-oxide and benz(a)anthracene 5,6-oxide, are not mutagenic to Salmonella typhimurium TA 1537 in the absence of mammalian enzyme preparations, were activated by liver microsomes from C3H mice, which had not received any pretreatment, to mutagens reverting this tester strain to histidine prototrophy. Addition of epoxide hydratase inhibitors greatly increased this mutagenicity and addition of pure epoxide hydratase reduced it by more than 95% down to the range of spontaneous mutations as observed in absence of any added mutagen. This demonstrates that the metabolic pathway responsible for the mut…

Salmonella typhimuriumCancer ResearchMutagenmedicine.disease_causechemistry.chemical_compoundEpoxide HydrataseBenz(a)AnthracenesmedicineBenzopyrenesHydro-LyasesHistidineEpoxide Hydrolaseschemistry.chemical_classificationChemistryfungifood and beveragesMolecular biologyEnzymeOncologyBiochemistryBenzo(a)pyreneHomogeneousMutationMicrosomes LiverMicrosomePyreneNADPInternational Journal of Cancer
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Dual role of epoxide hydratase in both activation and inactivation of benzo(a)pyrene.

1977

The effect of epoxide hydratase upon the mutagenicity of benzo(a)pyrene was investigated using two Salmonella typhimurium strains (TA 1537 and TA 98). These two bacterial strains were found to differ characteristically in their susceptibility to different mutagens biologically produced from benzo(a)pyrene providing a diagnostic tool to investigate which types of mutagenic metabolites were produced in various metabolic situations. The results showed that the pattern of mutagenic metabolites produced by microsomes from methylcholanthrene-treated mice was very different from that produced by microsomes from phenobarbital-treated or untreated mice. However in all cases at least two mutagenic me…

Salmonella typhimuriumendocrine systemHealth Toxicology and MutagenesisPharmacology toxicologyToxicologychemistry.chemical_compoundMiceDual roleEpoxide HydrataseAnimalsBenzopyrenesVolume concentrationBiotransformationEpoxide Hydrolasesfood and beveragesGeneral MedicineMonooxygenasechemistryBiochemistryBenzo(a)pyrenePhenobarbitalMutationMicrosomeMicrosomes LiverPyreneMethylcholanthreneMutagensArchives of toxicology
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Metabolic activation of dibenzo[a,l]pyrene by human cytochrome P450 1A1 and P450 1B1 expressed in V79 Chinese hamster cells.

1999

Metabolic activation of the strongly carcinogenic polycyclic aromatic hydrocarbon (PAH) dibenzo[a,l]pyrene (DB[a,l]P) and its trans-8,9-dihydrodiol (trans-8,9-diol) catalyzed by human cytochromes P450 (P450) 1A1 and 1B1 was investigated. DNA binding of DB[a,l]P in mammalian cell lines has previously been shown to be preferentially mediated by fjord region DB[a,l]P-11,12-dihydrodiol 13,14-epoxides (DB[a,l]PDE). In order to elucidate different capabilities of both P450 enzymes for metabolic activation of DB[a, l]P V79 Chinese hamster cells, stably expressing human P450s 1A1 or 1B1 have been exposed to the parent PAH or its racemic trans-8, 9-diol. For this purpose, synthesis and spectroscopic…

StereochemistryToxicologyChinese hamsterchemistry.chemical_compoundCytochrome P-450 Enzyme SystemCricetinaepolycyclic compoundsCytochrome P-450 CYP1A1AnimalsHumansBenzopyrenesBiotransformationCarcinogenic Polycyclic Aromatic HydrocarbonbiologyChemistryStereoisomerismGeneral MedicineMetabolismbiology.organism_classificationCell cultureCytochrome P-450 CYP1B1CarcinogensPyreneAryl Hydrocarbon HydroxylasesEnantiomerDNAHuman cytochromeChemical research in toxicology
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Structure elucidation of the adducts formed by fjord region Dibenzo[a,l]pyrene-11,12-dihydrodiol 13,14-epoxides with deoxyguanosine.

1999

Model adducts to be used in the identification of biologically formed adducts were synthesized by reaction of fjord-region dibenzo[a,l]pyrene 11,12-dihydrodiol 13,14-epoxides (DB[a,l]PDE) and deoxyadenosine (dA). The (+/-)-anti-DB[a,l]PDE was reacted with dA in dimethylformamide at 100 degrees C for 30 min to give four DB[a, l]PDE-14-N(6)dA adducts: (-)-anti-trans (26%), (+)-anti-trans (26%), (-)-anti-cis (17%), and (+)-anti-cis (17%). The (+/-)-syn-DB[a,l]PDE was reacted with dA under the same conditions to yield four DB[a, l]PDE-14-N(6)dA adducts and one N7Ade adduct: (+)-syn-cis (19%), (+)-syn-trans (13%), (-)-syn-cis (19%), (-)-syn-trans (13%), and (+/-)-syn-DB[a,l]PDE-14-N7Ade (22%). T…

Steric effectsCircular dichroismMagnetic Resonance SpectroscopyMolecular StructureStereochemistryDeoxyguanosineGeneral MedicineDNAFast atom bombardmentToxicologyMass SpectrometryAdductDihydroxydihydrobenzopyreneschemistry.chemical_compoundDNA AdductsStructure-Activity RelationshipSpectrometry FluorescenceDeoxyadenosinechemistryDimethylformamidePyreneStereoselectivityChromatography High Pressure LiquidChemical research in toxicology
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Reduction of benzo(a)pyrene mutagenicity by dihydrodiol dehydrogenase

1979

THE enigma of how inert chemicals can exert potent mutagenic, carcinogenic, allergenic and cytotoxic effects has been much debated. It has been learned that such compounds are metabolically converted to chemically reactive species1. In the case of aromatic or olefinic compounds, monooxygenases located in the membranes of the cell can transform these compounds into epoxides2–5 which by virtue of electrophilic reactivity can bind chemically to cellular macromolecules such as DNA, RNA and proteins, thereby disturbing biochemical control mechanisms and leading to the above mentioned toxic effects. The same membranes in which such epoxides are produced possess an enzyme, epoxide hydratase, which…

chemistry.chemical_classificationMultidisciplinarybiologyChemistryEpoxideMonooxygenaseCofactorAlcohol OxidoreductasesMiceStructure-Activity Relationshipchemistry.chemical_compoundEnzymeBiochemistryBenzo(a)pyreneMutationMicrosomes Liverpolycyclic compoundsbiology.proteinAnimalsPyreneBenzopyrenesBiotransformationCarcinogenDNANature
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