Search results for "BIOTRANSFORMATION"

showing 10 items of 183 documents

Biological activation of 1,3-butadiene to vinyl oxirane by rat liver microsomes and expiration of the reactive metabolite by exposed rats.

1983

When 1,3-butadiene is incubated with rat liver microsomes and NADPH both enantiomers of vinyl oxirane are formed, the amount of epoxide being dependent on incubation time, microsomal protein, and substrate concentration. Inhibition by SKF 525 A or dithiocarb as well as induction by pretreatment with phenobarbital or 20-methylcholanthrene suggest participation of cytochrome P-450 in this reaction. The amount of epoxide is enhanced by addition of 1,1,1-trichloropropene oxide and reduced by glutathione, especially in the presence of hepatic cytosol. When rats are exposed to 1,3-butadiene in a closed chamber (conditions of maximal metabolism) vinyl oxirane is exhaled and can be quantitatively d…

MaleCancer ResearchCytochromeMetaboliteEpoxideIn Vitro TechniquesAcetonechemistry.chemical_compoundEthers CyclicmedicineButadienesAnimalsBiotransformationbiology13-ButadieneRats Inbred StrainsStereoisomerismGeneral MedicineGlutathioneMetabolismRatsOncologychemistryBiochemistryMicrosomebiology.proteinMicrosomes LiverEpoxy CompoundsPhenobarbitalmedicine.drugMutagensJournal of cancer research and clinical oncology
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cAMP-dependent phosphorylation of CYP2B1 as a functional switch for cyclophosphamide activation and its hormonal controlin vitro andin vivo

2001

An important feature of cytochrome P450 (CYP) 2B1 is its high ability to convert the prodrug cyclophosphamide (CPA) to therapeutically cytotoxic metabolites, resulting in interstrand DNA-cross-linking and cell death. We have examined whether and how the phosphorylation of CYP2B1 influences CPA metabolic activation in vitro and in vivo. We found first that only part of the total CYP2B1 pool undergoes phosphorylation. This part is fully inactivated. Second, phosphorylation of CYP2B1 in intact hepatocytes reduced by up to 75% toxification of CPA to mutagenic metabolites (totally dependent on the same preferentially CYP2B-catalyzed 4-hydroxylation of CPA as is the generation of highly cytotoxic…

MaleCancer ResearchProgrammed cell deathTime FactorsCellRats Sprague-DawleyStructure-Activity RelationshipSex FactorsIn vivoCyclic AMPPhosphoprotein PhosphatasesSerinemedicineAnimalsCytotoxic T cellheterocyclic compoundsPhosphorylationProtein kinase AAntineoplastic Agents AlkylatingCyclophosphamideBiotransformationbiologyCytochrome P450GlucagonCyclic AMP-Dependent Protein KinasesIn vitroRatsCell biologymedicine.anatomical_structureOncologyBiochemistryCytochrome P-450 CYP2B1Hepatocytescardiovascular systembiology.proteinPhosphorylationFemaleMutagensInternational Journal of Cancer
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Characterization of highly polar bis-dihydrodiol epoxide--DNA adducts formed after metabolic activation of dibenz[a,h]anthracene.

1993

Dibenz[a,h]anthracene as well as a biologically important metabolite of dibenz[a,h]anthracene, namely the M-region dihydrodiol trans-3,4-dihydroxy-3,4-dihydrodibenz[a,h]anthracene were in addition to further metabolism to a bay region diol epoxide, extensively transformed to a distal bisdihydrodiol, 3,4,10,11-tetrahydroxy-3,4,10,11-tetrahydro-dibenz[a,h]anthracene, which exhibited after renewed metabolic activation high DNA binding efficiency, leading to a new class of very polar DNA adducts. After incubation of dibenz[a,h]anthracene with DNA in the presence of liver microsomes from Aroclor 1254 treated male Sprague-Dawley rats highly polar DNA adducts probably originating from 3R,4R,10R,11…

MaleCancer ResearchStereochemistryChemical structureDiolEpoxideDeoxyribonucleosidesAdductRats Sprague-Dawleychemistry.chemical_compoundBenz(a)AnthracenesDibenz(ah)anthraceneAnimalsBiotransformationChromatography High Pressure LiquidAnthraceneMolecular StructureGeneral MedicineDNARatsSpectrometry FluorescenceBiochemistrychemistryMicrosomes LiverEnantiomerDNACarcinogenesis
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An experimental design for the controlled modulation of intracellular GSH levels in cultured hepatocytes

2006

This work proposes a practical experimental approach that allows the rapid in situ generation of a wide range of intracellular GSH concentrations in the intact hepatocyte under highly reproducible conditions. The strategy involves the use of diethyl maleate, a thiol-reactive electrophile that causes rapid and extensive GSH depletion, as well as GSH monoethylester, a GSH analogue that is readily taken up by cells and deesterified intracellularly to render GSH. For both agents, we have analyzed (i) the minimal exposure time required to produce a maximal and dose-related effect on intracellular GSH without altering hepatocyte viability or subsequent survival in culture, and (ii) the relative s…

MaleCell typeNAPQIEndogenyBiochemistryRats Sprague-Dawleychemistry.chemical_compoundCytochrome P-450 Enzyme SystemPhysiology (medical)medicineAnimalsBiotransformationCells CulturedAcetaminophenChemistryGlutathioneGlutathioneIn vitroRatsAcetaminophenmedicine.anatomical_structureBiochemistryHepatocyteHepatocytesBiophysicsIntracellularmedicine.drugFree Radical Biology and Medicine
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Synthesis of fjord region tetraols and their use in hepatic biotransformation studies of dihydrodiols of benzo[c]chrysene, benzo[g]chrysene and diben…

1998

Metabolic activation of the racemic benzo[c]chrysene-trans-9,10-, benzo[g]chrysene-trans-11,12- and dibenzo[a,l]pyrene-trans-11,12-dihydrodiols to fjord region syn- and anti-dihydrodiol epoxides by microsomes of Aroclor 1254-treated Sprague-Dawley rats has been examined. Since the fjord region dihydrodiol epoxides were hydrolytically unstable under the experimental conditions, their enzymatic formation was determined by analyzing the tetraols as their products of acidic hydrolysis upon addition of perchloric acid. The various stereoisomeric tetraols formed were separated by HPLC and identified by co-chromatography with authentic tetraols, which had been prepared by acidic hydrolysis of synt…

MaleChryseneCancer ResearchMagnetic Resonance SpectroscopyDiolEpoxideMedicinal chemistryChrysenesMass SpectrometryRats Sprague-Dawleychemistry.chemical_compoundpolycyclic compoundsAnimalsBenzopyrenesBiotransformationCarcinogenMolecular StructureStereoisomerismGeneral MedicinePhenanthrenesRatschemistryBiochemistryBenzopyreneCarcinogensMicrosomes LiverMicrosomeEpoxy CompoundsPyreneStereoselectivityMutagensCarcinogenesis
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Metabolism of 3-hydroxychrysene by rat liver microsomal preparations

1990

3-Hydroxychrysene, a metabolite of the polycyclic aromatic hydrocarbon (PAH) chrysene, was metabolised by rat liver microsomal preparations obtained from Arochlor 1254-pretreated rats. Eight major metabolites were isolated by high performance liquid chromatography and characterised by u.v. spectroscopy and a variety of mass spectrometric techniques. The metabolites were unambiguously identified as 9-hydroxy-trans-1,2-dihydroxy-1,2-dihydrochrysene and 9-hydroxy-r-1,t-2,t-3,c-4-tetrahydroxy-1,2,3,4-tetrahydrochrysene and tentatively identified as 3-hydroxy-trans-5,6-dihydroxy-5,6-dihydrochrysene (since chrysene is a symmetrical molecule the 3- and 9-positions are equivalent), 9-hydroxy-trans-…

MaleChryseneMetabolitePolycyclic aromatic hydrocarbonToxicologyHigh-performance liquid chromatographyChrysenesGas Chromatography-Mass SpectrometryMass Spectrometrychemistry.chemical_compoundAnimalsPhenolTCPOBiotransformationChromatography High Pressure Liquidchemistry.chemical_classificationChromatographyMolecular StructureRats Inbred StrainsGeneral MedicineMetabolismPhenanthrenesRatschemistryMicrosomes LiverMicrosomeSpectrophotometry UltravioletChemico-Biological Interactions
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The inhibition by flavonoids of 2-amino-3-methylimidazo[4,5-f]quinoline metabolic activation to a mutagen: a structure-activity relationship study.

1997

The mutagenicity of 2-amino-3-methylimidazo[4,5-f]quinoline (IQ) in Salmonella typhimurium TA98 is inhibited by flavonoids with distinct structure-antimutagenicity relationships (Edenharder, R., I. von Petersdorff I. and R. Rauscher (1993). Antimutagenic effects of flavonoids, chalcones and structurally related compounds on the activity of 2-amino-3-methylimidazo[4,5-f]quinoline (IQ) and other heterocyclic amine mutagens from cooked food, Mutation Res., 287, 261-274). With respect to the mechanism(s) of antimutagenicity, the following results were obtained here. (1) 7-Methoxy- and 7-ethoxyresorufin-O-dealkylase activities in rat liver microsomes, linked to cytochrome P-450-dependent 1A1 and…

MaleCytochrome P-450 CYP1A2 InhibitorsHealth Toxicology and MutagenesisHydroxylationFlavonesRats Sprague-Dawleychemistry.chemical_compoundStructure-Activity RelationshipFlavonolsCytochrome P-450 Enzyme SystemGeneticsCytochrome P-450 CYP1A1AnimalsMolecular BiologyBiotransformationchemistry.chemical_classificationFlavonoidsMutagenicity Testsfood and beveragesAntimutagenic AgentsMonooxygenaseDiosmetinRatschemistryBiochemistryHydroxyquinolinesMicrosomes LiverQuinolinesOxidoreductasesAntimutagenFlavanoneLuteolinFisetinMutagensMutation research
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Metabolism of apigenin by rat liver phase I and phase II enzymes and by isolated perfused rat liver

2004

The metabolism of apigenin, a low estrogenic flavonoid phytochemical, was investigated in rat using liver models both in vitro (subcellular fractions) and ex vivo (isolated perfused liver). In vitro, phase I metabolism led to the formation of three monohydroxylated derivatives: luteolin which was the major metabolite (K(m) = 22.5 +/- 1.5 microM; V(max) = 5.605 +/- 0.090 nmol/min/mg protein, means +/- S.E.M.), scutellarein, and iso-scutellarein. These oxidative pathways were mediated by cytochrome P450 monooxygenases (P450s). The use of P450 inhibitors and inducers showed that CYP1A1, CYP2B, and CYP2E1 are involved. In vitro studies of phase II metabolism indicated that apigenin underwent co…

MaleFMN ReductaseMetabolite[SDV]Life Sciences [q-bio]Pharmaceutical ScienceIn Vitro TechniquesMethylation030226 pharmacology & pharmacyMass Spectrometry03 medical and health scienceschemistry.chemical_compoundGlucuronides0302 clinical medicineCytochrome P-450 Enzyme SystemAnimalsApigeninEnzyme InhibitorsRats WistarLuteolinBiotransformationChromatography High Pressure LiquidComputingMilieux_MISCELLANEOUS030304 developmental biologyFlavonoidsPharmacologySex Characteristics0303 health sciencesbiologySulfatesScutellareinCytochrome P450MonooxygenaseDiosmetinRats3. Good health[SDV] Life Sciences [q-bio]KineticsLiverBiochemistrychemistryApigeninbiology.proteinRATFemaleSpectrophotometry UltravioletLuteolinNADPDrug metabolismSubcellular Fractions
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Similar level of metabolic activation of benzo(a)pyrene in perfused rat lung and liver and protection of lung by liver in a combined perfusion system

1982

Abstract Irreversible binding of metabolically activated benzo(a)pyrene to DNA, RNA and protein proceeds by a different time course in perfused liver and lung of 5,6-benzoflavone-treated rats. Peak binding in liver is obtained after 15 min while binding in lung continuously increases over 120 min. Total irreversible binding per mg DNA or RNA is in the same order of magnitude in both organs. While binding in lung is lower at 15 min it exceeds binding in liver at 120 min. Binding per mg protein is higher in lung than in liver over the whole perfusion period. Introduction of a liver into the lung perfusion circuit decreases binding in lung. This protection effect is more pronounced when the li…

MaleIrreversible bindingBiophysicsIn Vitro TechniquesBiologyBiochemistrychemistry.chemical_compoundBenzo(a)pyrenemedicineAnimalsBenzopyrenesLungMolecular BiologyBiotransformationLungProteinsRNARats Inbred StrainsDNACell Biologyrespiratory systemMolecular biologyRatsrespiratory tract diseasesPerfusionKineticsmedicine.anatomical_structureLiverchemistryBiochemistryBenzo(a)pyreneTime courseRNAPyrenePerfusionDNABiochemical and Biophysical Research Communications
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Multi-step metabolic activation of benzene. Effect of superoxide dismutase on covalent binding to microsomal macromolecules, and identification of gl…

1980

Abstract Incubation of [ 14 C]benzene or [ 14 C]phenol with liver microsomes from untreated rats, in the presence of a NADPH-generating system, gave rise to irreversible binding of metabolites to microsomal macromolecules. For both substrates this binding was inhibited by more than 50% by addition of superoxide dismutase to the incubation mixtures. The decrease in binding was compensated for by accumulation of [ 14 C]hydroquinone, indicating superoxide-mediated oxidation of hydroquinone as one step in the activation of benzene to metabolites binding to microsomal macromolecules. Since our previous work had shown that binding occurred mainly with protein rather than ribonucleic acid and was …

MaleMacromolecular SubstancesMetaboliteIn Vitro TechniquesToxicologyMass SpectrometryAdductchemistry.chemical_compoundPhenolsAnimalsPhenolBenzeneBiotransformationChromatography High Pressure LiquidCatecholChromatographyHydroquinoneSuperoxide DismutaseChemistryBenzeneGeneral MedicineGlutathioneGlutathioneBenzoquinoneRatsMicrosomes LiverChemico-Biological Interactions
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