Search results for "Cytochrome P-450 Enzyme System"

showing 10 items of 163 documents

Metabolism and bioactivation of toxicants in the lung. The in vitro cellular approach.

2005

Lung is a target organ for the toxicity of inhalated compounds. The respiratory tract is frequently exposed to elevated concentrations of these compounds and become the primary target site for toxicity. Occupational, accidental or prolonged exposure to a great variety of chemicals may result in acute or delayed injury to cells of the respiratory tract. Nevertheless, lung has a significant capability of biotransforming such compounds with the aim of reducing its potential toxicity. In some instances, the biotransformation of a given compound can result in the generation of more reactive, and frequently more toxic, metabolites. Indeed, lung tissue is known to activate pro-carcinogens (i.e. po…

Pulmonary toxicityBiologyToxicologyModels BiologicalPathology and Forensic MedicineCell LineXenobioticsCytochrome P-450 Enzyme SystemmedicineHumansEpoxide hydrolaseLungBiotransformationA549 cellAir PollutantsLungCytochrome P450Cell BiologyGeneral Medicinerespiratory systemCYP2E1medicine.anatomical_structureBiochemistryCell cultureToxicitybiology.proteinExperimental and toxicologic pathology : official journal of the Gesellschaft fur Toxikologische Pathologie
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The induction of cytochrome P450 3A5 (CYP3A5) in the human liver and intestine is mediated by the xenobiotic sensors pregnane X receptor (PXR) and co…

2004

Induction of cytochrome P450 3A (CYP3A) by xenobiotics may lead to clinically relevant drug interactions. In contrast with other CYP3A family members, studies on the inducibility of CYP3A5 indicate conflicting results. We report the induction of CYP3A5 mRNA in 13 of 16 hepatocyte preparations exposed to rifampin. Furthermore, induction of CYP3A5 mRNA was observed in intestinal biopsies in three of eight probands following exposure to the antibiotic. The highest absolute levels of CYP3A5 transcripts were found following rifampin treatment in hepatocytes and intestines from carriers of CYP3A5*1 alleles. Elucidation of the mechanism involved in CYP3A5 induction revealed that constitutively act…

Receptors SteroidTime FactorsCYP3ABiopsyAmino Acid MotifsReceptors Cytoplasmic and NuclearPharmacology030226 pharmacology & pharmacyBiochemistryTransactivation0302 clinical medicineCytochrome P-450 Enzyme SystemGenes ReporterCytochrome P-450 CYP3AIntestinal MucosaReceptorPromoter Regions GeneticGenes Dominant0303 health sciencesPregnane X receptorPregnane X Receptor3. Good healthmedicine.anatomical_structureLiverHepatocyteRifampinPlasmidsProtein BindingTranscriptional ActivationHeterozygoteGenotypeBiologyTransfectionXenobiotics03 medical and health sciencesmedicineHumansRNA MessengerMolecular BiologyAllelesConstitutive Androstane Receptor030304 developmental biologyMessenger RNACYP3A4Cell BiologyMolecular biologyProtein Structure TertiaryHepatocytesRNADrug metabolismTranscription FactorsThe Journal of biological chemistry
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Evaluation of the genotoxic and cytochrome P450 monooxygenase‐inhibitory potential of dicuran on procaryotic and eucaryotic test systems

2000

The effect of the herbicide Dicuran 500 FL (formulated product) on the phenotypical and genotypical changes in procaryotic and eucaryotic organisms was investigated using short-term tests for detecting genotoxins. Since pesticides discharged in the water environment can modulate the mixed-function monooxygenases (MFO) detoxification system of water organisms, the in vivo and in vitro effects of Dicuran on hepatic cytochrome P450 (cyt P450) monooxygenase activities were also examined in juvenile carp (Cyprinus carpio L.). By measuring the activities of MFO in experimental carp exposed to Dicuran an attempt was made to establish whether Dicuran could be bioactivated by MFO into ultimate mutag…

Salmonella typhimuriumOxygenaseCarpsBiologymedicine.disease_causeMixed Function OxygenasesAmes testCytochrome P-450 Enzyme SystemmedicineWater environmentAnimalsCytochrome P-450 Enzyme InhibitorsCarpCytotoxinsHerbicidesMutagenicity Testsbusiness.industryPhenylurea CompoundsCytochrome P450General MedicineMonooxygenasebiology.organism_classificationPollutionBiotechnologyLiverBiochemistryMicronucleus testbiology.proteinbusinessWater Pollutants ChemicalGenotoxicityMutagensFood ScienceJournal of Environmental Science and Health, Part B
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Liver and Statins: A Critical Appraisal of the Evidence.

2019

Adverse drug reactions (ADRs) represent an important cause of morbidity and mortality worldwide. Statins are a class of drugs whose main adverse effects are drug-induced liver injury (DILI) and myopathy. Some of these may be predictable, due to their pharmacokinetic and pharmacodynamic properties, while others, unfortunately, are idiosyncratic. Genetic factors may also influence patient susceptibility to DILI and myopathy in the case of statins. This review will first discuss the role of statins in cardiovascular disease treatment and prevention and the underlying mechanisms of action. Furthermore, to explore the susceptibility of statin-induced adverse events such as myopathy and hepatoto…

Settore MED/09 - Medicina InternaOrganic Anion TransportersGenome-wide association studyBioinformaticsBiochemistryCytochrome P-450 Enzyme SystemHLA AntigensDrug DiscoveryMetSmedicineHumansGenetic Predisposition to DiseaseDrug reactionMyopathyAdverse effectDisease treatmentPharmacologybusiness.industryOrganic ChemistryStatinmedicine.diseaseHepatitis CHCV.Critical appraisalSingle Nucleotide Polymorphisms (SNPs)Cardiovascular DiseasesPharmacodynamicsliver damageMolecular MedicineATP-Binding Cassette TransportersMetabolic syndromemedicine.symptomChemical and Drug Induced Liver InjuryHydroxymethylglutaryl-CoA Reductase Inhibitorsbusinessgenetic susceptibilityCurrent medicinal chemistry
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Charged Tags for the Identification of Oxidative Drug Metabolites Based on Electrochemistry and Mass Spectrometry

2020

Abstract Most of the active pharmaceutical ingredients like Metoprolol are oxidatively metabolized by liver enzymes, such as Cytochrome P450 monooxygenases into oxygenates and therefore hydrophilic products. It is of utmost importance to identify the metabolites and to gain knowledge on their toxic impacts. By using electrochemistry, it is possible to mimic enzymatic transformations and to identify metabolic hot spots. By introducing charged‐tags into the intermediate, it is possible to detect and isolate metabolic products. The identification and synthesis of initially oxidized metabolites are important to understand possible toxic activities. The gained knowledge about the metabolism will…

Spectrometry Mass Electrospray IonizationAlkylationPyridinesElectrospray ionizationPyridinium CompoundsMass spectrometryHydroxylationlcsh:Chemistrydrug metabolitesCytochrome P-450 Enzyme Systemcharged tagsChromatography High Pressure Liquidmass spectrometrychemistry.chemical_classificationActive ingredientChromatographybiologyCommunicationanodic oxidationCytochrome P450General ChemistryMetabolismElectrochemical TechniquesMonooxygenaseCommunicationsEnzymelcsh:QD1-999chemistryelectrochemistrybiology.proteinOxidation-ReductionDrug metabolismMetoprololSignal TransductionChemistryOpen
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Synthesis and in vitro antileukemic activity of new 4-triazenopyrazole derivatives

2003

Several new 4-(3,3-dimethyltriazeno)-5-benzamidopyrazole derivatives were prepared by reacting 4-diazo-5-benzamidopyrazole derivatives with dimethylamine. The compounds were tested at 10 microM for their vitro antileukemic activity against K562 (Human chronic myelogenous leukemia) and Raji (human Burkitt limphoma ) cell lines. Dacarbazine and methotrexate were used for comparative purpose. The 3-methyl-4-(3,3-dimethyltriazeno)-5-(substituted benzamido)pyrazoles, bearing the pyrazole nucleus free at 1 position, resulted more active than the 1-(substituted phenyl)-3-methyl-4-(3,3-dimethyltriazeno)-5-benzamidopyrazoles. Dacarbazine at 10 microM showed no activity in the above tests. The observ…

StereochemistryDacarbazinePharmaceutical ScienceAntineoplastic AgentsPyrazoleSettore BIO/19 - Microbiologia GeneraleInhibitory Concentration 50Structure-Activity Relationshipchemistry.chemical_compoundCytochrome P-450 Enzyme SystemCell Line TumorLeukemia Myelogenous Chronic BCR-ABL PositiveDrug DiscoverymedicineHumansDimethylamine4-Triazenopyrazoles Antiproliferative activity In vitro antileukemic acitivityDemethylationTriazinesGeneral MedicineBurkitt LymphomaSettore CHIM/08 - Chimica FarmaceuticaIn vitroRaji cellchemistryMechanism of actionPyrazolesGrowth inhibitionmedicine.symptommedicine.drugIl Farmaco
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Stereoselective metabolism of dibenz(a,h)anthracene to trans-dihydrodiols and their activation to bacterial mutagens.

1990

Dibenz(a,h)anthracene (DBA), a carcinogenic, polycyclic aromatic hydrocarbon ubiquitous in the environment, is metabolized by the hepatic microsomal fraction of immature Sprague-Dawley rats pretreated with Aroclor 1254 to 27 ethyl acetate-extractable metabolites. More than half of these metabolites (51%) consisted of trans-1,2-; -3,4-; and -5,6-dihydrodiols including their identified secondary metabolites. The three trans-dihydrodiols (4.9, 15.8, and 0.6% of total metabolic conversion) were highly enriched in their R,R enantiomers (85, 71, and 98%) as determined by high performance liquid chromatography on suitable chiral stationary phases. This is explained on the basis of the stereoselect…

StereochemistryHealth Toxicology and MutagenesisPolycyclic aromatic hydrocarbonIn Vitro Techniqueschemistry.chemical_compoundCytochrome P-450 Enzyme Systempolycyclic compoundsBenz(a)AnthracenesAnimalsDibenz(ah)anthraceneCarcinogenHistidineEpoxide Hydrolaseschemistry.chemical_classificationAnthraceneMutagenicity TestsPublic Health Environmental and Occupational HealthRats Inbred StrainsStereoisomerismMetabolismRatschemistryEpoxide HydrolasesMicrosomes LiverMicrosomeMutagensResearch ArticleEnvironmental Health Perspectives
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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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Role of hepatocyte nuclear factor 3γ in the expression of human CYP2C genes

2004

Hepatocyte nuclear factor 3 gamma (HNF-3 gamma) is an important transcription factor for the maintenance of specific liver functions. However, its relevance in the expression of human cytochrome P450 (CYP) genes has not yet been explored. Several HNF3 putative binding sites can be identified in human CYP2C 5'-flanking regions. Gene reporter experiments with proximal promoters revealed that HNF-3 gamma transactivated CYP2C8, CYP2C9, and CYP2C19 (25-, 4-, and 4-fold, respectively), but it did not transactivate CYP2C18. However, overexpression of HNF-3 gamma in hepatoma cells by means of a recombinant adenovirus induced CYP2C9, CYP2C18, and CYP2C19 mRNA (4.5-, 20-, and 50-fold, respectively) b…

Transcriptional ActivationRecombinant Fusion ProteinsGenetic VectorsBiophysicsBiologyHydroxamic AcidsTransfectionBiochemistryGene Expression Regulation EnzymologicAdenoviridaeCytochrome P-450 Enzyme SystemSp3 transcription factorCell Line TumormedicineHumansRNA MessengerEnzyme InhibitorsLuciferasesPromoter Regions GeneticMolecular BiologyTranscription factorBinding SitesNuclear ProteinsPromoterMolecular biologyDNA-Binding ProteinsHistone Deacetylase InhibitorsHepatocyte nuclear factorsTrichostatin AHepatocyte nuclear factor 4Hepatocyte nuclear factor 4 alphaHepatocytesFOXA2Transcription Initiation SiteHepatocyte Nuclear Factor 3-gammaHeLa CellsTranscription Factorsmedicine.drugArchives of Biochemistry and Biophysics
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Transcriptional Regulation of Human CYP3A4 Basal Expression by CCAAT Enhancer-Binding Protein α and Hepatocyte Nuclear Factor-3γ

2003

Cytochrome P450 3A4 (CYP3A4) is involved in the metabolism of more than 50% of currently used therapeutic drugs, yet the mechanisms that control CYP3A4 basal expression in liver are poorly understood. Several putative binding sites for CCAAT/enhancer-binding protein (C/EBP) and hepatic nuclear factor 3 (HNF-3) were found by computer analysis in CYP3A4 promoter. The use of reporter gene assays, electrophoretic mobility shift assays, and site-directed mutagenesis revealed that one proximal and two distal C/EBP alpha binding sites are essential sites for the trans-activation of CYP3A4 promoter. No trans-activation was found in similar reporter gene experiments with a HNF-3 gamma expression vec…

Transcriptional ActivationTranscription GeneticGenetic VectorsBiologyTransfectiondigestive systemGene Expression Regulation EnzymologicChromatin remodelingAdenoviridaeCytochrome P-450 Enzyme SystemCCAAT-Enhancer-Binding Protein-alphamedicineCytochrome P-450 CYP3AHumansEnzyme InhibitorsBinding sitePromoter Regions GeneticCells CulturedPharmacologyReporter geneExpression vectorCcaat-enhancer-binding proteinsNuclear ProteinsMolecular biologyChromatinDNA-Binding ProteinsHistone Deacetylase InhibitorsHepatocyte nuclear factorsTrichostatin AHepatocytesMolecular MedicineHepatocyte Nuclear Factor 3-gammaTranscription Factorsmedicine.drugMolecular Pharmacology
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