Search results for "Enzyme system"

showing 10 items of 167 documents

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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Effect of onion consumption by rats on hepatic drug-metabolizing enzymes

2001

Fruits and vegetables or their natural constituents which increase detoxication enzymes and/or reduce activating enzymes are considered as good candidates to prevent chemically-induced carcinogenesis. In this study, rats were fed a diet supplemented with 20% onion powder for 9 days. Several cytochrome P450 (CYP)s enzymes (CYP 1A, 2B, 2E1, 3A), which are involved in carcinogen activation, were determined by measuring their enzyme activities using specific substrates. In addition, phase II enzymes activities such as UDP-glucuronosyltransferase (UGT) and glutathione S-transferase (GST), involved in detoxication of carcinogens, were measured. Protein levels of CYPs and GST A1/A2, A3/A5, Ml, M2 …

[SDE] Environmental SciencesMale[SDV]Life Sciences [q-bio]Toxicologychemistry.chemical_compoundCytosol0302 clinical medicineCytochrome P-450 Enzyme System[SDV.IDA]Life Sciences [q-bio]/Food engineeringOnionsAnticarcinogenComputingMilieux_MISCELLANEOUSChromatography High Pressure Liquid2. Zero hungerchemistry.chemical_classification0303 health sciencesbiologyfood and beveragesBiological activityGeneral Medicine[SDV.IDA] Life Sciences [q-bio]/Food engineeringGlutathione[SDV] Life Sciences [q-bio]LiverPharmaceutical PreparationsBiochemistry030220 oncology & carcinogenesis[SDE]Environmental SciencesMicrosomes Liver[SPI.GPROC] Engineering Sciences [physics]/Chemical and Process EngineeringImmunoblottingdigestive systemGas Chromatography-Mass Spectrometry03 medical and health sciencesGlycosyltransferaseAnimals[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringRats WistarCarcinogen030304 developmental biologyFlavonoidsSulfur CompoundsCytochrome P450GlutathioneDietRatsEnzymechemistrybiology.proteinMicrosomeRATSpectrophotometry UltravioletFood ScienceFood and Chemical Toxicology
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An in vitro tool to assess cytochrome P450 drug biotransformation-dependent cytotoxicity in engineered HepG2 cells generated by using adenoviral vect…

2011

Many adverse drug reactions leading to hepatotoxicity are caused by the cytochrome P450-dependent activation of non-toxic drugs or chemicals into reactive metabolites. To this end, adenoviruses were used as a tool to efficiently deliver specific CYP genes into cultured cells (i.e., human hepatoma cell line HepG2). Recombinant-defective adenoviral vectors encoding for genes CYP3A4 (Adv-CYP3A4), CYP2E1 (Adv-CYP2E1), CYP2A6 (Adv-CYP2A6) and CYP1A2 (Adv-CYP1A2) were used to confer specific CYP drug metabolic capabilities to HepG2 cells. Upgraded cells transiently expressed single specific cytochrome P450 enzymatic activities in terms of the number of the infecting virus particles used in their …

biologyCYP3A4Cell SurvivalGenetic VectorsCYP1A2Cytochrome P450Hep G2 CellsGeneral MedicineCYP2E1ToxicologyMolecular biologyAdenoviridaeTransduction (genetics)Cytochrome P-450 Enzyme SystemPharmaceutical PreparationsTransduction GeneticToxicity Tests Acutebiology.proteinHumansMTT assayViability assayCytotoxicityBiotransformationToxicology in Vitro
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Phosphorylation of cytochrome P450 isoenzymes in intact hepatocytes and its importance for their function in metabolic processes.

1990

Recent data show that besides the well-known long-term regulation of cytochrome P450-dependent monooxygenase activity by induction there also exists a fast regulation by phosphorylation. This phosphorylation occurs when purified cytochromes P450 are combined with purified protein kinases, and also in intact cells. This process is donor- and acceptor-selective leading to phosphorylation of defined isoenzymes by defined protein kinases. This in turn leads to fast and marked changes in metabolism which are selective for given substrates and regio- and stereo-selective for given positions. This in turn is selectively and differentially influenced by the individual control of the protein kinase …

chemistry.chemical_classificationCytochromebiologyKinaseHealth Toxicology and MutagenesisCytochrome P450General MedicineMetabolismToxicologyIsoenzymesEnzymeBiochemistrychemistryCytochrome P-450 Enzyme SystemLiverbiology.proteinPhosphorylationAnimalsHumansProtein phosphorylationPhosphorylationProtein kinase AArchives of toxicology
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Comparison of the Biosynthesis of Cellulose in vitro and in vivo in Cotton Bolls

1966

THE work of Hassid et al.1–3 on the cell-free synthesis of cellulose with an enzyme system isolated from mung bean seedlings and young cotton bolls has shown that the enzyme is apparently unable to distinguish guanosine diphosphate-D-glucose from guanosine diphosphate-D-mannose. Moreover, there was a notable decrease in the amount of the synthesized cellulose using enzymes from cotton bolls older than 15 days.

chemistry.chemical_classificationMultidisciplinaryMung beanGuanosineIn vitrochemistry.chemical_compoundEnzymeBiochemistrychemistryEnzyme systemBiosynthesisIn vivoBotanyCelluloseNature
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A newin vitroapproach for the simultaneous determination of phase I and phase II enzymatic activities of human hepatocyte preparations

2007

Primary hepatocytes are still the best qualified in vitro system to anticipate drug metabolism in man. Recent advances in hepatocytes cryopreservation have notably increased their use not only for drug metabolism studies, but also for other applications such as cell transplantation. Evaluation of the drug-metabolizing competence of each hepatocytes preparation is needed. To date, the metabolic characterization of hepatocytes preparations relies on the assessment of phase I activities and the role of phase II enzymes receives little attention. A novel approach for the rapid assessment of the metabolic functionality of hepatocytes has been developed. A five-probe cocktail was used to simultan…

chemistry.chemical_classificationSpectrometry Mass Electrospray IonizationSulfotransferaseCYP3A4Organic ChemistryTandem mass spectrometryMetabolic Detoxication Phase IICryopreservationIn vitroAnalytical ChemistryGlucuronidaseEnzymeCytochrome P-450 Enzyme SystemBiochemistrychemistryTandem Mass SpectrometryHepatocytesHumansMetabolic Detoxication Phase IGlucuronosyltransferaseSulfotransferasesCells CulturedChromatography High Pressure LiquidSpectroscopyDrug metabolismRapid Communications in Mass Spectrometry
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Effect of cytochrome P450 inhibitors (diethyl dithiocarbamate, ketoconazole and grapefruit juice) on the pharmacokinetics of all-trans-retinoic acid.

2004

Diethyl dithiocarbamate (DEDTC) has been reported to be a more powerful inhibitor of all-trans-retinoic acid (ATRA) in vitro metabolism than the well-established cytochrome P450 (CYP) inhibitor ketoconazole (KC). In recent years grapefruit juice (GJ) has been shown to be able to increase the oral bioavailability of several drugs by inhibiting intestinal CYP. This study investigated the in vivo effect of these CYP inhibitors on the pharmacokinetics of ATRA. The latter was administered to rats as a constant-rate intravenous (i.v.) infusion (0.48 mg h(-1) kg(-1)) during 10 h and orally (1.6 mg kg(-1)). DEDTC (320 mg kg(-1) x 2 i.v., 6.4 and 32 mg kg(-1) per os (p.o.)) did not change the ATRA c…

food.ingredientRetinoic acidPharmaceutical ScienceTretinoinPharmacologyGrapefruit juiceBeverageschemistry.chemical_compoundfoodPharmacokineticsCytochrome P-450 Enzyme SystemIn vivoDrug DiscoverymedicineAnimalsCytochrome P-450 Enzyme InhibitorsEnzyme InhibitorsneoplasmsCytochrome P-450 Enzyme Inhibitorsbiologyorganic chemicalsCytochrome P450BioavailabilityRatsKetoconazolechemistrybiology.proteinKetoconazoleDitiocarbmedicine.drugCitrus paradisiFarmaco (Societa chimica italiana : 1989)
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Cytochrome-P450 phosphorylation as a functional switch

2002

Xenobiotic metabolizing cytochromes P450 (CYP) were shown to be phosphorylated in vitro (using purified protein kinases together with purified CYPs), in intact cells (in V79 cells after transfection of cDNAs coding for individual CYPs, in diagnostic mutants, in hepatocytes), and in whole organisms (rats). CYP phosphorylation is highly isoenzyme selective in that only some CYPs are phosphorylated. Protein kinase A (PKA) was identified as a major catalyst for the phosphorylation of CYPs. The PKA recognition motif Arg-Arg-X-Ser is present in several members of the CYP2 family, but is used by only some of them, most notably by CYP2B1/2B2 and CYP2E1. For CYP2B1 it was shown that a substantial po…

inorganic chemicalsAmino Acid MotifsMutantBiophysicsBiologyTransfectionBiochemistryCatalysisCytochrome P-450 Enzyme SystemCyclic AMPAnimalsheterocyclic compoundsProtein phosphorylationPhosphorylationEnzyme inducerProtein kinase AMolecular BiologyCells CulturedKinaseorganic chemicalsCytochrome P450Transfectionrespiratory systemMolecular biologyRatsKineticsenzymes and coenzymes (carbohydrates)LiverBiochemistryMutagenesis Site-Directedbiology.proteinPhosphorylationRabbitsArchives of Biochemistry and Biophysics
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