Search results for "cytochrome p450"

showing 10 items of 135 documents

Induction of hepatic heme oxygenase-1 by diclofenac in rodents: role of oxidative stress and cytochrome P-450 activity

2003

Abstract Background/Aims : The role of oxidative stress in diclofenac hepatotoxicity is still not clear. This study examined whether the drug induced heme oxygenase-1 (HO-1), a stress protein. Methods : HO-1 mRNA and HO activity were measured in mouse liver and in rat hepatocytes after treatment with diclofenac parallel to release of serum alanine aminotransferase (ALT) and sorbitol dehydrogenase (SDH) as a marker of hepatic damage. Results : HO-1 was transcriptionally and dose-dependently induced by diclofenac in mouse liver and rat hepatocytes. HO-1 mRNA, ALT and SDH peaked at the same time. Mechanistic studies revealed that the drug synergized with buthionine sulfoximine (BSO) in lowerin…

MaleCarcinoma HepatocellularDiclofenacCytochromeMice Inbred StrainsOxidative phosphorylationPharmacologymedicine.disease_causeMicechemistry.chemical_compoundCytochrome P-450 Enzyme SystemCell Line TumormedicineAnimalsCytochrome P-450 Enzyme InhibitorsHumansButhionine sulfoximineEnzyme InhibitorsButhionine SulfoximineDose-Response Relationship DrugHepatologybiologyLiver NeoplasmsMembrane ProteinsCytochrome P450GlutathioneAcetylcysteineRatsHeme oxygenaseOxidative Stressstomatognathic diseasesmedicine.anatomical_structureLiverchemistryBiochemistryEnzyme InductionHepatocyteHeme Oxygenase (Decyclizing)Hepatocytesbiology.proteinFemaleHeme Oxygenase-1Oxidative stressJournal of Hepatology
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Cultures with cryopreserved hepatocytes: applicability for studies of enzyme induction

2000

The use of hepatocyte cultures is well established for the study of drug-drug interactions. However, the major hindrance for the use of human hepatocyte cultures is that human hepatocytes are only occasionally available. This problem could be overcome by cryopreservation. Although cryopreserved hepatocytes have been recommended for short term applications in suspension, studies on induction of enzyme activity, requiring a more prolonged maintenance of cryopreserved hepatocytes in culture, represent a new field of research. In the present study, we established a technique that allows preparation of rat hepatocyte co-cultures, using cryopreserved hepatocytes. After incubation with phenobarbit…

MaleCell SurvivalMetaboliteBiologyToxicologyCryopreservationRats Sprague-DawleyHydroxylationchemistry.chemical_compoundCytochrome P-450 Enzyme SystemIn vivoCell AdhesionCytochrome P-450 CYP1A1medicineAnimalsEnzyme inducerCells CulturedGlutathione TransferaseCryopreservationCytochrome P450General MedicineCoculture TechniquesEnzyme assayRatsmedicine.anatomical_structureLiverchemistryBiochemistryEnzyme InductionPhenobarbitalHepatocyteCytochrome P-450 CYP2B1biology.proteinHydroxytestosteronesInstitut für ErnährungswissenschaftMethylcholanthreneChemico-Biological Interactions
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Differential Effects of Nonhydroxylated Flavonoids as Inducers of Cytochrome P450 1A and 2B Isozymes in Rat Liver

1996

Flavanone, flavone, and tangeretin differentially affected the activities of cytochrome P540 1A and 2B isozymes in rat liver. Flavone and, to a lesser extent, tangeretin, increased activities of ethoxyresorufin O-deethylase, methoxyresorufin O-demethylase, and pentoxyresorufin O-dealkylase (PROD), whereas flavanone mainly enhanced PROD activity. Immunoblot analysis indicated that flavone and tangeretin increased cytochrome P450 1A1, 1A2, and 2B1,2 forms, whereas flavanone only enhanced the cytochrome P450 2B isozymes. Northern blot study showed that flavone and tangeretin increased the level of the cytochrome P450 1A2 mRNAs. The concentration of the other mRNAs were slightly or not affected…

MaleCytochromeBlotting WesternMolecular Sequence Data[SDV.TOX.TCA]Life Sciences [q-bio]/Toxicology/Toxicology and food chainToxicologyFlavonesIsozymeTangeretinchemistry.chemical_compoundCytochrome P-450 Enzyme SystemAnimalsRNA MessengerRats WistarEnzyme inducerFlavonoidsPharmacologychemistry.chemical_classificationBase SequencebiologyCYP1A2Cytochrome P450Blotting NorthernFlavonesRatsIsoenzymesLiverchemistryBiochemistryEnzyme InductionFlavanonesMicrosomes Liverbiology.proteinFlavanoneToxicology and Applied Pharmacology
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Distribution and induction of cytochrome P-450 and two cytochrome P-450-dependent monooxygenase activities in rat liver parenchymal cell subpopulatio…

1989

Liver parenchymal cells from the periportal and centrilobular zones differ in their morphological, biochemical and functional characteristics. In an effort to obtain fractions enriched in either periportal or centrilobular cells, isolated rat liver parenchymal cells were separated into five subpopulations by centrifugal elutriation. The mean diameters of the cells present in fractions I-V were 19.6, 21.1, 21.8, 22.7 and 23.5 micron, respectively. The content of cytochrome P-450 as well as benzphetamine N-demethylase and 7-ethoxyresorufin O-deethylase activities were higher in the larger parenchymal cells than in the smaller ones. After administration of phenobarbital the content of cytochro…

MaleCytochromeHealth Toxicology and MutagenesisPyruvate KinaseElutriationIn Vitro TechniquesToxicologyMixed Function OxygenasesCytochrome P-450 Enzyme SystemParenchymamedicineCytochrome P-450 CYP1A1AnimalsEnzyme inducerbiologyCytochrome P450Alanine TransaminaseOxidoreductases N-DemethylatingRats Inbred StrainsGeneral MedicineMonooxygenaseRatsBiochemistryLiverEnzyme InductionPhenobarbitalbiology.proteinPhenobarbitalBenzphetamineOxidoreductasesmedicine.drugMethylcholanthreneArchives of toxicology
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Regio- and stereoselective regulation of monooxygenase activities by isoenzyme-selective phosphorylation of cytochrome P450.

1989

The phosphorylation of the two major phenobarbital-inducible cytochrome P450 isoenzymes IIB1 and IIB2 was increased in hepatocytes by the action of the membrane permeating cAMP derivatives N6-dibutyryl-cAMP and 8-thiomethyl-cAMP. Under these conditions the dealkylation of 7-pentoxyresorufin, a selective substrate of cytochrome P450IIB1 and P450IIB2 was markedly reduced. 16 beta-Hydroxylation of testosterone which is catalyzed specifically only by cytochrome P450IIB1 and IIB2 was strongly reduced; for 16 alpha-hydroxylation which is also catalyzed by cytochrome P450IIB1 and IIB2 but additionally by 3 further cytochrome P450 isoenzymes, this reduction was less pronounced; for the oxidation of…

MaleCytochromeStereochemistry25-Hydroxyvitamin D3 1-alpha-hydroxylaseBiophysicsHydroxylationBiochemistryMixed Function OxygenasesCytochrome P-450 Enzyme SystemCyclic AMPCytochrome c oxidaseAnimalsTestosteronePhosphorylationMolecular BiologybiologyChemistryCytochrome c peroxidaseCytochrome cCYP1A2Cytochrome P450 reductaseRats Inbred StrainsCell BiologyRatsIsoenzymesBiochemistryLiverSteroid 16-alpha-HydroxylaseCoenzyme Q – cytochrome c reductasePhenobarbitalbiology.proteinProtein Processing Post-TranslationalBiochemical and biophysical research communications
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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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CHARACTERIZATION OF MICROSOMAL CYTOCHROME P450-DEPENDENT MONOOXYGENASES IN THE RAT OLFACTORY MUCOSA

2005

Nasal administration of a drug ensures therapeutic action by rapid systemic absorption and/or the entry of some molecules into the brain through different routes. Many recent studies have pointed out the presence of xenobiotic-metabolizing enzymes in rat olfactory mucosa (OM). Nevertheless, very little is known about the precise identity of isoforms of cytochrome P450 (P450)-dependent monooxygenases (P450) and their metabolic function in this tissue. Therefore, we evaluated mRNA expression of 19 P450 isoforms by semiquantitative reverse transcriptase-polymerase chain reaction and measured their microsomal activity toward six model substrates. For purposes of comparison, studies were conduct…

MaleGene isoformPharmaceutical ScienceOlfactionSubstrate SpecificityOlfactory mucosaOlfactory MucosaMicrosomesmedicineAnimalsRNA MessengerEnzyme InhibitorsRats WistarPharmacologychemistry.chemical_classificationbiologyReverse Transcriptase Polymerase Chain ReactionCYP1A2Cytochrome P450MonooxygenaseRatsIsoenzymesKineticsEnzymemedicine.anatomical_structureBiochemistrychemistryMicrosomes Liverbiology.proteinMicrosomeAryl Hydrocarbon HydroxylasesDrug Metabolism and Disposition
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Modification of hepatic drug-metabolizing enzymes in rat fed naturally occurring allyl sulphides

1994

1. The effects of feeding allyl sulphides to rat (2000 ppm of the diet for 15 days) were investigated on various microsomal hepatic drug-metabolizing enzymes by their immunochemical detection and catalytic activity. 2. Allyl sulphides provoked a temporary dietary restriction, which enhanced the microsomal level of P450 and the activities of NADH-cytochrome c reductase and p-hydroxybiphenyl UDP-glucuronyltransferase (UDPGT 2), and lowered the activities of p-nitrophenol hydroxylase (PNPH), N-nitrosodimethylamine demethylase (NDMAD), laurate omega-hydroxylase (LAH) and glutathione S-transferase (GST). Therefore, pair-fed animals were used as a more relevant control for the dietary effects of …

MaleHealth Toxicology and MutagenesisImmunoblottingAllyl compoundAntineoplastic Agents[SDV.BID]Life Sciences [q-bio]/BiodiversitySulfidesReductaseToxicologyBiochemistryEating03 medical and health scienceschemistry.chemical_compound0302 clinical medicineIMMUNOCHIMIECytochrome P-450 Enzyme SystemAnimalsDisulfidesGlucuronosyltransferaseRats WistarEpoxide hydrolaseAnticarcinogenGlutathione Transferase030304 developmental biologyEpoxide HydrolasesPharmacologychemistry.chemical_classification0303 health sciencesDose-Response Relationship DrugbiologyChemistryBody WeightCytochrome P450Organ SizeGeneral MedicineGlutathioneDietRatsAllyl CompoundsEnzymeLiverBiochemistryTOXICOLOGIE030220 oncology & carcinogenesisMicrosomes Liverbiology.proteinMicrosomeRAT[SDV.BID] Life Sciences [q-bio]/Biodiversity
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Cryopreservation of rat, dog and human hepatocytes: influence of preculture and cryoprotectants on recovery, cytochrome P450 activities and induction…

2006

Several cryopreservation protocols for hepatocytes have been proposed over the past few years, but their effectiveness varies greatly as a function of the characteristics of the method used. One factor in the success of cryopreservation is the quality of cells before freezing. The results suggest that the cryopreservation of hepatocytes in a medium containing polyvinylpyrrolidone (PVP), in addition to DMSO, constitutes a convenient means of long-term storage of hepatocytes for preparing primary cultures to be used in drug metabolism studies. The combined use of the two cryoprotectants is particularly critical for low-viability cell suspensions. An interesting alternative to increase cell vi…

MaleHot TemperatureCryoprotectantHealth Toxicology and MutagenesisCellCombined useDrug Evaluation PreclinicalToxicologyBiochemistryCryopreservationRats Sprague-DawleyCryoprotective AgentsDogsCytochrome P-450 Enzyme SystemmedicineAnimalsHumansDimethyl SulfoxideViability assayCells CulturedCryopreservationPharmacologybiologyPovidoneCytochrome P450General MedicineRatsCell biologyEnzyme Activationmedicine.anatomical_structureBiochemistryHepatocytesbiology.proteinDrug metabolismXenobiotica
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Studies on the Biosynthesis of Microsomal Membrane Proteins. Site of Synthesis and Mode of Insertion of Cytochrome b5, Cytochrome b5 Reductase, Cytoc…

1982

The site of synthesis and mechanism of insertion into membranes of several microsomal polypeptides was studied using translation system programmed in vitro with polysomes or with mRNA extracted from free and membrane-bound rat liver polysomes. Primary translation products of cytochrome b5, NADH: cytochrome b5 oxidoreductase, NADPH: cytochrome P-450 oxidoreductase and epoxide hydrolase were isolated by specific immunoprecipitation and compared with the mature proteins. The following observations were made: 1 While cytochrome b5 and NADH: cytochrome b5 oxidoreductase are synthesized in free polysomes, NADPH: cytochrome P-450 oxidoreductase and epoxide hydrolase are made in membrane-bound poly…

MaleImmunodiffusionTime FactorsCytochromeBiochemistryElectron TransportCytochrome b5AnimalsCytochrome P450 family 1 member A1Epoxide hydrolaseCytochrome ReductasesCytochrome b5 reductaseNADPH-Ferrihemoprotein ReductaseEpoxide HydrolasesbiologyCytochrome bMembrane ProteinsCytochrome P450 reductaseRats Inbred StrainsMolecular biologyRatsCytochromes b5BiochemistryEnzyme InductionPhenobarbitalProtein BiosynthesisCoenzyme Q – cytochrome c reductaseMicrosomes Liverbiology.proteinCytochromesRabbitsCytochrome-B(5) ReductaseEuropean Journal of Biochemistry
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