Search results for "cytochrome P450"

showing 10 items of 135 documents

Interacciones farmacológicas de los fármacos antihipertensivos

2005

A drug interaction is the quantitative or qualitative modification of the effect of a drug by the simultaneous or successive administration of a different one. Hypertensive patients, mainly the more elderly ones, frequently present concomitant diseases that require the administration of several medicines which facilitates the appearance of interactions. The lack of effectiveness of the antihypertensive treatment is a relatively frequent fact that sometimes is due to interactions of antihypertensive drugs with other treatments. It is difficult to determine the incidence of interactions, but it is related to the number of drugs administered simultaneously. Between 37 and 60% of hospital-admis…

Drugbiologybusiness.industrymedia_common.quotation_subjectCytochrome P450Angiotensin-converting enzymeGeneral MedicineDrug interactionBioinformaticsPharmacokineticsbiology.proteinMedicineIn patientAngiotensin Receptor Blockersbusinessmedia_commonMedicina Clínica
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Drug-metabolizing enzymes in the skin of man, rat, and pig.

2007

The mammalian skin has long been considered to be poor in drug metabolism. However, many reports clearly show that most drug metabolizing enzymes also occur in the mammalian skin albeit at relatively low specific activities. This review summarizes the current state of knowledge on drug metabolizing enzymes in the skin of human, rat, and pig, the latter, because it is often taken as a model for human skin on grounds of anatomical similarities. However only little is known about drug metabolizing enzymes in pig skin. Interestingly, some cytochromes P450 (CYP) have been observed in the rat skin which are not expressed in the rat liver, such as CYP 2B12 and CYP2D4. As far as investigated most d…

Drugcytochrome P450Swinemedia_common.quotation_subjectMetaboliteAldehyde dehydrogenaseHuman skinEpoxide hydrolaseEsterasechemistry.chemical_compoundOrgan Culture TechniquesCytochrome P-450 Enzyme SystemSpecies SpecificityGlycosyltransferaseAnimalsHumansPharmacology (medical)ratGeneral Pharmacology Toxicology and PharmaceuticsFlavin monooxygenaseCells Culturedmedia_commonSkinchemistry.chemical_classificationquinone reductase [NAD(P)H]biologyintegumentary systemAlcohol dehydrogenaseSulfotransferaseCytochrome P450Aldehyde dehydrogenaseMetabolic Detoxication Phase IIEnzymesRatsGlutathione S-transferaseIsoenzymesEnzymechemistryBiochemistryPharmaceutical PreparationsN-acetyltransferasebiology.proteinMetabolic Detoxication Phase IPig skin drug metabolismDrug metabolismUDP-glucuronosyltransferaseHuman
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Fast Regulation of Cytochrome P450 Activities by Phosphorylation and Consequences for Drug Metabolism and Toxicity

2002

In contrast to the well-known regulation of cytochrome P450 (CYP) activity by enzyme induction, which represents a process with slow onset and slow offset, more recent studies revealed phosphorylation as a fast (within observation instantaneous) and isoenzyme-selective regulation. The phosphorylated enzyme (investigated isozyme: CYP2B1) was fully inactive. The phosphorylation is mediated by PKA and hence under control of hormones and drugs that alter cellular cAMP levels. The consequences for the metabolic control of toxic species derived from drugs and environmental carcinogens are discussed. This information will help to improve therapy with drugs metabolized by CYPs which are phosphoryla…

Drug-Related Side Effects and Adverse ReactionsClinical BiochemistryPharmacologyBiochemistryIsozymeCytochrome P-450 Enzyme SystemCyclic AMPAnimalsHumansDrug InteractionsPhosphorylationEnzyme inducerMolecular BiologyCarcinogenchemistry.chemical_classificationbiologyCytochrome P450Cyclic AMP-Dependent Protein KinasesHormonesIsoenzymesenzymes and coenzymes (carbohydrates)EnzymePharmaceutical PreparationsBiochemistrychemistryCytochrome P-450 CYP2B1ToxicityCarcinogensbiology.proteinPhosphorylationDrug metabolismBiological Chemistry
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Woc (without children) gene control of ecdysone biosynthesis in Drosophila melanogaster.

2001

Abstract The first step in ecdysteroidogenesis, i.e. the 7,8-dehydrogenation of dietary cholesterol (C) to 7-dehydrocholesterol (7dC), is blocked in Drosophila melanogaster homozygous woc (without children) third instar larval ring glands (source of ecdysone). Unlike ring glands from wild-type D. melanogaster larvae, glands from woc mutants cannot convert radiolabelled C or 25-hydroxycholesterol (25C) to 7dC or 7-dehydro-25-hydroxycholesterol (7d25C) in vitro, nor to ecdysone (E). Yet, when these same glands are incubated with synthetic tracer 7d25C, the rate of metabolism of this polar Δ5,7-sterol into E is identical to that observed with glands from comparably staged wild-type larvae. The…

Ecdysoneanimal structuresGenotypemedia_common.quotation_subjectMutantBiochemistryHalloween geneschemistry.chemical_compoundEndocrinologyMelanogasterAnimalsDrosophila ProteinsMetamorphosisMolecular BiologyChromatography High Pressure Liquidmedia_commonEcdysteroidbiologyfungiCytochrome P450BrainEcdysteroidsbiology.organism_classificationMolecular biologyDNA-Binding ProteinsDrosophila melanogasterchemistryBiochemistryGene Expression RegulationLarvaMutationbiology.proteinInsect ProteinsSteroidsDrosophila melanogasterEcdysoneTranscription FactorsMolecular and cellular endocrinology
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Differential sensitivity of rat hepatocyte CYP isoforms to self-generated nitric oxide.

2001

AbstractEarly loss of P450 in rat hepatocyte cultures appears directly related to nitric oxide (NO) overproduction. This study investigates the influence of endogenously generated NO (or NO-derived species) on the relative expression of cytochrome P450 (CYP) isoforms in rat hepatocytes. Our results support the view that loss of P450 holoenzyme in culture is the ultimate consequence of a NO driven process, activated during the common hepatocyte isolation procedure, that leads to an accelerated and selective degradation of specific CYP apoproteins. Under conditions in which NO and peroxynitrite formation is operative, changes in the level of specific CYP isoforms result in a significant alter…

Gene isoformMaleTime FactorsBlotting WesternBiophysicsNitric OxideBiochemistryDexamethasoneNitric oxideRats Sprague-Dawleychemistry.chemical_compoundP450 contentApoenzymesCytochrome P-450 Enzyme Systembeta-NaphthoflavoneStructural BiologyGeneticsmedicineAnimalsInducerOverproductionMolecular BiologyCells CulturedDrug metabolismbiologyCytochrome P450Cell BiologyCytochrome P450 inductionCell biologyRatsIsoenzymesmedicine.anatomical_structureNG-Nitroarginine Methyl EsterBiochemistrychemistryHepatocyteEnzyme Inductionbiology.proteinHepatocytesNitric Oxide SynthaseCytochrome P450 isoformRat hepatocyte cultureHoloenzymesPeroxynitriteDrug metabolismFEBS letters
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Semi-automatic quantitative RT-PCR to measure CYP induction by drugs in human hepatocytes

2003

An assay has been developed for the quantitative measurement of CYP mRNA content of the major human isoforms (1A1, 1A2, 2A6, 2B6, 2C9, 2C19, 2D6, 2E1, 3A4 and 3A5) in human hepatocytes. The method is based on the conversion of mRNAs into their corresponding cDNAs, followed by PCR amplification using appropriate primers. Making use of appropriate internal and external standards it is possible to estimate changes in CYP mRNA content of hepatocytes. The technique has been standardised to run semi-automatically. This procedure can be used to assess the CYP induction potential of new pharmaceuticals at a pre-clinical stage of development. To this aim, human hepatocytes obtained from functional l…

Gene isoformMessenger RNADrug-Related Side Effects and Adverse ReactionsbiologyReverse Transcriptase Polymerase Chain ReactionDrug Evaluation PreclinicalCytochrome P450General MedicineToxicologyIsozymeMolecular biologyReverse transcriptaseXenobioticsReverse transcription polymerase chain reactionReal-time polymerase chain reactionCytochrome P-450 Enzyme SystemBiochemistryEnzyme InductionComplementary DNAHepatocytesbiology.proteinHumansBiological AssayRNA MessengerCells CulturedToxicology in Vitro
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DNA Modification Induced After Metabolic Activation of the Potent Carcinogen Dibenzo[a, l]pyrene in V79 Chinese Hamster Cells Stably Expressing Singl…

2000

Abstract The polycyclic aromatic hydrocarbon (PAH) dibenzo[a, l]pyrene (DB[a, l]P) has been found to be an environmental pollutant and, considering the available data from rodent bioassays, it represents the most carcinogenic member compound of the class of PAH yet discovered. To sort out the contribution of individual cytochromes P450 (P450) in the metabolic activation of this PAH, V79 cells stably expressing a single P450 isoform were treated with DB[a, l]P or enantiomeric DB[a, l]P-11,12-dihydrodiols (diols). Subsequent analysis of the DNA adducts formed revealed substantial differences in the adduct pattern and the total DNA binding depending on the cell line used. Human P450 1B1 effect…

Gene isoformPolymers and PlasticsbiologyChemistryStereochemistryOrganic ChemistryCytochrome P450biology.organism_classificationChinese hamsterAdductchemistry.chemical_compoundCell cultureMaterials Chemistrybiology.proteinPyreneCarcinogenDNAPolycyclic Aromatic Compounds
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Constitutive and inducible expression of CYP enzymes in immortal hepatocytes derived from SV40 transgenic mice

2003

1. The expression of liver-specific transcription factors and cytochrome P450 (CYP) enzymes have been studied in three new hepatocyte-like cell lines derived from SV Delta 202 transgenic mice: AMH-Delta 202 (adult mouse hepatocytes), TAMH-Delta 202 (tumour-derived adult mouse hepatocytes) and NMH-Delta 202 (newborn mouse hepatocytes). 2. mRNA levels of liver-enriched transcription factors such as D-element binding protein (DBP), liver-enriched transcription activating protein (LAP) and the hepatic nuclear factors (HNF) 1, 2 and 3 in all Delta 202 transgenic hepatocyte lines were similar to those in the wild-type liver and in primary mouse hepatocytes. 3. Analysis of basal CYP activities and…

Genetically modified mouseHealth Toxicology and MutagenesisTransgeneGene ExpressionMice TransgenicBiologyHydroxylationToxicologyBiochemistryDexamethasoneCell LineMiceCytochrome P-450 Enzyme SystemGene expressionmedicineAnimalsTestosteroneRNA MessengerTranscription factorPharmacologyEthanolCytochrome P450General MedicineCYP2E1Molecular biologymedicine.anatomical_structureLiverCell cultureEnzyme InductionPhenobarbitalHepatocyteHepatocytesbiology.proteinRifampinMethylcholanthreneTranscription FactorsXenobiotica
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Isoflavonoid-based bone-sparing treatments exert a low activity on reproductive organs and on hepatic metabolism of estradiol in ovariectomized rats

2007

International audience; The use of soy isoflavones is a potential alternative to hormone replacement therapy in post-menopausal bone-loss prevention. Nevertheless, phytoestrogens can target other organs and may disrupt cell proliferation, or could modify endogenous steroid hormone metabolism. These mechanisms could be linked to an increased risk of developing cancer. We therefore studied the possible side effects of such treatments in an experimental model of menopause. Forty adult female Wistar rats were ovariectomized and fed with a genistein-, daidzein- or equol-supplemented diet at bone-sparing levels (10 mg/kg BW/day) for 3 months. The estrogenic effects were assessed by histological a…

GenisteinEstrogen receptorToxicologychemistry.chemical_compound0302 clinical medicineCytochrome P-450 Enzyme SystemBone Density[SDV.IDA]Life Sciences [q-bio]/Food engineeringESTROGEN RECEPTORS0303 health sciencesEstradiolfood and beveragesOrgan SizeEquolGenistein3. Good healthCYTOCHROME P450SOY ISOFLAVONEHormone receptor030220 oncology & carcinogenesisVaginaMicrosomes LiverFemaleMenopauseEQUOLmedicine.medical_specialtymedicine.drug_classOvariectomyPhytoestrogensBiology03 medical and health sciencesProliferating Cell Nuclear AntigenInternal medicinemedicineUTEROTROPHYAnimals[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringRats Wistar030304 developmental biologyPharmacologyUterusDaidzeinIsoflavonesRatsDisease Models AnimalEndocrinologyGene Expression RegulationchemistryEstrogenESTRADIOL METABOLISMOsteoporosisPhytoestrogensSteroid hormone metabolism
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Drug-metabolizing enzyme activities in freshly isolated oval cells and in an established oval cell line from carcinogen-fed rats

1994

The activities of several different phase I and phase II drug-metabolizing enzymes were measured in freshly isolated oval cells from rats fed a choline-deficient/DL-ethionine-supplemented diet for 6 weeks and also in vitro in the established oval cell line OC/CDE 6. No cytochrome P450 was spectrophotometrically measurable in both preparations and two cytochrome P450-dependent monoxygenase activities, aminopyrine N-demethylase and ethoxyresorufin O-deethylase, could not be detected in the oval cells of both sources. However, cytosolic glutathione transferase, microsomal epoxide hydrolase and UDP-glucuronosyltransferase activities were clearly measurable in oval cells. Similar enzyme activiti…

Health Toxicology and MutagenesisBiologyToxicologyCytochrome P-450 Enzyme SystemAnimalsCytotoxic T cellRNA MessengerGlucuronosyltransferaseCells CulturedGlutathione TransferaseEpoxide HydrolasesConfluencyCytochrome P450Cell BiologyRats Inbred F344In vitroDietRatsLiverBiochemistryCell cultureSulfurtransferasesMicrosomal epoxide hydrolaseCarcinogensbiology.proteinMicrosomeDrug metabolismCell Biology and Toxicology
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