Search results for " P4"

showing 10 items of 151 documents

Biotransformation of methylxanthines in mammalian cell lines genetically engineered for expression of single cytochrome P450 isoforms. Allocation of …

1993

V79 Chinese hamster cells genetically engineered for stable expression of single forms of rat cytochromes P450IA1, P450IA2, P450IIB1, human P450IA2, and rat liver epithelial cells expressing murine P450IA2 were used to allocate metabolic pathways of methylxanthines to specific isoforms and to test the suitability of such cell lines for investigations on drug interactions occurring at the cytochrome expressed. The cell lines were exposed to caffeine and/or theophylline and concentrations of metabolites formed in the medium were determined by HPLC. Caffeine was metabolized by human, rat and murine P450IA2, resulting in the formation of four primary demethylated and hydroxylated metabolites. H…

CytochromeToxicologyCell Linechemistry.chemical_compoundCricetulusCytochrome P-450 Enzyme SystemIn vivoCaffeineCricetinaemedicineAnimalsHumansTheophyllineBiotransformationChromatography High Pressure LiquidbiologyCytochrome P450PefloxacinPipemidic AcidRatsIsoenzymesMetabolic pathwayBiochemistrychemistryCell cultureMicrosomebiology.proteinQuinolinesCaffeinemedicine.drugToxicology
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Cytochrome c is released in a single step during apoptosis

2005

Release of cytochrome c from mitochondria is a central event in apoptotic signaling. In this study, we utilized a cytochrome c fusion that binds fluorescent biarsenical ligands (cytochrome c-4CYS (cyt. c-4CYS)) as well as cytochrome c-green fluorescent protein (cyt. c-GFP) to measure its release from mitochondria in different cell types during apoptosis. In single cells, the kinetics of cyt. c-4CYS release was indistinguishable from that of cyt. c-GFP in apoptotic cells expressing both molecules. Lowering the temperature by 7 degrees C did not affect this corelease, but further separated cytochrome c release from the subsequent decrease in mitochondrial membrane potential (DeltaPsi(m)). Cyt…

CytochromeUltraviolet RaysGreen Fluorescent ProteinsApoptosisLigandsMembrane PotentialsJurkat CellsCytochrome C1HumansCytochrome c oxidaseEnzyme InhibitorsMolecular BiologyProtein Synthesis InhibitorsMicroscopy VideobiologyTumor Necrosis Factor-alphaCytochrome bCytochrome cTemperatureCytochromes cCytochrome P450 reductaseCell BiologyStaurosporineMitochondriaCell biologyKineticsenzymes and coenzymes (carbohydrates)Coenzyme Q – cytochrome c reductaseDactinomycinbiology.proteinApoptosomeBiomarkersHeLa CellsCell Death & Differentiation
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Hepatic metabolism of diclofenac: role of human CYP in the minor oxidative pathways.

1999

The aim of this study was to re-examine the human hepatic metabolism of diclofenac, with special focus on the generation of minor hydroxylated metabolites implicated in the idiosyncratic hepatotoxicity of the drug. Different experimental approaches were used: human hepatocytes, human microsomes, and engineered cells expressing single human CYP (cytochromes P450). Human hepatocytes formed 3'-hydroxy-, 4'-hydroxy-, 5-hydroxy- 4',5-dihydroxy-, and N,5-dihydroxydiclofenac, as well as several lactams. Formation of 4'- and 5-hydroxydiclofenac by human liver microsomes followed a Michaelis-Menten kinetics (Km 9 +/- 1 microM; Vmax 432 +/- 15 pmol/min/mg and Km 43 +/- 5 microM; and Vmax 15.4 +/- 0.6…

DiclofenacMetaboliteIn Vitro TechniquesBiochemistryCell LineHydroxylationCytochrome P-450 CYP2C8chemistry.chemical_compoundTolbutamideCytochrome P-450 Enzyme SystemmedicineHumansBiotransformationCytochrome P-450 CYP2C9PharmacologybiologyAnti-Inflammatory Agents Non-SteroidalCytochrome P450Metabolismmedicine.anatomical_structureBiochemistrychemistrySteroid 16-alpha-HydroxylaseHepatocyteSteroid HydroxylasesMicrosomebiology.proteinMicrosomes LiverAryl Hydrocarbon HydroxylasesOxidation-ReductionDrug metabolismmedicine.drug
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The Influence of Single-Dose and Short-Term Administration of Quercetin on the Pharmacokinetics of Midazolam in Humans.

2015

Quercetin is a plant flavonol that is available from both daily diet and nutraceuticals. To investigate the effect of acute and short-term intake of high-dose quercetin on CYP3A-mediated metabolism, 10 healthy volunteers received 7.5 mg oral midazolam without, with a single dose of 1500 mg quercetin and after 1-week supplementation with 1500 mg quercetin daily. A substudy was performed in three subjects to explore the impact of repeated quercetin intake on intravenously administered midazolam. Coadministration with a single dose of quercetin did not significantly alter the pharmacokinetics of midazolam and its 1'-hydroxymetabolite, but following short-term quercetin intake, there was a tren…

DrugAdultMalemedia_common.quotation_subjectMidazolamPharmaceutical ScienceAdministration OralPharmacologychemistry.chemical_compoundPharmacokineticsmedicineCytochrome P-450 CYP3AHumansheterocyclic compoundsDrug InteractionsAdverse effectmedia_commonCross-Over StudiesbiologyCytochrome P450MetabolismBioavailabilitychemistryArea Under Curvebiology.proteinMidazolamAdministration IntravenousFemaleQuercetinQuercetinmedicine.drugJournal of pharmaceutical sciences
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Hepatocytes--the choice to investigate drug metabolism and toxicity in man: in vitro variability as a reflection of in vivo.

2007

The pharmaceutical industry is committed to marketing safer drugs with fewer side effects, predictable pharmacokinetic properties and quantifiable drug-drug interactions. Drug metabolism is a major determinant of drug clearance and interindividual pharmacokinetic differences, and an indirect determinant of the clinical efficacy and toxicity of drugs. Progressive advances in the knowledge of metabolic routes and enzymes responsible for drug biotransformation have contributed to understanding the great metabolic variations existing in human beings. Phenotypic as well genotypic differences in the expression of the enzymes involved in drug metabolism are the main causes of this variability. How…

DrugDiclofenacDrug-Related Side Effects and Adverse Reactionsmedia_common.quotation_subjectBiologyPharmacologyIn Vitro TechniquesToxicologyModels BiologicalPharmacokineticsCytochrome P-450 Enzyme SystemIn vivoGenetic variationHumansDrug InteractionsPharmacokineticsBiotransformationCells Culturedmedia_commonMolecular StructureAnti-Inflammatory Agents Non-SteroidalCytochrome P450Genetic VariationGeneral MedicineIn vitroPharmaceutical PreparationsToxicityInactivation Metabolicbiology.proteinHepatocytesDrug metabolismMetabolic Networks and PathwaysChemico-biological interactions
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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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