Search results for "Enzyme system"

showing 10 items of 167 documents

Development of new Coumarin-based profluorescent substrates for human cytochrome P450 enzymes

2018

Cytochrome P450 (CYP) enzymes constitute an essential xenobiotic metabolizing system that regulates the elimination of lipophilic compounds from the body. Convenient and affordable assays for CYP enzymes are important for assessing these metabolic pathways.In this study, 10 novel profluorescent coumarin derivatives with various substitutions at carbons 3, 6 and 7 were developed. Molecular modeling indicated that 3-phenylcoumarin offers an excellent scaffold for the development of selective substrate compounds for various human CYP forms, as they could be metabolized to fluorescent 7-hydroxycoumarin derivatives. Oxidation of profluorescent coumarin derivatives to fluorescent metabolites by 1…

Models MolecularentsyymitoxidationHealth Toxicology and MutagenesisToxicology030226 pharmacology & pharmacyBiochemistrycoumarinFluorescence03 medical and health scienceschemistry.chemical_compound0302 clinical medicineCytochrome P-450 Enzyme SystemCoumarinsCYPenzyme kineticsderivativeCytochrome P-450 Enzyme InhibitorsHumansheterocyclic compoundsEnzyme kineticskumariiniCYP2A6ta317Pharmacologychemistry.chemical_classificationBenzoflavonesbiologyChemistryCYP1A2fluoresenssiCytochrome P450substraatit (kemia)General MedicineCoumarindrug metabolismMolecular Docking SimulationMetabolic pathwayKineticsEnzymeBiochemistrylääkekemia030220 oncology & carcinogenesisInactivation Metabolicbiology.proteinMicrosomes LiverOxidation-ReductionDrug metabolism
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Characterization of monoclonal antibodies generated against bovine and porcine prostacyclin synthase and quantitation of bovine prostacyclin synthase

1994

AbstractMonoclonal antibodies were raised against prostacyclin synthases purified from bovine and porcine aortae, respectively. Two monoclonal antibodies, RS1 and RS2, were purified and characterized. As shown by enzyme activity precipitation and Western blot analysis, in solubilized bovine and porcine aortae microsomes the monoclonal antibodies reacted only with prostacyclin synthase. The monoclonal antibody RS1 cross-reacts with partially purified prostacyclin synthase from human umbilical veins in an ELISA-based assay. None of the antibodies inhibited the enzyme activity. By combination of the monoclonal antibody RS2 with a polyclonal antibody we established an enzyme-linked immunosorben…

Monoclonal antibodyUmbilical VeinsSwinemedicine.drug_classProstaglandinBlotting WesternBiophysicsProstaglandinEnzyme-Linked Immunosorbent AssayProstacyclinMonoclonal antibodySensitivity and SpecificityBiochemistryProstacyclin synthasechemistry.chemical_compoundCytochrome P-450 Enzyme SystemWestern blotAntibody SpecificityStructural BiologyMicrosomesGeneticsmedicineAnimalsHumansTissue DistributionIsomerasesMolecular BiologyAortaImmunosorbent Techniquesbiologymedicine.diagnostic_testAntibodies MonoclonalCell BiologyMolecular biologyImmunohistochemistryIntramolecular OxidoreductasesBiochemistrychemistryPolyclonal antibodiesImmunoquantitationProstacyclin synthasebiology.proteinImmunohistochemistryCattleAntibodymedicine.drugFEBS Letters
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Expression and inducibility of drug-metabolizing enzymes in preneoplastic and neoplastic lesions of rat liver during nitrosamine-induced hepatocarcin…

1987

The expression, inducibility, and regulation of four different cytochrome (cyt.) P-450 isoenzymes (PB1, PB2, MC1, and MC2) NADPH-cytochrome P-450 reductase, the glutathione transferases (GSTs) B and C and microsomal epoxide hydrolase (mEHb) have been studied during nitrosamine-induced hepatocarcinogenesis using immunohistochemical techniques. The investigations revealed basic differences in the expression of the individual drug metabolizing enzymes in the course of neoplastic development. While the two GSTs and mEHb were increased in all preneoplastic and benign neoplastic lesions, the levels of the distinct cyt. P-450 isoenzymes were characteristically different from each other. Following …

NitrosaminesCytochromeHealth Toxicology and MutagenesisReductaseToxicologyenvironment and public healthIsozymeMixed Function Oxygenaseschemistry.chemical_compoundLiver Neoplasms ExperimentalCytochrome P-450 Enzyme SystemAnimalsCytochrome P-450 Enzyme InhibitorsAdenosine Triphosphataseschemistry.chemical_classificationbiologyHistocytochemistryImmunochemistryProteinsRats Inbred StrainsGeneral MedicineMolecular biologyRatsenzymes and coenzymes (carbohydrates)Drug metabolizing enzymesEnzymeLiverchemistryBiochemistryNitrosamineEnzyme InductionMicrosomal epoxide hydrolaseembryonic structurescardiovascular systembiology.proteinImmunohistochemistryFemalePrecancerous ConditionsArchives of Toxicology
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Modulation of mutagenicity by phosphorylation of mutagen-metabolizing enzymes.

2004

In this Minireview, we discuss our findings on phosphorylation of cytochromes P450 (CYP) and influence of this modification on metabolic toxification and/or detoxification of a variety of mutagens. We show that phosphorylation drastically interferes with the mutagenicity of several classes of compounds which are of high human relevance (cytostatic drugs of the cyclophosphamide type, aromatic amines/amides, and nitrosamines). We illustrate this by describing the consequences of the stimulation of protein kinase A (with the example of CYP2B1 and CYP2E1), stimulation of protein kinase C, and inhibition of protein phosphatases PP1 and PP2A (with the example of CYP1A1 and CYP1A2). We discuss a p…

NitrosaminesPhosphataseBiophysicsMutagenmacromolecular substancesmedicine.disease_causeenvironment and public healthBiochemistryDimethylnitrosamineCytochrome P-450 Enzyme SystemmedicineSerineAnimalsHumansProtein phosphorylationPhosphorylationProtein kinase AMolecular BiologyProtein kinase CChemistryProtein phosphatase 2CYP2E1EnzymesRatsenzymes and coenzymes (carbohydrates)BiochemistryPhosphorylationMutagensArchives of biochemistry and biophysics
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Fluvoxamine but not sertraline inhibits the metabolism of olanzapine: evidence from a therapeutic drug monitoring service.

2001

Therapeutic drug monitoring data of the new atypical neuroleptic drug olanzapine were used to study interactions with the selective serotonin reuptake inhibitors fluvoxamine and sertraline. The distribution of the ratio of concentration/daily dose (C/D; ng/mL per mg/d) of olanzapine was compared in three groups: patients treated with olanzapine (n = 134), patients treated with olanzapine plus fluvoxamine (n = 10) concomitantly, and patients treated with olanzapine plus sertraline (n = 21) concomitantly. No significant difference was seen between the olanzapine and the olanzapine plus sertraline groups. Patients receiving fluvoxamine in addition to olanzapine had C/D ratios that were in the …

OlanzapineAdultMaleFluvoxaminePharmacologyBenzodiazepinesPharmacokineticsCytochrome P-450 Enzyme SystemSertralineMedicineHumansPharmacology (medical)Drug InteractionsAdverse effectChromatography High Pressure LiquidAgedPharmacologySertralineDepressive Disordermedicine.diagnostic_testbusiness.industryPirenzepineDrug interactionMiddle AgedLiverTherapeutic drug monitoringFluvoxamineOlanzapineAntidepressive Agents Second-GenerationFemaleDrug MonitoringbusinessReuptake inhibitorSelective Serotonin Reuptake Inhibitorsmedicine.drugTherapeutic drug monitoring
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Prediction of paclitaxel resistance in breast cancer: is CYP1B1*3 a new factor of influence?

2008

This article focuses on the recent findings by Marsh and colleagues, and also discusses recent findings with regards to breast cancer. Taxanes are amongst the most active agents in the treatment of breast cancer. However, many tumors are intrinsically resistant. Therefore, it would be an enormous progress, if factors could be identified that reliably differentiate between taxane-sensitive and -resistant patients. Marsh and colleagues analyzed the CYP1B1*3 (Val432Leu) polymorphism in patients with high-risk stage III and IV breast cancer, who received dose-intense paclitaxel in combination with doxorubicin and cyclophosphamide. They report for the first time that patients with two leucine al…

Oncologymedicine.medical_specialtyCyclophosphamidePaclitaxelmedicine.medical_treatmentBreast NeoplasmsDisease-Free Survivalchemistry.chemical_compoundBreast cancerCytochrome P-450 Enzyme SystemInternal medicineGenotypeGeneticsAdjuvant therapyMedicineHumansDoxorubicinProgression-free survivalPharmacologyChemotherapyPolymorphism GeneticDose-Response Relationship Drugbusiness.industrymedicine.diseaseAntineoplastic Agents Phytogenicbody regionsPaclitaxelchemistryDrug Resistance NeoplasmImmunologyCytochrome P-450 CYP1B1Molecular MedicineFemaleAryl Hydrocarbon Hydroxylasesbusinessmedicine.drugPharmacogenomics
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The capacity of liver microsomes to form benzo[a]pyrene-diolepoxide-DNA adducts and induction of cytochrome P450 1A in feral fish exposed to pulp mil…

1996

An investigation was made of cytochrome P4501A (CYP1A) induction, determined by the activity of EROD (7-ethoxyresorufin O-deethylase), and formation of benzo[a]pyrene-diolepoxide-DNA (BPDE-DNA) adducts, measured by synchronous fluorescence spectrophotometry, in liver microsomes of perch (Perca fluviatilis), bream (Abramis brama), and roach (Rutilus rutilus). Fish were collected from the southern part of Lake Saimaa (Finland), an area polluted by effluents from the pulp and paper industry. In addition, two conjugation enzymes (UDP-glucuronosyltransferase and glutathione S-transferase) were determined. Overall, when compared to an upstream reference, EROD activity was higher in fish at waters…

PaperHealth Toxicology and MutagenesisIndustrial WasteBiologyToxicologychemistry.chemical_compoundDNA AdductsCytochrome P-450 Enzyme SystemBenzo(a)pyreneCytochrome P-450 CYP1A1EcotoxicologyAnimalsBenzopyrenesCarcinogenBiotransformationFinlandPublic Health Environmental and Occupational HealthFishesCytochrome P450General MedicineGlutathionebiology.organism_classificationPollutionchemistryBenzo(a)pyreneEnvironmental chemistryBenzopyreneMicrosomebiology.proteinMicrosomes LiverRutilusWater Pollutants ChemicalEcotoxicology and environmental safety
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An update on metabolism studies using human hepatocytes in primary culture

2008

Background: Cultured human hepatocytes are the closest in vitro model to human liver and constitute a very predictive model for drug metabolism in vivo. The variability observed in human hepatocytes reflects the existing phenotypic heterogeneity of cytochrome P450 expression in human liver. Objectives: As drug metabolism is the major source of pharmacokinetic variability in human beings, the main areas of current drug metabolism research in human hepatocytes are reviewed. Methods: To speed up the selection of drug candidates, the evaluation of metabolic stability, metabolite profiling and identification, and drug–drug interaction potential are key issues in drug development. Results/conclus…

PharmacologyDrugbiologyMechanism (biology)media_common.quotation_subjectCytochrome P450General MedicinePharmacologyToxicologyIn vitroCytochrome P-450 Enzyme SystemPharmaceutical PreparationsPharmacokineticsDrug developmentIn vivoEnzyme InductionHepatocytesbiology.proteinAnimalsCytochrome P-450 Enzyme InhibitorsHumansEnzyme InhibitorsCells CulturedDrug metabolismmedia_commonExpert Opinion on Drug Metabolism & Toxicology
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Experiments on the metyrapone reducing microsomal enzyme system.

1970

The formation of reduced metyrapone [2-methyl-1.2-bis-(3-pyridyl)-1-propanol] from metyrapone [2-methyl-1.2-bis-(3-pyridyl)-1-propanone] in the liver has been studied. Reduced metyrapone appeared as the main metabolite of metyrapone in the isolated perfused rat liver. Experiments on the intracellular distribution of the metyrapone reducing activity revealed that metyrapone reductase is mainly localized in the microsomal fraction. In the 105,000 × g supernatant only a little activity was found.

PharmacologyMetyrapone reductasemedicine.medical_specialtyMetyraponeChemistryMetaboliteGeneral Medicinechemistry.chemical_compoundEndocrinologyEnzyme systemInternal medicineRat livermedicineMicrosomeAnimalsChromatography Thin LayerIntracellularDrug metabolismmedicine.drugNaunyn-Schmiedebergs Archiv fur Pharmakologie
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Transcriptional regulation and expression of CYP3A4 in hepatocytes.

2007

CYP3A4 is the most abundantly expressed drug-metabolizing P450 enzyme in human liver and contributes to the metabolism of a large number of drugs in use today. CYP3A4 is constitutively expressed in adult hepatocytes but it can also be transcriptionally induced by a variety of structurally diverse xenochemicals. CYP3A4 strongly contributes to the important variability in the therapeutic and toxic effects of drugs owing to the major role it plays in xenobiotic metabolism and the large intra- and inter-individual variability to which it is subjected. The functional examination of up to 13 kb of the CYP3A4 5'-flanking region has revealed that the regulation of this gene is a complex issue, with…

PharmacologyRegulation of gene expressionPregnane X receptorTranscription GeneticClinical BiochemistryDown-RegulationBiologyPharmacologyRegulatory Sequences Nucleic AcidGene Expression Regulation EnzymologicCell biologyDrug developmentNuclear receptorCytochrome P-450 Enzyme SystemLiverRegulatory sequenceTranscriptional regulationHepatocytesAnimalsCytochrome P-450 CYP3AHumansTranscription factorDrug metabolismCurrent drug metabolism
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