Search results for "Enzyme system"

showing 7 items of 167 documents

Effects of steatosis on drug-metabolizing capability of primary human hepatocytes.

2007

Abstract The suitability of liver grafts discarded for transplantation because of macrosteatosis for preparing human hepatocyte cultures for in vitro drug metabolism studies has been examined. Lower cell viability and yield of isolation procedure were obtained from fatty livers (>40% steatosis) with respect to normal tissue. Significant reductions in 7-ethoxycoumarin O-deethylation (ECOD) and testosterone oxidations were found in hepatocytes prepared from steatotic livers. The potential impact of lipid accumulation on P450 enzymes was studied in vitro by incubation of cultured hepatocytes with long chain free fatty acids (FFA). Treatment of cells with 0.25–3 mM FFA induced dose-dependent ac…

medicine.medical_specialtyCYP3A4CYP1A2General MedicineBiologyCYP2E1Fatty Acids NonesterifiedToxicologymedicine.diseaseTransplantationFatty LiverEndocrinologymedicine.anatomical_structureCytochrome P-450 Enzyme SystemInternal medicineHepatocytemedicineHepatocytesHumansTestosteroneViability assaySteatosisOxidation-ReductionDrug metabolismCells CulturedToxicology in vitro : an international journal published in association with BIBRA
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18-hydroxylation in the Y-1 adrenal cell line: response to ACTH and to culture conditions.

1992

The 18-hydroxylation of deoxycorticosterone in the Y-1 adrenal cell line was studied under various incubation and cell culture conditions and compared to 11 beta-hydroxylation. Repeated incubation of the substrate increased both 18- and 11 beta-hydroxylation in the Y-1 cells. Furthermore, both 18- and 11 beta-hydroxylation were increased with increased serum concentration and prolonged incubation time. While the increase in 11 beta-hydroxylation seemed to be independent of the type of serum, 18-hydroxylation was much more important in cells cultured in fetal or newborn calf serum supplemented medium than in those cultured in horse serum supplemented medium. As expected, ACTH treatment incre…

medicine.medical_specialtyCytochromeEndocrinology Diabetes and Metabolismmedicine.medical_treatmentClinical BiochemistryHydroxylationBiochemistryHydroxylationchemistry.chemical_compoundMiceEndocrinologyAdrenocorticotropic HormoneCytochrome P-450 Enzyme SystemInternal medicineAdrenal GlandsmedicineAnimalsCytochrome P-450 CYP11B2DesoxycorticosteroneMolecular BiologyIncubationCells CulturedFetusbiologyDose-Response Relationship DrugSubstrate (chemistry)Cell BiologyFetal BloodIn vitroCulture MediaSteroid hormoneEndocrinologyBloodchemistryCell cultureSteroid Hydroxylasesbiology.proteinMolecular MedicineSteroid 11-beta-HydroxylaseThe Journal of steroid biochemistry and molecular biology
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Pentobarbital-sensitive EDHF comediates ACh-induced arteriolar dilation in the hamster microcirculation

1999

It is unclear to what extent the endothelium-derived hyperpolarizing factor (EDHF) contributes to the control of microcirculatory blood flow in vivo. We analyzed, by intravital microscopy in hamster muscles, the potential role of EDHF along the vascular tree under stimulated (ACh) or basal conditions. Experiments were performed in conscious as well as anesthetized (pentobarbital, urethan) animals. Additionally, cellular effects of the potential EDHF were studied in isolated small arteries. In pentobarbital-anesthetized animals, treatment with N ω-nitro-l-arginine (l-NNA; 30 μmol/l) and indomethacin (3 μmol/l) reduced the dilation in response to 10 μmol/l ACh from 60 ± 6 to 20 ± 4%. This ni…

medicine.medical_specialtyPentobarbitalEndothelium-derived hyperpolarizing factorPotassium ChannelsCharybdotoxinPhysiologyVasodilator AgentsIndomethacinHamsterVasodilationNitroarginineMuscle Smooth VascularMicrocirculationGlibenclamideBiological FactorsCytochrome P-450 Enzyme SystemArterioleCricetinaePhysiology (medical)Internal medicinemedicine.arterymedicineAnimalsCyclooxygenase InhibitorsMuscle SkeletalPentobarbitalSkinMesocricetusChemistryMicrocirculationPenicillamineAcetylcholineArteriolesEndocrinologyAnesthesiaFatty Acids UnsaturatedPotassiumEndothelium VascularCardiology and Cardiovascular MedicineIntravital microscopyAdjuvants Anesthesiamedicine.drugAmerican Journal of Physiology-Heart and Circulatory Physiology
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Progestogens reduce thromboxane production by cultured human endothelial cells.

2011

Objectives Progestogens have been poorly studied concerning their roles in endothelial physiology. Prostanoids are vasoactive compounds, such as thromboxane A2, a potent vasoconstrictor, and prostacyclin, a vasodilator. We examined the effects of two progestogens used clinically, progesterone and medroxyprogesterone acetate, on thromboxane A2 production by cultured human umbilical vein endothelial cells (HUVEC) and investigated the role of progesterone receptors and the enzymes involved in production of thromboxane A2 and prostacyclin. Methods Cells were exposed to 1‐100 nmol/l of either progesterone or medroxyprogesterone acetate, and thromboxane A2 production was measured in culture mediu…

medicine.medical_specialtyUmbilical VeinsAntineoplastic Agents HormonalThromboxaneBlotting WesternGene ExpressionProstacyclinMedroxyprogesterone AcetatePolymerase Chain ReactionProstacyclin synthaseThromboxane receptorThromboxane ProductionThromboxane A2chemistry.chemical_compoundThromboxane A2Hormone AntagonistsCytochrome P-450 Enzyme SystemInternal medicineProgesterone receptorMedicineHumansCyclooxygenase InhibitorsRNA MessengerCells CulturedProgesteronebiologyDose-Response Relationship Drugbusiness.industryObstetrics and GynecologyEndothelial CellsGeneral MedicineIntramolecular OxidoreductasesThromboxane B2MifepristoneEndocrinologychemistrycardiovascular systembiology.proteinPyrazolesThromboxane-A synthaseThromboxane-A SynthaseProgestinsbusinessmedicine.drugClimacteric : the journal of the International Menopause Society
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Regulation of cytochrome P450 IID by acute phase mediators in C3H/HeJ mice.

1992

Abstract Cytochrome P450 IID6 is a drug metabolizing enzyme and the major target antigen in LKM-1 antibody positive chronic active hepatitis. The histological hallmark of chronic active hepatitis is a lymphocytic infiltrate in the liver. It is unknown whether and how cytokines produced and secreted by these tissue infiltrating mononuclear cells regulate the cellular expression of cytochrome P450 IID6. To study the effect of interleukin 1, tumor necrosis factor and interleukin 6 on the hepatocellular RNA expression of cytochrome P450 IID, we injected each of the cytokines in C3H HeJ mice. We found a time-dependent suppression of the cytochrome in the liver. Six hours after the intraperitonea…

medicine.medical_treatmentIntraperitoneal injectionBiophysicsBiochemistryMixed Function OxygenasesMiceCytochrome P-450 Enzyme SystemmedicineEscherichia coliAnimalsHumansInterleukin 6Molecular BiologyHepatitisMice Inbred C3HbiologyInterleukin-6Tumor Necrosis Factor-alphaCytochrome P450InterleukinCell Biologymedicine.diseaseBlotting NorthernRecombinant ProteinsEndotoxinsCytokineCytochrome P-450 CYP2D6LiverImmunologybiology.proteinRNATumor necrosis factor alphaFemaleAntibodyInterleukin-1Biochemical and biophysical research communications
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Degradation of an alkaloid pheromone from the pale-brown chafer, Phyllopertha diversa (Coleoptera: Scarabaeidae), by an insect olfactory cytochrome P…

1999

AbstractThe pale-brown chafer, Phyllopertha diversa, utilizes an unusual alkaloid, 1,3-dimethyl-2,4-(1H,3H)-quinazolinedione, as its sex pheromone. This compound is rapidly degraded in vitro by the antennal protein extracts from this scarab beetle. Demethylation at the N-1 position and hydroxylation of the aromatic ring have been identified as the major catabolic pathways. The enzyme responsible for the pheromone degradation is membrane-bound, requires NAD(P)H for activity and is sensitive to cytochrome P450 inhibitors, such as proadifen and metyrapone. The ability to metabolize this unusual pheromone was not detected in 12 species tested, indicating that the P450 system, specific to male P…

pheromone-degrading enzymemedia_common.quotation_subjectBiophysicsInsectOlfactionscarab beetleBiochemistryMass SpectrometryHydroxylationchemistry.chemical_compoundAlkaloidsCytochrome P-450 Enzyme SystemStructural BiologyMicrosomesBotanyGeneticsAnimalsCytochrome P-450 Enzyme InhibitorsEnzyme InhibitorsSex AttractantsMolecular BiologyChromatography High Pressure LiquidDemethylationmedia_commonbiologyMolecular StructureProadifenCytochrome P450Cell BiologyMetyraponeProadifenColeopteraBiochemistrychemistrySex pheromonebiology.proteinQuinazolinesPheromoneInsect ProteinsChromatography Thin Layerpheromone inactivationolfactionFEBS letters
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Protein tyrosine nitration and thiol oxidation by peroxynitrite-strategies to prevent these oxidative modifications.

2013

The reaction product of nitric oxide and superoxide, peroxynitrite, is a potent biological oxidant. The most important oxidative protein modifications described for peroxynitrite are cysteine-thiol oxidation and tyrosine nitration. We have previously demonstrated that intrinsic heme-thiolate (P450)-dependent enzymatic catalysis increases the nitration of tyrosine 430 in prostacyclin synthase and results in loss of activity which contributes to endothelial dysfunction. We here report the sensitive peroxynitrite-dependent nitration of an over-expressed and partially purified human prostacyclin synthase (3.3 μM) with an EC50 value of 5 μM. Microsomal thiols in these preparations effectively co…

thiol oxidationprotein tyrosine nitrationlcsh:Chemistrychemistry.chemical_compoundCytochrome P-450 Enzyme SystemSf9 CellsTyrosinelcsh:QH301-705.5Spectroscopychemistry.chemical_classification0303 health sciencesbiologySuperoxide030302 biochemistry & molecular biologyGeneral MedicineComputer Science ApplicationsIntramolecular OxidoreductasesBiochemistryThiolprostacyclin synthasesuperoxideOxidation-ReductionPeroxynitriteOxidative phosphorylationSpodopteraCatalysisArticleperoxynitriteNitric oxideProstacyclin synthaseInorganic Chemistry03 medical and health sciencesnitric oxideddc:570NitrationPeroxynitrous AcidAnimalsHumansSulfhydryl CompoundsPhysical and Theoretical ChemistryMolecular Biology030304 developmental biologyOrganic Chemistrynitric oxide; superoxide; peroxynitrite; protein tyrosine nitration; thiol oxidation; peroxynitrite scavengers; prostacyclin synthasechemistrylcsh:Biology (General)lcsh:QD1-999biology.proteinTyrosineCattleperoxynitrite scavengersProtein Processing Post-TranslationalInternational journal of molecular sciences
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