Search results for "Steroid 16-alpha-Hydroxylase"

showing 9 items of 9 documents

Re-expression of C/EBP alpha induces CYP2B6, CYP2C9 and CYP2D6 genes in HepG2 cells.

1998

Cytochrome P450 (CYP) activity is very low or even absent in human hepatomas, a phenomenon that is accompanied by low levels of some liver transcription factors, notably C/EBP alpha. To investigate a possible link between this transcription factor and hepatic CYP expression, we have stably transfected HepG2 cells with a C/EBP alpha vector containing a Zn-inducible metallothionein promoter. Expression of functional C/EBP alpha up to liver levels concomitantly increased the mRNAs of several members of the CYP2 family (2B6, 2C9 and 2D6), suggesting that this transcription factor may play a relevant role in controlling the hepatic expression of CYP enzymes.

Carcinoma HepatocellularCYP2B6BiophysicsHepG2 cellTransfectionBiochemistryGene Expression Regulation EnzymologicCytochrome P-450 Enzyme SystemStructural BiologyTumor Cells CulturedGeneticsHumansMetallothioneinRNA MessengerVector (molecular biology)Molecular BiologyTranscription factorGeneCells CulturedCytochrome P-450 CYP2C9biologyChemistryNuclear ProteinsCytochrome P450Oxidoreductases N-DemethylatingCell BiologyTransfectionMolecular biologyDNA-Binding ProteinsCytochrome P-450 CYP2B6C/EBPαCytochrome P-450 CYP2D6Steroid 16-alpha-HydroxylaseHepatocyte nuclear factor 4 alphaEnzyme InductionSteroid HydroxylasesCCAAT-Enhancer-Binding Proteinsbiology.proteinAryl Hydrocarbon HydroxylasesHuman hepatocyteCytochrome P450 gene regulationTranscription Factors
researchProduct

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
researchProduct

Xenobiotic metabolizing enzyme activities and viability are well preserved in EDTA-isolated rat liver parenchymal cells after cryopreservation

1995

Rat liver parenchymal cells (PC) were isolated by EDTA perfusion and were purified by a subsequent Percoll centrifugation. The isolated PC had a viability of 95%, as judged by trypan blue exclusion. Freshly isolated PC were cryopreserved with an optimized protocol in a computer-controlled freezer. After thawing, the PC still retained a viability of 89%. The activities of representative xenobiotic metabolizing enzymes were compared between freshly isolated and cryopreserved PC after thawing. The cytochrome P450 content and the cytochrome P450 2C11 isoenzyme activity, determined by hydroxylation of testosterone in intact cells, were not affected by the cryopreservation. The following phase II…

Epoxide hydrolase 2MalePlating efficiencyLiver cytologyCell Survival10050 Institute of Pharmacology and Toxicology610 Medicine & healthBiologyToxicologyAnimal Testing AlternativesHydroxylationCryopreservationRats Sprague-Dawleychemistry.chemical_compoundCytochrome P-450 Enzyme SystemAnimalsCentrifugationComputer SimulationTestosteroneGlucuronosyltransferaseCells CulturedEdetic AcidGlutathione TransferasePharmacologyCryopreservationEpoxide Hydrolases3005 ToxicologyGlutathioneTrypan BlueMolecular biologyArylsulfotransferaseRats3004 PharmacologychemistryBiochemistryLiverSteroid 16-alpha-HydroxylaseSteroid HydroxylasesCytochromes570 Life sciences; biologyTrypan blueAryl Hydrocarbon HydroxylasesPercoll
researchProduct

Androgen hydroxylation catalysed by a cell line (SD1) that stably expresses rat hepatic cytochrome P-450 PB-4 (IIB1).

1989

Androgen hydroxylation catalysed by Chinese hamster fibroblast SD1 cells, which stably express cytochrome P-450 form PB-4, the rat P450IIB1 gene product, was assessed and compared to that catalysed by purified cytochrome P-450 PB-4 isolated from rat liver. SD1 cell homogenates catalysed the NADPH-dependent hydroxylation of androstenedione and testosterone with a regioselectivity very similar to that purified by P-450 PB-4 (16 beta-hydroxylation/16 alpha-hydroxylation = 6.0-6.8 for androstenedione; 16 beta/16 alpha = 0.9 for testosterone). Homogenates prepared from the parental cell line V79, which does not express detectable levels of P-450 PB-4 or any other cytochrome P-450, exhibited no a…

HemeproteinCytochromemedicine.drug_classBiologyHydroxylationBiochemistryCatalysisCell LineHydroxylationchemistry.chemical_compoundCricetulusCricetinaemedicineAnimalsTestosteroneAndrostenedioneMolecular BiologyAndrostenedioneCytochrome P450Cell BiologyFibroblastsAndrogenRatsBiochemistrychemistryLiverSteroid 16-alpha-HydroxylaseCell cultureSteroid HydroxylasesMicrosomebiology.proteinSteroid 11-beta-HydroxylaseAryl Hydrocarbon HydroxylasesResearch Article
researchProduct

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
researchProduct

Oxidation of tienilic acid by human yeast-expressed cytochromes P-450 2C8, 2C9, 2C18 and 2C19. Evidence that this drug is a mechanism-based inhibitor…

1996

Oxidation of tienilic acid by human cytochromes P-450 (CYP) 2C9, 2C18, 2C8 and 2C19 was studied using recombinant enzymes expressed in yeast. CYP 2C9 was the best catalyst for 5-hydroxylation of tienilic acid (K(m) = 5 +/- 1 microM, kcat = 1.7 +/- 0.2 min-1), 30-fold more potent in terms of kcat/K(m) than CYP 2C18 (K(m) = 150 +/- 15 microM, kcat = 1.8 +/- 0.2 min-1) and 300-fold more potent than CYP 2C8 (K(m) = 145 +/- 15 microM, kcat = 0.2 +/- 0.1 min-1). CYP 2C19 was unable to catalyze this hydroxylation under our experimental conditions. During this study, a marked effect of the ionic strength on the activities (hydroxylations of tienilic acid and tolbutamide) of these cytochromes P-450 …

MaleCytochromeTolbutamideTicrynafenSaccharomyces cerevisiaeurologic and male genital diseasesHydroxylationBiochemistryMixed Function OxygenasesHydroxylationchemistry.chemical_compoundCytochrome P-450 Enzyme SystemMicrosomesmedicineCytochrome P-450 Enzyme InhibitorsHumansheterocyclic compoundsEnzyme InhibitorsCytochrome P-450 Enzyme Inhibitorschemistry.chemical_classificationbiologyChemistryorganic chemicalsMembrane ProteinsGlutathionerespiratory systemRecombinant ProteinsIsoenzymesenzymes and coenzymes (carbohydrates)EnzymeBiochemistrySteroid 16-alpha-HydroxylaseTienilic acidSuicide inhibitionbiology.proteinMicrosomeMicrosomes LiverAryl Hydrocarbon HydroxylasesOxidation-Reductionmedicine.drugEuropean journal of biochemistry
researchProduct

Kinetics of tienilic acid bioactivation and functional generation of drug–protein adducts in intact rat hepatocytes

2005

13 pages; Drug-induced autoimmune hepatitis is among the most severe hepatic idiosyncratic adverse drug reactions. Considered multifactorial, the disease combines immunological and metabolic aspects, the latter being to date much better known. As for many other model drugs, studies on tienilic acid (TA)-induced hepatitis have evidenced the existence of bioactivation during the hepatic oxidation of the drug, allowing the identification of the neoantigen of anti-LKM2 autoantibodies and the pathway responsible for its formation. However, most of these results are based on the use of microsomal fractions whose relevance to the liver in vivo still needs to be established. In the more complex int…

MaleTicrynafen[SDV.BC]Life Sciences [q-bio]/Cellular BiologyAutoimmune hepatitisPlasma protein bindingHydroxylationBiochemistryRats Sprague-Dawley03 medical and health scienceschemistry.chemical_compound0302 clinical medicineIn vivoCYP[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologymedicineAnimalsPrimary cultured hepatocytesTienilic acid[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyCytochrome P450 Family 2[SDV.BC] Life Sciences [q-bio]/Cellular BiologyBiotransformationCells Cultured030304 developmental biologyPharmacologyHepatitis0303 health sciencesDrug bioactivationChemistryGlutathionemedicine.diseaseGlutathioneIn vitroRats3. Good health[SDV.TOX] Life Sciences [q-bio]/Toxicologymedicine.anatomical_structureSteroid 16-alpha-HydroxylaseBiochemistryTienilic acid[SDV.TOX]Life Sciences [q-bio]/Toxicology030220 oncology & carcinogenesisHepatocyteHepatocytesAryl Hydrocarbon HydroxylasesDrug–protein adductsProtein Bindingmedicine.drugBiochemical Pharmacology
researchProduct

Permissive and suppressive effects of dexamethasone on enzyme induction in hepatocyte co-cultures.

2002

1. Steroids are known to act as permissive factors in hepatocytes. This study shows that dexamethasone (DEX) is a permissive factor for induction of CYP2B1/2, CYP3A1, CYP2A1 and probably also CYP2C11 in cultures with primary rat hepatocytes. 2. The induction factor of phenobarbital (PB)-induced formation of 16beta-hydroxytestosterone (OHT), a testosterone biotransformation product predominantly formed by CYP2B1, is increased 18-fold by the addition of 32 nM DEX to the culture medium. Interestingly, higher concentrations of DEX up to 1000 nM led to a concentration-dependent maximally 5-fold decrease (p = 0.002) of phenobarbital-induced 16beta-OHT formation compared with the effect observed w…

Malemedicine.medical_specialtyTime FactorsHealth Toxicology and MutagenesisAnti-Inflammatory AgentsBiologyToxicologyBiochemistryDexamethasoneRats Sprague-DawleyEnzyme activatorInternal medicinepolycyclic compoundsmedicineCytochrome P-450 CYP1A1AnimalsCytochrome P-450 CYP3AProtein IsoformsPermissiveEnzyme inducerCytochrome P450 Family 2DexamethasoneCells CulturedPharmacologyCryopreservationDose-Response Relationship DrugBiological activityGeneral MedicineIn vitroCoculture TechniquesRatsEnzyme ActivationEndocrinologymedicine.anatomical_structureLiverSteroid 16-alpha-HydroxylaseHepatocytePhenobarbitalCytochrome P-450 CYP2B1Steroid Hydroxylasesbiology.proteinHepatocytesHydroxytestosteronesAryl Hydrocarbon HydroxylasesExcitatory Amino Acid Antagonistshormones hormone substitutes and hormone antagonistsGlucocorticoidmedicine.drugXenobiotica; the fate of foreign compounds in biological systems
researchProduct

Estrogen metabolism modulates bone density in men.

2007

Estrogen is a critical hormone for bone homeostasis in men, but no information is available on the role of estrogen metabolism among men. The aim of this study was to evaluate the effect of estrogen hydroxylation on male bone mineral density (BMD). Participants consisted of 61 healthy Caucasian males (mean age 66.6 +/- 1.0 years). Urinary estrogen metabolites were measured by enzyme-linked immunosorbent assay, serum estradiol by ultrasensitive radioimmunoassay, sex hormone binding globulin by radioimmunoassay, and BMD of the lumbar spine and the proximal femur by dual-energy X-ray absorptiometry. Active estrogen metabolites, 16alpha-hydroxyestrone (16alphaOHE(1)) and estriol (E(3)), positiv…

musculoskeletal diseasesMalemedicine.medical_specialtyBone densitymedicine.drug_classEndocrinology Diabetes and MetabolismMotor ActivityHydroxylationArticleBody Mass IndexEndocrinologySex hormone-binding globulinBone DensityInternal medicinemedicineHumansOrthopedics and Sports MedicineFemoral neckAgedBone mineralAged 80 and overbiologyChemistryEstriolEstriolRadioimmunoassayEstrogensMiddle Agedmusculoskeletal systemEndocrinologymedicine.anatomical_structureCross-Sectional StudiesSteroid 16-alpha-HydroxylaseEstrogenbiology.proteinBody mass indexCalcified tissue international
researchProduct