Search results for "substrate"

showing 10 items of 1018 documents

p42 MAPK phosphorylates 80 kDa MARCKS at Ser-113.

1996

Abstract It is demonstrated here that p42 MAPKinase (p42 MAPK) phosphorylates the M yristoylated A lanine- R ich C - K inase S ubstrate (MARCKS) at Ser-113. In permeabilised Swiss 3T3 cells activation of protein kinase C (PKC) leads to p42 MAPK activation, but only the protein kinase C sites in MARCKS become phosphorylated and not Ser-113. The mitogen platelet-derived growth factor (PDGF) elicits the same response. These results demonstrate that while Ser-113 is a substrate for p42 MAPK in vitro and can be phosphorylated in vivo as shown by Taniguchi et al. [(1994) J. Biol. Chem. 269, 18299–18302], its phosphorylation is not subject to acute regulation by p42 MAPK in Swiss 3T3 cells.

MAPK/ERK pathwayMARCKSmedicine.medical_treatmentMitogen-activated protein kinase kinaseBiochemistryenvironment and public healthSubstrate SpecificityMiceStructural BiologySerinep42MAPKinasePhosphorylationMyristoylated Alanine-Rich C Kinase SubstrateCells CulturedProtein Kinase CMitogen-Activated Protein Kinase 1Platelet-Derived Growth FactorbiologyChemistryIntracellular Signaling Peptides and Proteins3T3 CellsProtein-Tyrosine KinasesCell biologyBiochemistryMitogen-activated protein kinasePhosphorylationTetradecanoylphorbol Acetatebiological phenomena cell phenomena and immunityPlatelet-derived growth factor receptorhormones hormone substitutes and hormone antagonistsendocrine systemRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsGeneticsmedicineAnimalsAmino Acid SequenceMARCKSMolecular BiologyProtein kinase CGrowth factorMembrane ProteinsProteinsCell BiologyPeptide FragmentsEnzyme ActivationMolecular Weightenzymes and coenzymes (carbohydrates)Calcium-Calmodulin-Dependent Protein Kinasesbiology.proteinMutagenesis Site-DirectedMitogensFEBS letters
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Effect of oxidative stress on UDP-glucuronosyltransferases in rat astrocytes.

2012

WOS:000309170300003; International audience; The present work reports data regarding effects of an induced oxidative stress on the mainly expressed isoforms of UDP-glucuronosyltransferases (UGTs) in the brain. UGT1A6 and UGT1A7 expression and enzymatic activities toward the 1-naphthol were analyzed in rat cultured astrocytes following the exposure for 48 h to redox-cycling xenobiotic compounds such as quinones and bipyridinium ions. The expression of NADPH:cytochrome P450 reductase and NAD(P)H:quinone oxidoreductase 1 (NQO1) was also investigated. Oxidative stress induced significant deleterious changes in astrocyte morphology, decreased cell viability and inhibited catalytic function of UG…

MESH : Oxidative StressMESH : RNA MessengerAntioxidantTranscription Geneticmedicine.medical_treatmentToxicologyNAD(P)H:quinone oxidoreductase 1MESH: GlucuronosyltransferaseAntioxidantsSubstrate SpecificityRats Sprague-Dawley0302 clinical medicineMESH: NADPH-Ferrihemoprotein ReductaseMESH: GlucuronidesNAD(P)H Dehydrogenase (Quinone)MESH : CatalysisMESH: AnimalsMESH : NAD(P)H Dehydrogenase (Quinone)GlucuronosyltransferaseCells Culturedchemistry.chemical_classificationMESH : Cell Survival0303 health sciencesMESH : Substrate SpecificityMESH : Animals NewbornCytochrome P450 reductaseGeneral MedicineMESH: Cell SurvivalMESH: Pyridinium CompoundsMESH : AntioxidantsMESH: Cells CulturedOxidative phosphorylationGene Expression Regulation EnzymologicMESH : QuinonesMESH : Glucuronides03 medical and health sciencesRNA MessengerCell ShapeNADPH-Ferrihemoprotein ReductaseMESH : Oxidation-ReductionMESH : Pyridinium CompoundsMESH: NaphtholsMESH : GlucuronosyltransferaseMESH: AntioxidantsMESH: CatalysischemistryOxidative stressAstrocytesReactive Oxygen Species030217 neurology & neurosurgeryMESH: Oxidation-ReductionTime Factors[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionMESH : Reactive Oxygen SpeciesNADPH:cytochrome P450 reductasePyridinium CompoundsNaphtholsMESH: Rats Sprague-DawleyProtein oxidationmedicine.disease_causeMESH: Animals NewbornMESH: NAD(P)H Dehydrogenase (Quinone)Protein CarbonylationMESH : OxidantsMESH: OxidantsMelatoninMESH: MelatoninMESH: Oxidative StressMESH : MelatoninMESH : RatsMESH: Gene Expression Regulation EnzymologicQuinonesMESH: Reactive Oxygen SpeciesOxidantsBiochemistryMESH : Protein CarbonylationOxidation-ReductionUDP-glucuronosyltransferaseMESH : Time FactorsMESH: Protein CarbonylationMESH: RatsCell SurvivalMESH : NaphtholsBiologyCatalysisMESH: QuinonesMESH : Gene Expression Regulation EnzymologicGlucuronidesMESH : Cells CulturedmedicineAnimalsMESH: Cell Shape030304 developmental biologyMESH: RNA MessengerReactive oxygen speciesMESH: Transcription GeneticMESH: Time FactorsMESH : AstrocytesMESH : Transcription GeneticNAD(P)H Dehydrogenase (Quinone)MESH : Rats Sprague-DawleyRatsMESH: AstrocytesAnimals NewbornMESH : NADPH-Ferrihemoprotein ReductaseMESH: Substrate SpecificityMESH : AnimalsNAD+ kinaseMESH : Cell Shape[SDV.AEN]Life Sciences [q-bio]/Food and NutritionOxidative stress
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Properties of the F0F1 ATPase Complex from Rhodospirillum rubrum Chromatophores, Solubilized by Triton X-100

1979

1. A cold-stable oligomycin-sensitive F0F1 ATPase complex from chromatophores of Rhodospirillum rubrum FR 1 was solubilized by Triton X-100 and purified by gel filtration. 2. The F0F1 complex is resolved by sodium dodecyl sulfate electrophoresis into 14 polypeptides with approximate molecular weights in the range of 58000--6800; five of these polypeptides are derived from the F1 moiety of the complex which carries the catalytic centers of the enzyme. 3. The purified F0F1 complex is homogeneous according to analytical ultracentrifugation and isoelectric focusing. 4. The molecular weight as determined by gel filtration is about 480 000 +/- 30 000. S020,w is 1.45 +/- 0.1 S and the pI is 5.4. 5…

Macromolecular SubstancesSize-exclusion chromatographyRhodospirillum rubrumBiochemistryPolyethylene GlycolsSubstrate SpecificityDivalentchemistry.chemical_compoundMoietyAmino AcidsSodium dodecyl sulfateAdenosine Triphosphataseschemistry.chemical_classificationChromatographyMolecular massbiologyChemistryIsoelectric focusingRhodospirillum rubrumBacterial Chromatophoresbiology.organism_classificationMolecular WeightKineticsOxidative Phosphorylation Coupling FactorsTriton X-100OligomycinsEuropean Journal of Biochemistry
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Fiber-coupled dielectric-loaded plasmonic waveguides.

2010

Fiber in- and out-coupling of radiation guided by dielectric-loaded surface plasmon-polariton waveguides (DLSPPWs) is realized using intermediate tapered dielectric waveguides. The waveguide structures fabricated by large-scale UV-lithography consist of 1-microm-thick polymer ridges tapered from 10-microm-wide ridges deposited directly on a magnesium fluoride substrate to 1-microm-wide ridges placed on a 50-nm-thick and 100-microm-wide gold stripe. Using fiber-to-fiber transmission measurements at telecom wavelengths, the performance of straight and bent DLSPPWs is characterized demonstrating the overall insertion loss below 24 dB, half of which is attributed to the DLSPPW loss of propagati…

Magnesium fluorideMaterials sciencebusiness.industrySurface plasmonPhotonic integrated circuitSubstrate (electronics)DielectricSurface plasmon polaritonAtomic and Molecular Physics and Opticslaw.inventionchemistry.chemical_compoundOpticschemistrylawInsertion lossbusinessWaveguideOptics express
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Magnetic and magnetoelastic properties of epitaxial (2 1 1)-oriented RFe2 (R=Dy, Tb) thin films

2005

Abstract Epitaxial, (2 1 1)-oriented thin films of RFe 2 (R: rare earth; here: Dy, Tb) were deposited by molecular beam epitaxy on faceted and non-faceted α - Al 2 O 3 ( 1 0 1 ¯ 0 ) (m-plane) substrates utilizing a 15 A thin Fe seed layer and a 500 A Nb buffer layer. Detailed X-ray diffraction analyses revealed a twin-free epitaxial (2 1 1)-oriented growth of buffer layer and film. The magnetostrictive layer RFe 2 , as well as the template layers Nb and Mo exhibited the same crystallographic in-plane orientation with regard to the substrate. The same epitaxial relationship was found for films prepared on faceted and on non-faceted substrates. This implies a coherent crystal overgrowth of th…

MagnetizationCrystallographyMaterials scienceMagnetostrictionSubstrate (electronics)Thin filmCoercivityCondensed Matter PhysicsEpitaxyLayer (electronics)Electronic Optical and Magnetic MaterialsMolecular beam epitaxyJournal of Magnetism and Magnetic Materials
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Elevation of hepatic epoxide hydratase activity by ethoxyquin is due to increased synthesis of the enzyme.

1980

Abstract Feeding of the antioxidant ethoxyquin to rats leads to an increase of epoxide hydratase activity in liver microsomes. The apparent half life of the increase is 3–4 days. Elevation of epoxide hydratase activity is also obtained by intraperitoneal treatment of mice with ethoxyquin. This elevation is prevented by concomitant treatment with cycloheximide. When radiolabelled leucine is incorporated into microsomal protein by liver cell fractions from either ethoxyquin-fed or untreated rats, gel electrophoresis reveals that ethoxyquin feeding increases incorporation into epoxide hydratase. These results suggest that the elevation of epoxide hydratase activity by ethoxyquin is due to incr…

MaleAntioxidantmedicine.medical_treatmentBiophysicsCycloheximideBiochemistrySubstrate Specificitychemistry.chemical_compoundEthoxyquinmedicineAnimalsEnzyme inducerBenzopyrenesCycloheximideMolecular Biologychemistry.chemical_classificationEpoxide HydrolasesEthoxyquinbiologyLiver cellCell BiologyRatsEnzymechemistryBiochemistryEnzyme Inductionbiology.proteinMicrosomeMicrosomes LiverQuinolinesLeucineBiochemical and biophysical research communications
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Intestinal cholesterol absorption: identification of different binding proteins for cholesterol and cholesterol absorption inhibitors in the enterocy…

2003

Absorption of cholesterol from the intestine is a central part of body cholesterol homeostasis. The molecular mechanisms of intestinal cholesterol absorption and the proteins mediating membrane transport are not known. We therefore aimed to identify the proteins involved in intestinal cholesterol absorption across the luminal brush border membrane of small intestinal enterocytes. By photoaffinity labeling using photoreactive derivatives of cholesterol and 2-azetidinone cholesterol absorption inhibitors, an 80-kDa and a 145-kDa integral membrane protein were identified as specific binding proteins for cholesterol and cholesterol absorption inhibitors, respectively, in the brush border membra…

MaleBrush bordermedicine.drug_classBiologyCholesterol 7 alpha-hydroxylaseIntestinal absorptionSubstrate SpecificityCholesterol DietaryEzetimibeIntestine SmallmedicineAnimalsTissue DistributionCholesterol absorption inhibitorMolecular BiologyMicrovilliMolecular StructureAnticholesteremic AgentsReverse cholesterol transportMembrane ProteinsBiological TransportCell BiologyMembrane transportMolecular WeightEnterocytesIntestinal AbsorptionBiochemistryIntestinal cholesterol absorptionlipids (amino acids peptides and proteins)RabbitsCarrier Proteinsmedicine.drugBiochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids
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Regiospecific oxidation of polycyclic aromatic dihydrodiols by rat liver dihydrodiol dehydrogenase

1991

Rat liver dihydrodiol dehydrogenase (DDH, E.C. 1.3.1.20) has recently been shown to oxidize the highly carcinogenic benz[a]anthracene-3,4- dihydrodiol in an NADP(+)-dependent reaction to its corresponding catechol. The present study is a systematic investigation of the substrate specificity of the purified enzyme towards synthetic trans-dihydrodiol metabolites of phenanthrene, benz[a]anthracene, chrysene, dibenz[a, h]anthracene and benzo[a]pyrene. DDH exhibited a remarkable regiospecificity of enzymatic catalysis with regard to the site of the dihydrodiol moiety of the parent hydrocarbon. M-region- and, with lower efficiency, bay-region dihydrodiols were found to be good substrates of the e…

MaleChryseneOxidoreductases Acting on CH-CH Group DonorsAnthraceneStereochemistryMetaboliteGeneral MedicinePhenanthreneToxicologyCatalysisDihydroxydihydrobenzopyrenesRatsSubstrate SpecificityEnzyme catalysisAlcohol OxidoreductasesKineticschemistry.chemical_compoundLiverchemistryBenzo(a)pyrenepolycyclic compoundsAnimalsPyreneOxidoreductasesCarcinogenChemico-Biological Interactions
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CHARACTERIZATION OF MICROSOMAL CYTOCHROME P450-DEPENDENT MONOOXYGENASES IN THE RAT OLFACTORY MUCOSA

2005

Nasal administration of a drug ensures therapeutic action by rapid systemic absorption and/or the entry of some molecules into the brain through different routes. Many recent studies have pointed out the presence of xenobiotic-metabolizing enzymes in rat olfactory mucosa (OM). Nevertheless, very little is known about the precise identity of isoforms of cytochrome P450 (P450)-dependent monooxygenases (P450) and their metabolic function in this tissue. Therefore, we evaluated mRNA expression of 19 P450 isoforms by semiquantitative reverse transcriptase-polymerase chain reaction and measured their microsomal activity toward six model substrates. For purposes of comparison, studies were conduct…

MaleGene isoformPharmaceutical ScienceOlfactionSubstrate SpecificityOlfactory mucosaOlfactory MucosaMicrosomesmedicineAnimalsRNA MessengerEnzyme InhibitorsRats WistarPharmacologychemistry.chemical_classificationbiologyReverse Transcriptase Polymerase Chain ReactionCYP1A2Cytochrome P450MonooxygenaseRatsIsoenzymesKineticsEnzymemedicine.anatomical_structureBiochemistrychemistryMicrosomes Liverbiology.proteinMicrosomeAryl Hydrocarbon HydroxylasesDrug Metabolism and Disposition
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Purification and characterization of rat-liver cytosolic epoxide hydrolase.

1988

Rat liver cytosolic epoxide hydrolase has been purified and characterized. The enzyme was purified from tiadenol-induced rat liver 540-fold with respect to trans-stilbene oxide as a substrate. Similar purification was obtained with the substrates trans-beta-ethyl styrene oxide and styrene 7,8-oxide, the specific activities decreasing in the order trans-beta-ethyl styrene oxide greater than styrene 7,8-oxide greater than trans-stilbene oxide. The enzyme exerts highest activity at pH 7.4 Km and Vmax of the pure enzyme for trans-stilbene oxide were 1.7 microM and 205 nmol x min-1 x mg protein-1 respectively. With trans-stilbene oxide as a substrate, the inhibition by organic solvents (2.5% by …

MaleGuinea PigsBiologyBiochemistryPeptide MappingStyreneSubstrate Specificitychemistry.chemical_compoundMiceCytosolStyrene oxideAnimalsIsoelectric PointEpoxide hydrolasechemistry.chemical_classificationEpoxide HydrolasesMolecular massHydrolysisImmunochemistrySubstrate (chemistry)Rats Inbred StrainsHydrogen-Ion ConcentrationRats Inbred F344RatsMice Inbred C57BLMolecular WeightEnzymechemistryBiochemistryLiverMicrosomal epoxide hydrolaseMicrosomeMicrosomes LiverSolventsPeptide HydrolasesEuropean journal of biochemistry
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