Search results for "Transferase"

showing 10 items of 1030 documents

PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163

1996

AbstractThe 80kDa Myristolated Alanine-Rich C-Kinase Substrate (MARCKS) in a major in vivo substrate of protein kinase C (PKC). Here we report that MARCKS is a major substrate for the lipid-activated PKC-related kinase (PRK1) in cell extracts. Furthermore, PRK1 is shown to phosphorylate MARCKS on the same sites as PKC in vitro. Thus, control of MARCKS phosphorylation on these previously identified ‘PKC’ sites may be regulated under certain circumstances by PRK as well as PKC mediated signalling pathways. The implications for MARCKS as a marker of PKC activation and as a point of signal convergence are discussed.

PhosphopeptidesMARCKSPRKRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsKidneyBiochemistryCell-free systemCell LineSerineStructural BiologyProtein kinase CGeneticsAnimalsAmino Acid SequenceBinding siteMARCKSPKCPhosphorylationMyristoylated Alanine-Rich C Kinase SubstrateMolecular BiologyProtein kinase CGlutathione TransferaseBinding SitesCell-Free SystemKinaseChemistryIntracellular Signaling Peptides and ProteinsMembrane ProteinsProteinsCell BiologyHaplorhiniPeptide FragmentsBiochemistryPhosphorylationElectrophoresis Polyacrylamide GelSignal transductionSequence AnalysisSignal TransductionFEBS Letters
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Release of Hypoacetylated and Trimethylated Histone H4 Is an Epigenetic Marker of Early Apoptosis

2006

11 p.-5 fig.-1 fig. supl.

PhysiologyFisiologiaHL-60 CellsApoptosisDNA FragmentationBiologyBiochemistryHistonesHistone H4Jurkat CellsHistone H1HeterochromatinHistone methylationHistone H2AHumansHistone codeCancer epigeneticsMolecular BiologyEpigenomicsApoptosiDNACell BiologyMetabolismeMetabolismHistone methyltransferaseCancer researchBiomarkersJournal of Biological Chemistry
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The depletion of nuclear glutathione impairs cell proliferation in 3t3 fibroblasts.

2009

BACKGROUND:Glutathione is considered essential for survival in mammalian cells and yeast but not in prokaryotic cells. The presence of a nuclear pool of glutathione has been demonstrated but its role in cellular proliferation and differentiation is still a matter of debate. PRINCIPAL FINDINGS:We have studied proliferation of 3T3 fibroblasts for a period of 5 days. Cells were treated with two well known depleting agents, diethyl maleate (DEM) and buthionine sulfoximine (BSO), and the cellular and nuclear glutathione levels were assessed by analytical and confocal microscopic techniques, respectively. Both agents decreased total cellular glutathione although depletion by BSO was more sustaine…

PhysiologyGlutathione reductaseCell Biology/Cell Growth and Divisionlcsh:MedicineBiology3T3 cellschemistry.chemical_compoundMicemedicineBiochemistry/Cell Signaling and Trafficking StructuresAnimalsButhionine sulfoximinelcsh:ScienceTranscription factorButhionine SulfoximineCell ProliferationGlutathione TransferaseCell NucleusMultidisciplinaryMicroscopy ConfocalCell growthlcsh:RMaleatesGlutathione3T3 CellsFibroblastsMolecular biologyGlutathioneCell biologyCell nucleusmedicine.anatomical_structureGlutathione ReductasechemistryCytoplasmlcsh:QResearch ArticlePloS one
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Separation by FPLC chromatofocusing of UDP-glucosyltransferases from three developmental stages of Drosophila melanogaster.

1997

Variation of UDP-glucosyltransferase activity, during Drosophila melanogaster development, was analyzed. The endogenous metabolite xanthurenic acid and the xenobiotic compounds 1-naphthol and 2-naphthol were used as substrates. Developmentally regulated differences were observed for the three substrates, suggesting the presence of UDP-glucosyltransferase isoenzymes. This was further confirmed by FPLC chromatofocusing on a Mono P column: seven peaks of UDP-glucosyltransferase activity (pHs: ≥6.3, 5.8, 5.5, 4.9, 4.5, 4.2, ≤4.0) with either single or overlapping substrate specificity were detected. A single xanthurenic acid:UDP-glucosyltransferase activity (pl 5.8) was found throughout develop…

PhysiologyMetaboliteOvipositionBiochemistryIsozymeGene Expression Regulation EnzymologicSubstrate Specificitychemistry.chemical_compoundGlucosyltransferasesAnimalsXanthurenic acidChromatography High Pressure LiquidbiologyChromatofocusingGene Expression Regulation DevelopmentalFast protein liquid chromatographyGeneral Medicinebiology.organism_classificationIsoenzymesDrosophila melanogasterchemistryBiochemistryGlucosyltransferasesInsect ScienceChromatography GelFemaleDrosophila melanogasterXenobioticArchives of insect biochemistry and physiology
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6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase from frog skeletal muscle: purification, kinetics and immunological properties.

1993

Fructose 2,6-bisphosphate is the most potent activator of 6-phosphofructo-1-kinase, a key regulatory enzyme of glycolysis in animal tissues. This study was prompted by the finding that the content of fructose 2,6-bisphosphate in frog skeletal muscle was dramatically increased at the initiation of exercise and was closely correlated with the glycolytic flux during exercise. 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, the enzyme system catalyzing the synthesis and degradation of fructose 2,6-bisphosphate, was purified from frog (Rana esculenta) skeletal muscle and its properties were compared with those of the rat muscle type enzyme expressed in Escherichia coli using recombinant DN…

PhysiologyPhosphofructokinase-2BiologyBiochemistrychemistry.chemical_compoundEndocrinologymedicineFructosediphosphatesAnimalsGlycolysisPhosphorylationEcology Evolution Behavior and Systematicschemistry.chemical_classificationMolecular massImmunochemistryMusclesPhosphotransferasesSkeletal muscleRana esculentaFructoseHydrogen-Ion ConcentrationMolecular WeightKineticsmedicine.anatomical_structureEnzymechemistryFructose 26-bisphosphateBiochemistryGRENOUILLEAnimal Science and ZoologyPhosphoenolpyruvate carboxykinaseProtein KinasesJournal of comparative physiology. B, Biochemical, systemic, and environmental physiology
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Xyloglucan endotransglucosylase/hydrolases (XTHs) during tomato fruit growth and ripening

2009

Abstract: Depolymerization of cell watt xyloglucan has been proposed to be involved in tomato fruit softening, along with the xyloglucan modifying enzymes. Xyloglucan endo-transgtucosylase/hydrolases (XTHs: EC 2.4.1.207 and/or EC 3.2.1.151) have been proposed to have a dual role integrating newly secreted xyloglucan chains into an existing watt-bound xyloglucan, or restructuring the existing cell watt material by catalyzing transglucosylation between previously wall-bound xyloglucan molecules. Here, 10 tomato (Solanum lycopersicum) SIXTHs were studied and grouped into three phylogenetic groups to determine which members of each family were expressed during fruit growth and fruit ripening, a…

PhysiologyPlant ScienceCell wallchemistry.chemical_compoundSolanum lycopersicumGene Expression Regulation PlantHemicelluloseBiologyPhylogenybiologyReverse Transcriptase Polymerase Chain ReactionComputational BiologyGlycosyltransferasesfood and beveragesPlant physiologyRipeningEthylenesXyloglucan endotransglucosylasebiology.organism_classificationXyloglucanHorticulturechemistryBiochemistryFruitSolanumAgronomy and Crop ScienceSolanaceaeJournal of Plant Physiology
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Detection of a plant enzyme exhibiting chlorogenate-dependant caffeoyltransferase activity in methanolic extracts of arbuscular mycorrhizal tomato ro…

2012

When Glomus intraradices-colonised tomato roots were extracted in methanol at 6 degrees C, chlorogenic acid (5-caffeoylquinic acid), naturally present in the extract, was slowly converted by transesterification into methyl caffeate. The progress of the reaction could be monitored by HPLC. The reaction only occurred when the ground roots were left in contact with the hydro-alcoholic extract and required the presence of 15-35% water in the mixture. When the roots were extracted in ethanol, chlorogenic acid was transformed to ethyl caffeate in the same conditions. The reaction was also detected in Glomus mosseae-colonised tomato root extracts. It was also detectable in non-mycorrhizal root ext…

Physiology[SDV]Life Sciences [q-bio]Arbuscular mycorrhizal fungiPlant SciencePlant RootsSubstrate SpecificityACBIOSYNTHESISchemistry.chemical_compoundTRANSFERASESolanum lycopersicumMycorrhizaeMethyl caffeateSWEET-POTATO ROOTSFood scienceEnzyme InhibitorsGlomusChromatography High Pressure LiquidPlant ProteinsbiologyTemperaturePlant physiologyfood and beveragesChlorogenic acidBiochemistryFUNGUSCOFFEE[SDE]Environmental SciencesGENESMETABOLISMCaffeoyltransferaseTomatoCaffeic AcidsChlorogenic acidTransferasesGenetics[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyEnzyme AssaysEthanolEsterificationPlant ExtractsfungiEthyl caffeatePlant Components Aerialbiology.organism_classificationRootsEnzyme assayEnzyme ActivationPhenylmethylsulfonyl FluorideTransesterificationchemistrybiology.proteinMethanolCAFFEIC ACIDCATALYZED SYNTHESIS
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Regulation of NADPH oxidase-mediated superoxide production by acetylation and deacetylation

2021

Oral treatment of apolipoprotein E-knockout (ApoE-KO) mice with the putative sirtuin 1 (SIRT1) activator resveratrol led to a reduction of nicotinamide adenine dinucleotide phosphate (NADPH) oxidase activity in the heart. In contrast, the SIRT1 inhibitor EX527 enhanced the superoxide production in isolated human polymorphonuclear granulocytes. In human monocytic THP-1 cells, phorbol ester-stimulated superoxide production was enhanced by inhibitors of histone deacetylases (HDACs; including quisinostat, trichostatin A (TSA), PCI34051, and tubastatin A) and decreased by inhibitors of histone acetyltransferases [such as garcinol, curcumin, and histone acetyltransferase (HAT) Inhibitor II]. Thes…

Physiologyresveratrolsirtuin 1histone acetyltransferaseSirtuinechemistry.chemical_compoundHistone deacetylasesSirtuin 1Physiology (medical)NADPH-OxidasemedicineQP1-981ddc:610Original ResearchacetylationAcetyltransferasenNADPH oxidasebiologyNADPH oxidaseSirtuin 1SuperoxideAcetylationHistone acetyltransferaseTrichostatin AchemistryBiochemistryHistone acetyltransferasesAcetylationResveratrolNADPH oxidaseshistone deacetylasebiology.proteinHistone deacetylaseDDC 610 / Medicine & healthNicotinamide adenine dinucleotide phosphateRac1medicine.drug
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Subcellular distribution of choline acetyltransferase by immunogold electron microscopy in non-neuronal cells: Placenta, airways and murine embryonic…

2012

Abstract Aims Acetylcholine is synthesized in more or less all mammalian cells. However, little is known about the subcellular location of acetylcholine synthesis. Therefore, in the present experiments the subcellular location of the synthesizing enzyme choline acetyltransferase (ChAT) was investigated by anti-ChAT immunogold electron microscopy in human placenta and airways as well as in a murine embryonic stem cell line (CGR8 cell line). Main methods Human tissue was obtained as so-called surplus tissue (after delivery/surgical removal because of lung tumor); the CGR8 stem cell line was cultured under standard conditions. For human tissue a monoclonal mouse anti-ChAT antibody (ab) was use…

PlacentaeducationBronchiRespiratory MucosaBiologyGeneral Biochemistry Genetics and Molecular BiologyCell LineCholine O-AcetyltransferaseCell membraneMicePregnancyCaveolaeMacrophages Alveolarmental disordersmedicineAnimalsHumansGeneral Pharmacology Toxicology and PharmaceuticsNuclear membraneCells CulturedEmbryonic Stem Cellshealth care economics and organizationsEpithelial CellsGeneral MedicineImmunogold labellingImmunohistochemistryCholine acetyltransferaseMolecular biologyCellular StructureshumanitiesTrophoblastsCell biologyMicroscopy ElectronCytosolCell nucleusmedicine.anatomical_structureCell cultureFemaleLife Sciences
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l-Tyrosine β-naphthylamide is a potent competitive inhibitor of tyramine N-(hydroxycinnamoyl)transferase in vitro

2001

L-Tyrosine beta-naphthylamide, a synthetic substrate designed to measure tyrosine aminopeptidase activity, is a potent inhibitor of hydroxycinnamoyl-CoA:tyramine N-(hydroxycinnamoyl)transferase (THT) purified from elicited tobacco cell-suspension cultures. The inhibition is competitive, with the inhibitor binding reversibly to the tyramine binding site of the enzyme. Similar results were obtained with THT extracted from elicited potato cell-suspension cultures. Ki values were found to be 0.66 microM for the enzyme from tobacco and 0.3 microM for the enzyme from potato. L-Tyrosine 7-amido-4-methylcoumarin, a fluorogenic substrate for tyrosine aminopeptidases, the structure of which is close …

Plant ScienceNaphthalenesHorticultureBiologyBinding CompetitiveBiochemistryAminopeptidaseStructure-Activity Relationshipchemistry.chemical_compoundNon-competitive inhibitionTyrosine aminotransferaseTobaccoTransferaseEnzyme InhibitorsTyrosineMolecular BiologySolanum tuberosumchemistry.chemical_classificationGeneral MedicineTyramineKineticsPlants ToxicEnzymechemistryBiochemistryEnzyme inhibitorbiology.proteinTyrosineAcyltransferasesPhytochemistry
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