Search results for "Transferase"

showing 10 items of 1030 documents

Talin1 sets the stage for dendritic cell activation

2020

In dendritic cells, talin1 links integrin binding to efficient TLR downstream signaling through interaction with MyD88 and PIP5K.

TalinCellular differentiationImmunologyIntegrinInsightsMiceConditional gene knockoutImmune ToleranceImmunology and AllergyAnimalsSkinMice KnockoutMembrane GlycoproteinsbiologyChemistryChemotaxisToll-Like ReceptorsNF-kappa BReceptors Interleukin-1Dendritic cellCell biologyPhosphotransferases (Alcohol Group Acceptor)Langerhans CellsMyeloid Differentiation Factor 88biology.proteinCytokinesSignal transductionSignal TransductionThe Journal of Experimental Medicine
researchProduct

Epigenetic Regulation of Early- and Late-Response Genes in Acute Pancreatitis

2015

Abstract Chromatin remodeling seems to regulate the patterns of proinflammatory genes. Our aim was to provide new insights into the epigenetic mechanisms that control transcriptional activation of early- and late-response genes in initiation and development of severe acute pancreatitis as a model of acute inflammation. Chromatin changes were studied by chromatin immunoprecipitation analysis, nucleosome positioning, and determination of histone modifications in promoters of proinflammatory genes in vivo in the course of taurocholate-induced necrotizing pancreatitis in rats and in vitro in rat pancreatic AR42J acinar cells stimulated with taurocholate or TNF-α. Here we show that the upregulat…

Taurocholic AcidTranscriptional Activation0301 basic medicineChromatin ImmunoprecipitationImmunologyAcinar CellsBiologyMethylationChromatin remodelingEpigenesis GeneticHistones03 medical and health sciences0302 clinical medicineHistone methylationAnimalsImmunology and AllergyNucleosomeEpigeneticsPromoter Regions GeneticEarly Growth Response Protein 1Histone AcetyltransferasesInflammationPancreatitis Acute NecrotizingTumor Necrosis Factor-alphaDNA HelicasesNuclear ProteinsAcetylationHistone acetyltransferaseChromatin Assembly and DisassemblyRatsChromatin030104 developmental biologyHistoneGene Expression Regulation030220 oncology & carcinogenesisbiology.proteinCancer researchProtein Processing Post-TranslationalChromatin immunoprecipitationTranscription FactorsThe Journal of Immunology
researchProduct

Chromatin modifiers and recombination factors promote a telomere fold-back structure, that is lost during replicative senescence.

2020

Telomeres have the ability to adopt a lariat conformation and hence, engage in long and short distance intra-chromosome interactions. Budding yeast telomeres were proposed to fold back into subtelomeric regions, but a robust assay to quantitatively characterize this structure has been lacking. Therefore, it is not well understood how the interactions between telomeres and non-telomeric regions are established and regulated. We employ a telomere chromosome conformation capture (Telo-3C) approach to directly analyze telomere folding and its maintenance in S. cerevisiae. We identify the histone modifiers Sir2, Sin3 and Set2 as critical regulators for telomere folding, which suggests that a dis…

TelomeraseProtein Folding:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::DNA-Binding Proteins::Rad52 DNA Repair and Recombination Protein [Medical Subject Headings]:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::Fungal Proteins::Saccharomyces cerevisiae Proteins [Medical Subject Headings]Gene ExpressionYeast and Fungal ModelsArtificial Gene Amplification and ExtensionQH426-470BiochemistryPolymerase Chain ReactionChromosome conformation captureHistonesCromatina0302 clinical medicineSirtuin 2Macromolecular Structure AnalysisSilent Information Regulator Proteins Saccharomyces cerevisiaeCellular Senescence:Organisms::Eukaryota::Fungi::Yeasts::Saccharomyces::Saccharomyces cerevisiae [Medical Subject Headings]0303 health sciencesChromosome BiologyEukaryota:Phenomena and Processes::Genetic Phenomena::Genetic Processes::DNA Replication [Medical Subject Headings]TelomereSubtelomere:Anatomy::Cells::Cellular Structures::Intracellular Space::Cell Nucleus::Cell Nucleus Structures::Intranuclear Space::Chromosomes::Chromosome Structures::Telomere [Medical Subject Headings]Chromatin3. Good healthChromatinCell biologyNucleic acidsTelomeres:Phenomena and Processes::Cell Physiological Phenomena::Cell Physiological Processes::Cell Cycle::Cell Division::Telomere Homeostasis [Medical Subject Headings]Experimental Organism SystemsDaño del ADNEpigeneticsResearch ArticleSenescenceDNA Replication:Chemicals and Drugs::Enzymes and Coenzymes::Enzymes::Hydrolases::Amidohydrolases::Histone Deacetylases [Medical Subject Headings]Chromosome Structure and FunctionProtein StructureSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeBiologyResearch and Analysis MethodsHistone DeacetylasesChromosomes03 medical and health sciencesSaccharomycesModel Organisms:Chemicals and Drugs::Enzymes and Coenzymes::Enzymes::Transferases::One-Carbon Group Transferases::Methyltransferases [Medical Subject Headings]:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::Intracellular Signaling Peptides and Proteins::Sirtuins::Sirtuin 2 [Medical Subject Headings]:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::Fungal Proteins::Saccharomyces cerevisiae Proteins::Silent Information Regulator Proteins Saccharomyces cerevisiae [Medical Subject Headings]DNA-binding proteinsGenetics:Chemicals and Drugs::Enzymes and Coenzymes::Enzymes::Recombinases::Rec A Recombinases::Rad51 Recombinase [Medical Subject Headings]Molecular Biology TechniquesMolecular Biology030304 developmental biologyCromosomasSenescencia celularOrganismsFungiBiology and Life SciencesProteinsTelomere HomeostasisCell BiologyDNAMethyltransferasesG2-M DNA damage checkpointProteína recombinante y reparadora de ADN Rad52YeastTelomereRad52 DNA Repair and Recombination ProteinRepressor ProteinsAnimal Studies:Chemicals and Drugs::Amino Acids Peptides and Proteins::Proteins::Transcription Factors::Repressor Proteins [Medical Subject Headings]DNA damageRad51 RecombinaseHomologous recombination030217 neurology & neurosurgeryTelómeroDNA DamagePLoS Genetics
researchProduct

The role of polymorphisms of thiopurine methyltransferase in therapy with Azathioprine: preliminary study

2018

Azathioprine is an immunosuppressant drug belonging to the class of thiopurines widely used in clinical therapy. Its immunosuppressive action is linked to the substantial action mechanism in the inhibition of the synthesis of nitrogenous bases purine carried out in T-lymphocyte. The level of such medication limit resides in side effects such as myelosuppression and the development of tumours. The occurrence of side effects is linked to the presence of genetic polymorphisms of Thiopurine methyltransferase (TPMT). To date, 40 allelic variants for TPMT have been detected. However, those responsible for the reduction of enzyme activity are three: *2, *3A, *3C. The presence of one of the three p…

Thiopurine methyltransferasebiologybusiness.industryBiochemistry (medical)AzathioprinePlant ScienceThiopurine methyltransferasePharmacologyGeneral Biochemistry Genetics and Molecular Biologylcsh:Biology (General)PharmacogeneticsAzathioprinebiology.proteinMedicinebusinessPolymorphisms of metabolising enzymes drugslcsh:QH301-705.5medicine.drugJournal of Biological Research - Bollettino della Società Italiana di Biologia Sperimentale
researchProduct

Thiosulfate Reduction in Salmonella enterica Is Driven by the Proton Motive Force

2012

ABSTRACT Thiosulfate respiration in Salmonella enterica serovar Typhimurium is catalyzed by the membrane-bound enzyme thiosulfate reductase. Experiments with quinone biosynthesis mutants show that menaquinol is the sole electron donor to thiosulfate reductase. However, the reduction of thiosulfate by menaquinol is highly endergonic under standard conditions (Δ E °′ = −328 mV). Thiosulfate reductase activity was found to depend on the proton motive force (PMF) across the cytoplasmic membrane. A structural model for thiosulfate reductase suggests that the PMF drives endergonic electron flow within the enzyme by a reverse loop mechanism. Thiosulfate reductase was able to catalyze the combined …

ThiosulfatesSulfurtransferaseElectron donorNaphtholsBiologyPhotochemistryMicrobiologyGene Expression Regulation Enzymologicchemistry.chemical_compoundElectron transferSulfiteEscherichia coliFormateMolecular BiologyExergonic reactionThiosulfateTerpenesChemiosmosisProton-Motive ForceSalmonella entericaGene Expression Regulation BacterialArticleschemistryBiochemistrySulfurtransferasesThermodynamicsProtonsOxidation-ReductionJournal of Bacteriology
researchProduct

Glucosylation of Rho proteins by Clostridium difficile toxin B.

1995

TOXIN A and B, the major virulence factors of Clostridium difficile, are the causative agents of antibiotic-associated pseudomembran-ous colitis. In cultured cell lines their potent cytotoxicity results from their ability to induce disaggregation of the microfilament cytoskeleton1,2. Toxin B acts on the low-molecular-mass GTPase Rho A3,4, which is involved in the regulation of the actin cytoskeleton. We report here that toxin B catalyses the incorporation of up to one mole of glucose per mole of RhoA at the amino acid thre-onine at position 37. The modification was identified and localized by tandem electrospray mass spectrometry. UDP-glucose selectively serves as cosubstrate for the monogl…

ThreonineRHOAGlycosylationBacterial ToxinsMolecular Sequence DataClostridium difficile toxin AClostridium difficile toxin Bmacromolecular substancesmedicine.disease_causeMicrofilamentCatalysisMass SpectrometryGTP PhosphohydrolasesBacterial ProteinsGTP-Binding ProteinsmedicineTumor Cells CulturedAnimalsAmino Acid SequenceCytoskeletonActinCells CulturedCytoskeletonMultidisciplinarybiologyToxinClostridioides difficileActin cytoskeletonActinsRecombinant ProteinsRatsGlucoseMarsupialiaBiochemistryGlucosyltransferasesbiology.proteinrhoA GTP-Binding ProteinNature
researchProduct

Ras, Rap, and Rac Small GTP-binding Proteins Are Targets for Clostridium sordellii Lethal Toxin Glucosylation

1996

Lethal toxin (LT) from Clostridium sordellii is one of the high molecular mass clostridial cytotoxins. On cultured cells, it causes a rounding of cell bodies and a disruption of actin stress fibers. We demonstrate that LT is a glucosyltransferase that uses UDP-Glc as a cofactor to covalently modify 21-kDa proteins both in vitro and in vivo. LT glucosylates Ras, Rap, and Rac. In Ras, threonine at position 35 was identified as the target amino acid glucosylated by LT. Other related members of the Ras GTPase superfamily, including RhoA, Cdc42, and Rab6, were not modified by LT. Incubation of serum-starved Swiss 3T3 cells with LT prevents the epidermal growth factor-induced phosphorylation of m…

ThreonineUridine Diphosphate GlucoseRHOABacterial ToxinsMolecular Sequence DataClostridium sordelliimacromolecular substancesCDC42GTPaseBiologyCell morphologyBiochemistryGTP PhosphohydrolasesProto-Oncogene Proteins p21(ras)MiceGTP-binding protein regulatorsGTP-Binding ProteinsAnimalsHumansAmino Acid SequenceMolecular BiologyClostridiumEpidermal Growth FactorKinase3T3 CellsCell Biologybiology.organism_classificationMolecular biologyActinsrac GTP-Binding ProteinsActin CytoskeletonKineticsGlucoserap GTP-Binding ProteinsGlucosyltransferasesCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinPhosphorylationGuanosine TriphosphateHeLa CellsJournal of Biological Chemistry
researchProduct

Oxidative DNA damage and disturbance of antioxidant capacity by alternariol in Caco-2 cells

2015

Oxidative stress occurs as a consequence of an imbalance between the prooxidant/antioxidant systems, causing an increase of intracellular generation of reactive oxygen species. Alternariol (AOH), a mycotoxin produced by Alternaria sp. can alter the action of glutathione (GSH) and the enzymes involved in the redox system, causing damage to cellular macromolecules such as DNA. The aims of this work were to determine the induction of oxidative stress by the antioxidant defenses imbalance in relation to glutathione (GSH), glutathione reductase (GR), glutathione transferase (GST), glutathione peroxidase (GPx) levels and DNA damage in Caco-2 cells derived from adenocarcinoma human colon. Oxidativ…

Time FactorsAntioxidantDNA damagemedicine.medical_treatmentGlutathione reductaseAlternariolBiologyToxicologymedicine.disease_causeAntioxidantsLactoneschemistry.chemical_compoundmedicineHumansGlutathione Transferasechemistry.chemical_classificationGlutathione PeroxidaseDose-Response Relationship DrugGlutathione peroxidaseGeneral MedicineGlutathioneMycotoxinsGlutathioneComet assayOxidative StressGlutathione ReductaseBiochemistrychemistryComet AssayCaco-2 CellsOxidative stressDNA DamageToxicology Letters
researchProduct

Expression and possible functions of the cholinergic system in a murine embryonic stem cell line.

2007

The expression of a cholinergic system during embryonic development is a widespread phenomenon. However, no precise function could be assigned to it during early pre-neural stages and there are only few studies that document when it precisely starts to be expressed. Here, we examined the expression of cholinergic components in a murine embryonic stem cell line by RT-PCR, histochemistry, and enzyme activity measurements; the acetylcholine (ACh) content was measured by HPLC. We have demonstrated that embryonic stem cells express ACh, acetylcholine receptors, choline acetyltransferase (ChAT), acetyl- and butyryl-cholinesterase (AChE and BChE). Butyryl-cholinesterase (BChE) expression was highe…

Time FactorsBiologyGeneral Biochemistry Genetics and Molecular BiologyCell LineCholine O-AcetyltransferaseMicemedicineAnimalsCholinesterasesReceptors CholinergicGeneral Pharmacology Toxicology and PharmaceuticsEmbryonic Stem CellsAcetylcholine receptorCell ProliferationTetraisopropylpyrophosphamideReverse Transcriptase Polymerase Chain ReactionGene Expression ProfilingGeneral MedicineBenzenaminium 44'-(3-oxo-15-pentanediyl)bis(NN-dimethyl-N-2-propenyl-) DibromideCholine acetyltransferaseEmbryonic stem cellMolecular biologyAcetylcholineCell cultureButyrylcholinesteraseAcetylcholinesteraseCholinergicCholinesterase InhibitorsStem cellAcetylcholineAdult stem cellmedicine.drugLife sciences
researchProduct

Inhibition of giant cell formation by compound 48/80 after infection with herpesvirus hominis

1974

Choline kinase has been found to be a soluble enzyme with a molecular weight of 105,000 in the cytoplasm of primary rabbit kidney cells. It has been purified 150-fold. It was investigated whether the inhibiting effect of Cpd 48/80 on virus-induced giant cell formation is due to interference with this enzyme. Cpd 48/80-dimer was shown to inhibit the choline kinase activityin vitro without a concomitant inhibition of giant cell formation. Likewise, another competitive inhibitor of choline kinase, purinyl-6-histamine, does not prevent giant cell formation. This finding suggests that there is no correlation between choline kinase activity and giant cell formation.

Time FactorsCholine kinaseeducationGalactosamineOleic AcidsBiologyKidneyTritiumCholinechemistry.chemical_compoundCytopathogenic Effect ViralBiosynthesisVirologyAnimalsSimplexvirusp-Methoxy-N-methylphenethylamineCarbon RadioisotopesCells Culturedchemistry.chemical_classificationGlucosamineBinding SitesPhosphotransferasesGeneral MedicineCompound 48/80LipidsVirologyMolecular biologyIn vitroEnzymechemistryEthanolaminesCytoplasmGiant cellDepression ChemicalPhosphatidylcholinesTritiumChromatography Thin LayerRabbitsArchiv f�r die gesamte Virusforschung
researchProduct