Search results for "adenosine triphosphate"

showing 10 items of 232 documents

Autophagy-Dependent Anticancer Immune Responses Induced by Chemotherapeutic Agents in Mice

2011

Antineoplastic chemotherapies are particularly efficient when they elicit immunogenic cell death, thus provoking an anticancer immune response. Here we demonstrate that autophagy, which is often disabled in cancer, is dispensable for chemotherapy-induced cell death but required for its immunogenicity. In response to chemotherapy, autophagy-competent, but not autophagy-deficient, cancers attracted dendritic cells and T lymphocytes into the tumor bed. Suppression of autophagy inhibited the release of adenosine triphosphate (ATP) from dying tumor cells. Conversely, inhibition of extracellular ATP-degrading enzymes increased pericellular ATP in autophagy-deficient tumors, reestablished the recr…

Programmed cell deathcells cancer immunogenicity calreticulin exposure hmgb1Antineoplastic AgentsBiologyimmunogenicityNOMicechemistry.chemical_compoundAdenosine TriphosphateImmune systemCell Line TumorNeoplasmsAutophagyExtracellularAnimalsHumanscancerMice Inbred BALB CMultidisciplinaryCell DeathImmunogenicityAutophagyDendritic CellsMice Inbred C57BLhmgb1chemistryCell cultureCancer researchImmunogenic cell deathcellsMitoxantroneCalreticulinAdenosine triphosphatecalreticulin exposure
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Botulinum A and the light chain of tetanus toxins inhibit distinct stages of Mg.ATP-dependent catecholamine exocytosis from permeabilised chromaffin …

1994

Susceptibilities of Mg.ATP-independent and Mg.ATP-requiring components of catecholamine secretion from digitonin-permeabilised chromaffin cells to inhibition by Clostridial botulinum type A and tetanus toxins were investigated. These toxins are Zn(2+)-dependent proteases which specifically cleave the 25-kDa synaptosomal-associated protein (SNAP-25) and vesicle-associated membrane protein (VAMP) II, respectively. When applied to permeabilised chromaffin cells they rapidly inhibited secretion in the presence of Mg.ATP but the catecholamine released in the absence of Mg.ATP, thought to represent fusion of primed granules, was not perturbed. The toxins can exert their effects per se in the abse…

ProteasesBotulinum ToxinsCell Membrane PermeabilityBiologymedicine.disease_causeBiochemistryExocytosisExocytosischemistry.chemical_compoundAdenosine TriphosphateCatecholaminesTetanus ToxinmedicineAnimalsSecretionChromaffin GranulesCells CulturedToxinKineticsmedicine.anatomical_structurechemistryMembrane proteinBiochemistryAdrenal MedullaCatecholamineCattleAdrenal medullaAdenosine triphosphatemedicine.drugEuropean journal of biochemistry
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Differential changes in purine nucleotides after Doxorubicin treatment of human cancer cells in vitro

2002

The present investigation was performed to elucidate the role of purine nucleotides as potential indicators of chemosensitivity of malignant tumors. Drug-sensitive (s) and -resistant (r) tumor cell lines grown as monolayers (s: T47D, MCF-7 wild-type; r: NCI/ADR-RES, MCF-7/MDR) or as multicellular spheroids (T47D; NCI/ADR-RES) were exposed to 0.1, 1.0, and 10.0 microM Doxorubicin for up to 24 h. Purine nucleotides were assayed using HPLC and with some selected spheroids using imaging bioluminescence. The data show that in the time frame of the experiments reproducible and statistically significant changes in the nucleotides only occur at the highest drug concentration investigated. Under the…

PurineCancer ResearchOligomycinGTP'Antineoplastic AgentsIn Vitro TechniquesBiologychemistry.chemical_compoundAdenosine TriphosphateIn vivoSpheroids CellularTumor Cells CulturedmedicineHumansNucleotideDoxorubicinATP Binding Cassette Transporter Subfamily B Member 1Chromatography High Pressure Liquidchemistry.chemical_classificationBiological activityMolecular biologyDrug Resistance MultipleIn vitroOncologyBiochemistrychemistryDoxorubicinDrug Resistance NeoplasmLuminescent MeasurementsGuanosine Triphosphatemedicine.drugInternational Journal of Oncology
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Arabinose nucleoside triphosphates are no inhibitors for DNA-dependent RNA polymerases.

1976

1-Beta-D-arabinofuranosylcytosine-5' -triphosphate and 9-beta-D-arabinofuranosyladenosine-5' -triphosphate were found to have no inhibitory potency for both mammalian DNA-dependent RNA polymerase II and E. coli DNA-dependent RNA polymerase.

RNA-dependent RNA polymeraseRNA polymerase IIOviductsCytosine NucleotidesQuailCellular and Molecular Neurosciencechemistry.chemical_compoundAdenosine TriphosphateTranscription (biology)RNA polymeraseRNA polymerase IEscherichia coliAnimalsMolecular BiologyPolymerasePharmacologybiologyChemistryMusclesCytarabineRNACell BiologyDNA-Directed RNA PolymerasesMolecular biologyKineticsAvian Sarcoma VirusesRNA editingbiology.proteinMolecular MedicineRNA Polymerase IIVidarabineExperientia
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Structural dynamics in F1ATPase during the first reaction cycle of ATP hydrolysis

1991

Abstract The velocity of ATP hydrolysis, catalyzed by purified F 1 ATPase from Micrococcus luteus , was decelerated on decreasing the temperature. At 13′C one reaction cycle is completed after 20 s. Hydrolysis was triggered upon rapid mixing of the enzyme with ATP. During the first reaction cycle, succeeding structural alterations of the F 1 ATPase were traced by time resolved X-ray scattering. The scattering spectra obtained from consecutive intervals of 1 s, revealed the F 1 ATPase to pass a conformational state exhibiting an expanded (6%) molecular shape. The expanded state was observed between 45% and 65% of the time required to complete the reaction cycle. This pointx out a conformatio…

Reaction mechanismProtein ConformationStereochemistryATPaseBiophysicsTime resolved X-ray scatteringBiochemistryMicrococcusCatalysisF1ATPaseHydrolysisMolecular dynamicsAdenosine TriphosphateStructural BiologyATP hydrolysisGeneticsMolecular Biologychemistry.chemical_classificationbiologyHydrolysisX-RaysReaction cycleCell Biologybiology.organism_classificationKineticsProton-Translocating ATPasesEnzymechemistryDynamic structure transitionbiology.proteinMicrococcus luteusFEBS Letters
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Partial purification and characterization of succinyl-CoA synthetase from Saccharomyces cerevisiae

1983

Succinyl-CoA synthetase from Saccharomyces cerevisiae was partially purified (20-fold) with a yield of 44%. The Michaelis-Menten constants were determined: Km (succinate) = 17 mM; Km (ATP) = 0.13 mM; Km (CoA) = 0.03 mM. The succinyl-CoA synthetase has a molecular weight of about 80000 dalton (as determined by polyacrylamide gradient gel electrophoresis). The pH optimum is at 6.0. During fermentation the activity of succinyl-CoA synthetase is lower than in aerobically grown yeast cells. The presence of succinyl-CoA synthetase in fermenting yeasts may be regarded as an indication for the oxidative formation of succinate. In fermenting yeast cells succinyl-CoA synthetase is repressed by glucos…

Saccharomyces cerevisiaeSuccinic AcidCatabolite repressionSaccharomyces cerevisiaeMicrobiologyAdenosine TriphosphateCoenzyme A LigasesSuccinate-CoA LigasesAnaerobiosisMolecular BiologyGel electrophoresischemistry.chemical_classificationChromatographybiologyorganic chemicalsSuccinyl coenzyme A synthetaseTemperatureSuccinatesSuccinate-CoA LigasesGeneral MedicineHydrogen-Ion Concentrationbiology.organism_classificationYeastAmino acidMolecular WeightKineticsBiochemistrychemistrybacteriaFermentationAntonie van Leeuwenhoek
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Novel Glutamate–Putrescine Ligase Activity in Haloferax mediterranei: A New Function for glnA-2 Gene

2021

This article belongs to the Section Cellular Biochemistry.

Salmonella typhimuriumTranscription GeneticNitrogen assimilationHaloferax mediterraneiGene ExpressionBiochemistryGlutamate-putrescine ligase activitySubstrate SpecificityLigasesAdenosine TriphosphateputrescineCloning MolecularPhylogenyhaloarchaeachemistry.chemical_classification0303 health sciencesbiologyChemistryHaloarchaeaEscherichia coli Proteinsglutamine synthetaseBioquímica y Biología MolecularQR1-502Recombinant ProteinsNitrogen assimilationHaloferax mediterraneiIsoenzymesBiochemistryArchaeal ProteinsGenetic VectorsGlutamic AcidGlutamate–putrescine ligaseMicrobiologyArticleglutamate–putrescine ligaseGlutamine synthetase03 medical and health sciencesAmmoniaGlutamine synthetaseNitrogen FixationEscherichia coliPutrescineAmino Acid SequenceMolecular Biology030304 developmental biologyDNA ligaseSequence Homology Amino Acid030306 microbiologyComputational Biologynitrogen assimilationbiology.organism_classificationMetabolic pathwayEnzymeProtein BiosynthesisHaloarchaeaGene Expression Regulation ArchaealSequence AlignmentBiomolecules
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Depletion of cytosolic GSH decreases the ATP levels and viability of synaptosomes from aged mice but not from young mice

1995

The effect of glutathione depletion on the viability of freshly isolated synaptosomes from whole brain was investigated in young and aged mice. Aging did not influence the GSH and ATP levels and the viability of these synaptosomes. However depletion of glutathione caused by the cytosolic glutathione inhibitor diethyl maleate (1 mM) resulted in a significant decline, after 60 min of incubation, in ATP levels and viability in the synaptosomes from aged mice but not in those from young mice. When synaptosomes were incubated in the presence of the mitochondrial glutathione inhibitor ethacrynic acid (0.2 mM) there was a similar decline in glutathione, ATP levels and synaptosomal viability, both …

SenescenceAgingmedicine.medical_specialtyRatónBiologyMitochondrionMiceRandom Allocationchemistry.chemical_compoundAdenosine TriphosphateCytosolInternal medicinemedicineAnimalsIncubationSynaptosomeGlutathioneGlutathioneIn vitroMitochondriaCytosolEthacrynic AcidEndocrinologychemistryFemaleEnergy MetabolismSynaptosomesDevelopmental BiologyMechanisms of Ageing and Development
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Interaction of UO2(2+) with ATP in aqueous ionic media.

2005

Interaction of dioxouranium(VI) (uranyl) ion with ATP was studied by ligand/proton and metal/hydroxide displacement technique, at very low ionic strength and at I=0.15 mol L(-1), in aqueous Me4NCl and NaCl solutions, at t=25 degrees C. Measurements were carried out in the pH range 3-8.5, before the formation of precipitate. Computer analysis allowed us to find the quite stable species UO2(ATP)H2(0), UO2(ATP)H-, UO2(ATP)2-, UO2(ATP)2(6-), UO2(ATP)2H2(4-) and UO2(ATP)(OH)3- whose formation constants are (at I=0 mol L(-1)) logbeta(112)=18.21, logbeta(111)=14.70, logbeta(110)=9.14, logbeta(120)=12.84, logbeta(122)=24.82, and logbeta(11-1)=2.09, respectively. Different values were obtained in th…

SpeciationInorganic chemistryIonic mediaBiophysicsIonic bondingLigandsBiochemistryComplexeIonMetalchemistry.chemical_compoundAdenosine TriphosphateMetals HeavySettore CHIM/01 - Chimica AnaliticaAqueous solutionLigandHydrolysisOrganic ChemistryWaterHydrogen-Ion ConcentrationUranylUranium CompoundsDioxouranium(VI)ATPchemistryStability constants of complexesvisual_artDependence on medium of stability constantvisual_art.visual_art_mediumHydroxideBiophysical chemistry
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Recovery of human fibroblasts from attack by the pore-forming alpha-toxin of Staphylococcus aureus.

1994

When applied at low concentrations (10 micrograms/ml), staphylococcal alpha-toxin generates a small channel in keratinocyte and lymphocyte membranes that permits selective transmembrane flux of monovalent ions. Here we show that a moderate concentration (1-50 micrograms/ml) of alpha-toxin similarly produces a small pore in membranes of human fibroblasts. This process leads to rapid leakage of K+ and to a drop in cellular ATP to 10-20% of normal levels in 2 h. In the presence of medium supplemented with serum and at pH 7.4, the cells are able to recover from toxin attack, so that normal levels of K+ and ATP are reached after 6-8 h at 37 degrees C. The repair process is dependent on the prese…

Staphylococcus aureusLymphocyteBacterial ToxinsBiologymedicine.disease_causeMicrobiologyOuabainIon ChannelsCell LineHemolysin ProteinsAdenosine TriphosphatemedicineHumansFibroblastOuabainToxinCell MembraneHemolysinFibroblastsTransmembrane proteinCulture MediaKineticsInfectious Diseasesmedicine.anatomical_structureMembraneBiochemistryBiophysicsPotassiumStreptolysinmedicine.drugMicrobial pathogenesis
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