Search results for "Jurkat"

showing 10 items of 90 documents

Pyrrolotetrazinones deazaanalogues of temozolomide induce apoptosis in Jurkat cell line: involvement of tubulin polymerization inhibition.

2009

Pyrrolotetrazinones are a new class of azolotetrazinones endowed with a high, remarkable antiproliferative activity in human tumor cultured cells. They hold the deaza skeleton of the antitumor drug temozolomide, although preliminary investigations indicated a different mechanism of action. To understand their mechanism(s) of action along with their target at molecular level, four derivatives were selected on the basis of their activity on a panel of human tumor cell lines and they were investigated in depth in a T leukemia cell line (Jurkat). Flow cytometric analysis of cell cycle after treatment with pyrrolotetrazinones has demonstrated that they were able to induce an arrest of the cell c…

MaleCancer ResearchProgrammed cell deathCarcinoma HepatocellularCell SurvivalCellGene ExpressionAntineoplastic AgentsApoptosisPhosphatidylserinesBiologyToxicologyJurkat cellsMicrotubulesMicrotubule polymerizationJurkat CellsMiceTubulinCell Line TumormedicineTemozolomideAnimalsHumansPharmacology (medical)Cell Proliferationbcl-2-Associated X ProteinPharmacologyMembrane Potential MitochondrialMice Inbred BALB CCaspase 3Cell CycleCell MembraneCell cycleSettore CHIM/08 - Chimica FarmaceuticaTubulin ModulatorsCell biologyMitochondriaDacarbazinemedicine.anatomical_structureOncologyMechanism of actionBiochemistryProto-Oncogene Proteins c-bcl-2ApoptosisCell culturemedicine.symptomPoly(ADP-ribose) PolymerasesReactive Oxygen SpeciesPyrrolotetrazinoneCancer chemotherapy and pharmacology
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Toxicological Study in vitro, in vivo and Transcriptomic of Mycotoxins. Estudio Toxicológico in vitro, in vivo y Transcriptómico de Micotoxinas

2018

Las micotoxinas, producidas por el metabolismo secundario de hongos filamentosos, se consideran contaminantes comunes de alimentos y piensos y constituyen una preocupación en el ámbito de la seguridad alimentaria. Se han estudiado los efectos tóxicos y mecanismos de acción de las micotoxinas emergentes Beauvericina (BEA) y Eniatinas (ENs) mediante ensayos in vitro en células Jurkat, in vivo en rata Wistar y transcriptómicos por secuenciación del ARN; así como la presencia de multi-micotoxinas en alimentos, piensos y muestras biológicas. Las revisiones realizadas ponen de manifiesto que (i) la investigación in vivo de fusarotoxinas se basa principalmente en estudios de toxicidad subaguda y s…

MicotoxinasJurkatRata WistarToxicologíaToxicogenómicaTranscriptómicaBeauvericinaEniatinas
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β2 integrin phosphorylation on Thr758 acts as a molecular switch to regulate 14-3-3 and filamin binding

2008

AbstractLeukocyte integrins of the β2 family are essential for immune cell-cell adhesion. In activated cells, β2 integrins are phosphorylated on the cytoplasmic Thr758, leading to 14-3-3 protein recruitment to the β2 integrin. The mutation of this phosphorylation site impairs cell adhesion, actin reorganization, and cell spreading. Thr758 is contained in a Thr triplet of β2 that also mediates binding to filamin. Here, we investigated the binding of filamin, talin, and 14-3-3 proteins to phosphorylated and unphosphorylated β2 integrins by biochemical methods and x-ray crystallography. 14-3-3 proteins bound only to the phosphorylated integrin cytoplasmic peptide, with a high affinity (Kd, 261…

Models MolecularTalinThreonineanimal structuresFilaminsT-LymphocytesStatic ElectricityImmunologyIntegrinCD18macromolecular substancesPlasma protein bindingIn Vitro TechniquesFilaminBiochemistryJurkat Cells03 medical and health sciencesFilamin bindingContractile Proteins0302 clinical medicineCell AdhesionHumansProtein Interaction Domains and MotifsPhosphorylationCell adhesion030304 developmental biology0303 health sciencesBinding SitesbiologyChemistryMicrofilament ProteinsCell BiologyHematologyIntercellular Adhesion Molecule-1Talin bindingRecombinant ProteinsCell biology14-3-3 ProteinsAmino Acid SubstitutionCD18 AntigensMultiprotein Complexes030220 oncology & carcinogenesisbiology.proteinPhosphorylationProtein BindingBlood
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Cytotoxic, immunomodulatory, antimycotic, and antiviral activities of semisynthetic 14-hydroxyabietane derivatives and triptoquinone C-4 epimers

2013

A series of C14-hydroxy derivatives of dehydroabietic acid were synthesised from commercial abietic acid and evaluated for their cytotoxic, antimycotic, and antiviral activities. From these C14-hydroxy derivatives, triptoquinone C-4 epimers were obtained and their immunomodulatory activity was additionally evaluated. None of the tested compounds showed antiviral activity against herpes simplex virus type 1 (HHV-1), and nor did they display antimycotic activity against certain Aspergillus, spp. except for one compound, abieta-8,11,13-trien-14,18-diol. Interestingly, two triptoquinone epimers showed cytotoxic activity, and one of them induced mitochondrial potential loss, DNA damage and cell …

PharmacologyDNA damagemedicine.medical_treatmentMonocyteOrganic ChemistryPharmaceutical ScienceBiologyCell cyclemedicine.disease_causeBiochemistryPeripheral blood mononuclear cellJurkat cellsHerpes simplex virusCytokinemedicine.anatomical_structureBiochemistryDrug DiscoverymedicineMolecular MedicineCytotoxic T cellMedChemComm
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n-3 PUFAs modulate T-cell activation via protein kinase C-α and -ε and the NF-κB signaling pathway

2005

We elucidated the mechanisms of action of two n-3 PUFAs, eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA), in Jurkat T-cells. Both DHA and EPA were principally incorporated into phospholipids in the following order: phosphatidylcholine < phosphatidylethanolamine < phosphatidylinositol/phosphatidylserine. Furthermore, two isoforms of phospholipase A(2) (i.e., calcium-dependent and calcium-independent) were implicated in the release of DHA and EPA, respectively, during activation of these cells. The two fatty acids inhibited the phorbol 12-myristate 13-acetate (PMA)-induced plasma membrane translocation of protein kinase C (PKC)-alpha and -epsilon. The two n-3 PUFAs also inhibited t…

PhosphatidylethanolaminePhospholipase Amitogen-activated protein kinaseProtein Kinase C-epsilonQD415-436Cell BiologyPhosphatidylserineBiologyfatty acidsBiochemistryJurkat cellsCell biologychemistry.chemical_compoundEndocrinologychemistryBiochemistryDocosahexaenoic acidlipids (amino acids peptides and proteins)Phosphatidylinositolnuclear factor κBProtein kinase Cpolyunsaturated fatty acidsJournal of Lipid Research
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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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Mitochondrial proteomics profile points oxidative phosphorylation as main target for beauvericin and enniatin B mixture

2020

Abstract Beauvericin (BEA) and enniatin B (EN B) are non-legislated Fusarium mycotoxins usually found in cereal and cereal-based products all around the world. By the proteomic analysis of mitochondria enriched extracts from Jurkat cells exposed for 24 h to three concentrations of BEA:EN B (0.01–0.1–0.5 μM), a number of 1821 proteins (202 mitochondrial) were identified and relatively quantified. 340 proteins (59 mitochondrial) were statistically significant altered in our samples (Anova p-value ≤ 0.05 and fold change (FC) ≥1.5). The protein mitochondrial translational release factor 1 like (MTRF1L) was the most abundant protein in the three mycotoxin exposures studied. The mycotoxins mixtur…

ProteomicsTranscription GeneticOxidative phosphorylationMitochondrionToxicologyProteomicsRibosomeJurkat cellsOxidative PhosphorylationElectron TransportMitochondrial ProteinsJurkat Cells03 medical and health scienceschemistry.chemical_compound0404 agricultural biotechnologyDepsipeptidesHumans030304 developmental biology0303 health sciencesfood and beverages04 agricultural and veterinary sciencesGeneral Medicine040401 food scienceBeauvericinFold changeMitochondriachemistryBiochemistryBacterial outer membraneFood ScienceFood and Chemical Toxicology
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Pyrrolo[3,2-h]quinazolines as Photochemotherapeutic Agents

2011

Heteroanalogues of angelicin, pyrrolo[3,2-h]quinazolines, were synthesized with the aim of obtaining new potent photochemotherapeutic agents. Many derivatives caused a significant decrease in cell proliferation in several human tumor cell lines after irradiation with UVA light (GI(50) =15.2-0.2 μM). Their phototoxicity effected apoptosis in Jurkat cells with the involvement of mitochondria (as determined by the loss of mitochondrial membrane potential and production of reactive oxygen species) and lysosomes. The phototoxicity of these compounds could be explained by lipid peroxidation.

Pyrrolo[3; 2-h]quinazolines; Angelicin; Photochemotherapeutic AgentsAngelicinUltraviolet RaysApoptosisMitochondrion2-h]quinazolinesBiochemistryJurkat cellsLipid peroxidationStructure-Activity Relationshipchemistry.chemical_compoundAngelicinCell Line TumorFurocoumarinsPhotochemotherapeutic AgentsDrug DiscoveryHumansPyrrolo[32-h]quinazolinePyrrolesPyrrolo[3General Pharmacology Toxicology and PharmaceuticsPharmacologychemistry.chemical_classificationReactive oxygen speciesPhotosensitizing AgentsOrganic ChemistrySettore CHIM/08 - Chimica FarmaceuticachemistryBiochemistryApoptosisCell cultureQuinolinesMolecular MedicineDrug Screening Assays AntitumorReactive Oxygen SpeciesPhototoxicityChemMedChem
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Pyrrolo[3,4-h]quinolinones a new class of photochemotherapeutic agents

2011

Abstract Pyrrolo[3,4- h ]quinolin-2-ones were synthesized as nitrogen isosters of the angular furocoumarin angelicin, with the aim of obtaining new photochemotherapeutic agents with increased antiproliferative activity and lower undesired toxic effects. A versatile synthetic pathway was approached to allow the isolation of derivatives of the new ring system with a good substitution pattern on the pyrrole moiety. Photobiological screenings of the new compounds revealed a potent phototoxic effect and a great UVA dose dependence, reaching IC 50 values at submicromolar level. The induced cellular photocytotoxicity was related to apoptosis with the involvement of mitochondria and lysosomes, alte…

Pyrrolo[3; 4-h]quinolinones; Angelicin heteroanalogues; Photochemotherapeutic agents; PhototoxicityStereochemistryClinical BiochemistryMembrane lipid peroxidationPharmaceutical ScienceHL-60 CellsPhosphatidylserinesQuinolonesMitochondrionBiochemistryPhototoxicityJurkat CellsStructure-Activity Relationshipchemistry.chemical_compoundPhotochemotherapeutic agentsAngelicinCell Line TumorDrug DiscoveryHumansMoietyFluorometryPyrrolesPyrrolo[3Molecular BiologyPyrrolePyrrolo[34-h]quinolinoneFurocoumarinCell CycleOrganic Chemistry4-h]quinolinonesDNAPhotochemical ProcessesSettore CHIM/08 - Chimica FarmaceuticaAngelicin heteroanaloguesPhotochemotherapeutic agentPhotochemotherapychemistryApoptosisMolecular MedicineLipid PeroxidationPhototoxicityAngelicin heteroanalogueSubcellular FractionsBioorganic &amp; Medicinal Chemistry
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EBV-Induced Gene 3 Transcription Is Induced by TLR Signaling in Primary Dendritic Cells via NF-κB Activation

2005

Abstract The EBV-induced gene 3 (EBI3) is expressed in dendritic cells (DCs) and part of the cytokine IL-27 that controls Th cell development. However, its regulated expression in DCs is poorly understood. In the present study we demonstrate that EBI3 is expressed in splenic CD8−, CD8+, and plasmacytoid DC subsets and is induced upon TLR signaling. Cloning and functional analysis of the EBI3 promoter using in vivo footprinting and mutagenesis showed that stimulation via TLR2, TLR4, and TLR9 transactivated the promoter in primary DCs via NF-κB and Ets binding sites at −90 and −73 bp upstream of the transcriptional start site, respectively. Furthermore, we observed that NF-κB p50/p65 and PU.1…

RNA Capsmedicine.medical_treatmentDNA Mutational AnalysisMolecular Sequence DataImmunologyAntigen-Presenting CellsReceptors Cell SurfaceBiologyCell LineMinor Histocompatibility AntigensJurkat CellsMiceCell Line TumorGene expressionmedicineAnimalsHumansImmunology and AllergyReceptors CytokinePromoter Regions GeneticGlycoproteinsMice KnockoutMembrane GlycoproteinsInnate immune systemBase SequenceToll-Like ReceptorsHEK 293 cellsNF-kappa BTLR9hemic and immune systemsEBI3Dendritic CellsMolecular biologyToll-Like Receptor 2Up-RegulationMice Inbred C57BLToll-Like Receptor 4Protein SubunitsTLR2CytokineGene Expression RegulationToll-Like Receptor 9NIH 3T3 CellsTLR4Protein BindingSignal TransductionThe Journal of Immunology
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