Search results for "Jurkat"

showing 10 items of 90 documents

Inhibition of Delayed-Type Hypersensitivity by Cucurbitacin R through the Curbing of Lymphocyte Proliferation and Cytokine Expression by Means of Nuc…

2009

Cucurbitacin R is known to exhibit an anti-inflammatory effect in different experimental models of inflammation. In this article, we outline the effect of cucurbitacin R on T lymphocyte proliferation, cytokine production, and nuclear factor activation, as well as its influence on various experimental models of delayed-type hypersensitivity (DTH) in mice. Cucurbitacin R reduced the proliferation of phytohemagglutinin A-stimulated human T lymphocytes (IC(50), 18 microM), modifying the cell cycle, as well as the production of cytokines [interleukin (IL)-2, IL-4, IL-10, and especially interferon-gamma] and the induction of the principal cyclins implicated in the cell cycle (A(1), B(1), D(2), an…

Interleukin 2medicine.medical_specialtyT-Lymphocytesmedicine.medical_treatmentAnti-Inflammatory AgentsLymphocyte proliferationBiologyPharmacologyJurkat cellsDrug HypersensitivityJurkat CellsMiceCyclinsInternal medicinemedicineAnimalsHumansHypersensitivity DelayedInterleukin 4Cell ProliferationPharmacologyNFATC Transcription FactorsFootCell CycleIntracellular Signaling Peptides and ProteinsOxazoloneEarNFATCell cycleTriterpenesInterleukin 10EndocrinologyCytokineCytokinesMolecular MedicineDinitrofluorobenzeneFemalemedicine.drugJournal of Pharmacology and Experimental Therapeutics
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Dinitrosyl-iron triggers apoptosis in Jurkat cells despite overexpression of Bcl-2

2004

Cells expressing the cytokine-inducible NO synthase are known to trigger apoptosis in neighboring cells. Paramagnetic dinitrosyl nonheme iron complexes (DNIC) were found in tumor tissue about 40 years ago; however, the role of these NO(+)-bearing species is not completely understood. In the human Jurkat leukemia cell line, the application of the model complex DNIC-thiosulfate (50-200 microM) induced apoptosis (defined by phosphatidylserine externalization) in a concentration- and time-dependent manner. In Jurkat cells, the pan-caspase inhibitor, zVADfmk (50 microM), and/or stable transfection of antiapoptotic protein, Bcl-2, was unable to afford protection against DNIC-induced apoptosis. Th…

IronNitrosationCellApoptosisBiochemistryJurkat cellsMetal ChelatorNitric oxideJurkat Cellschemistry.chemical_compoundPhysiology (medical)medicineExtracellularPiHumansElectron Spin Resonance SpectroscopyGlutathioneCaspase InhibitorsCell biologymedicine.anatomical_structureGene Expression RegulationProto-Oncogene Proteins c-bcl-2chemistryApoptosisCaspasesNitrogen OxidesFree Radical Biology and Medicine
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Phenolic-glycolipid-1 and lipoarabinomannan preferentially modulate TCR- and CD28-triggered proximal biochemical events, leading to T-cell unresponsi…

2012

Abstract Background Advanced stages of leprosy show T cell unresponsiveness and lipids of mycobacterial origin are speculated to modulate immune responses in these patients. Present study elucidates the role of phenolicglycolipid (PGL-1) and Mannose-capped lipoarabinomannan (Man-LAM) on TCR- and TCR/CD28- mediated signalling. Results We observed that lipid antigens significantly inhibit proximal early signalling events like Zap-70 phosphorylation and calcium mobilization. Interestingly, these antigens preferentially curtailed TCR-triggered early downstream signalling events like p38 phosphorylation whereas potentiated that of Erk1/2. Further, at later stages inhibition of NFAT binding, IL-2…

LipopolysaccharidesEndocrinology Diabetes and MetabolismT-LymphocytesClinical BiochemistryPGL-1Man-LAMGene ExpressionLymphocyte ActivationJurkat cellsJurkat CellsEndocrinologyT-cell activationIL-2 receptorPhosphorylationExtracellular Signal-Regulated MAP KinasesPromoter Regions Geneticlcsh:RC620-627Protein Kinase CImmunity CellularZAP-70 Protein-Tyrosine KinaseCD28hemic and immune systemsCell biologyMycobacterium lepraelcsh:Nutritional diseases. Deficiency diseasesmedicine.anatomical_structureHost-Pathogen InteractionsProtein BindingMAP Kinase Signaling SystemT cellReceptors Antigen T-Cellchemical and pharmacologic phenomenaBiologyImmune systemCD28 AntigensLeprosymedicineHumansSecretionCalcium SignalingCell ProliferationBiochemistry medicalAntigens BacterialLipoarabinomannanNFATC Transcription FactorsResearchBiochemistry (medical)T-cell receptorInterleukin-2 Receptor alpha SubunitMycobacteriaGene Expression RegulationAnergyImmunologyLeukocytes MononuclearInterleukin-2GlycolipidsLipids in Health and Disease
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CD38 expression enhances sensitivity of lymphoma T and B cell lines to biochemical and receptor-mediated apoptosis

2006

CD38 has been widely characterised both as an ectoenzyme and as a receptor. In the present paper, we investigated the role of CD38 as possible modulator of apoptosis. CD38-positive (CD38(+)) and negative (CD38(-)) fractions, obtained by sorting CD38(+) cells from lymphoma T (Jurkat) and lymphoma B (Raji) and by transfecting lymphoma LG14 and myeloid leukemia K562 cell lines, were used. Cellular subpopulations were exposed to different triggers (H(2)O(2), UV-B, alpha-TOS and hrTRAIL) and the extent of apoptosis was determined by Annexin V-FITC/PI assay. Our data showed that, in lymphoma cells, propensity to apoptosis was significantly linked to CD38 expression and that, remarkably, such resp…

Lymphoma B-CellCD30Ultraviolet RaysTocopherolsApoptosisCD38BiologyLymphoma T-CellJurkat cellsTNF-Related Apoptosis-Inducing LigandJurkat Cellsimmune system diseasesAnnexinCell Line Tumorhemic and lymphatic diseasesmedicineHumansVitamin EAnnexin A5B cellhemic and immune systemsHydrogen PeroxideCell BiologyGeneral MedicineOligonucleotides AntisenseFlow CytometryADP-ribosyl Cyclase 1Antigens DifferentiationMolecular biologyBCL10medicine.anatomical_structureApoptosisAnnexin A5K562 CellsFluorescein-5-isothiocyanateCell Biology International
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Targeted oligonucleotide delivery in human lymphoma cell lines using a polyethyleneimine based immunopolyplex.

2002

The efficacy of antisense gene therapy depends on efficient delivery of oligonucleotides into targeted cells. Although polyethyleneimine based polyplexes have been reported as good transfection reagents, they are inefficient in lymphoid cell transfection. We report the construction of an immunopolyplex, a targeted nonviral vector based on a polyplex backbone and its application for oligonucleotide transfer on human lymphoma cell lines. The salient characteristic of immunopolyplex lies in the possibility of easily replacing the targeting element (antibody), leaving the polyplex backbone intact. Furthermore, a study was made of the influence of endocytosis inhibitors on immunopolyplex activit…

LymphomaOligonucleotidemedia_common.quotation_subjectEndocytic cycleGenetic VectorsOligonucleotidesPharmaceutical ScienceTransfectionBiologyEndocytosisJurkat cellsMolecular biologyIn vitroDrug Delivery SystemsCell cultureTumor Cells CulturedHumansPolyethyleneimineInternalizationmedia_commonJournal of controlled release : official journal of the Controlled Release Society
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Eicosapentaenoic acid and docosahexaenoic acid modulate MAP kinase (ERK1/ERK2) signaling in human T cells

2001

This study was conducted on human Jurkat T cell lines to elucidate the role of EPA and DHA, n-3 PUFA, in the modulation of two mitogen-activated protein (MAP) kinases, that is, extracellular signal-regulated kinases 1 and 2 (ERK1 and ERK2). The n-3 PUFA alone failed to induce phosphorylation of ERK1/ERK2. We stimulated the MAP kinase pathway with anti-CD3 antibodies and phorbol 12-myristate 13-acetate (PMA), which act upstream of the MAP kinase (MAPK)/ERK kinase (MEK) as U0126, an MEK inhibitor, abolished the actions of these two agents on MAP kinase activation. EPA and DHA diminished the PMA- and anti-CD3-induced phosphorylation of ERK1/ERK2 in Jurkat T cells. In the present study, PMA act…

MAPK/ERK pathwayCD3 ComplexDocosahexaenoic AcidsMAP Kinase Signaling SystemT-LymphocytesQD415-436Arachidonic AcidsLymphocyte Activationfatty acidsBiochemistryJurkat cellsAntibodiesJurkat Cellschemistry.chemical_compoundEndocrinologyHumansPhosphorylationProtein Kinase CProtein kinase CMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3MAP kinase kinase kinasebiologyKinaseIonomycinfood and beveragesCell BiologyCell biologyEnzyme ActivationBiochemistrychemistryMitogen-activated protein kinasebiology.proteinPhorbolTetradecanoylphorbol AcetatePhosphorylationlipids (amino acids peptides and proteins)T cell receptorMitogen-Activated Protein KinasesJournal of Lipid Research
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Inhibition of c-MYC with involvement of ERK/JNK/MAPK and AKT pathways as a novel mechanism for shikonin and its derivatives in killing leukemia cells

2015

Leukemia remains life-threatening despite remarkable advances in chemotherapy. The poor prognosis and drug resistance are challenging treatment. Novel drugs are urgently needed. Shikonin, a natural naphthoquinone, has been previously shown by us to be particularly effective towards various leukemia cell lines compared to solid tumors. However, the underlying mechanisms are still poorly understood. Here, we investigated shikonin and 14 derivatives on U937 leukemia cells. Four derivatives (isobutyrylshikonin, 2-methylbutyrylshikonin, isovalerylshikonin and β,β-dimethylacrylshikonin) were more active than shikonin. AnnexinV-PI analysis revealed that shikonins induced apoptosis. Cell cycle G1/S…

MAPK/ERK pathwayMAP Kinase Signaling Systemshikonin and its derivativesJurkat cellsProto-Oncogene Proteins c-mycCell Line TumormedicineHumansacute leukemiaExtracellular Signal-Regulated MAP KinasesProtein kinase BPI3K/AKT/mTOR pathwayMitogen-Activated Protein Kinase KinasesLeukemiaU937 cellERK/JNK/MAP kinasesbusiness.industryAnti-Inflammatory Agents Non-SteroidalJNK Mitogen-Activated Protein KinasesU937 CellsCell cyclemedicine.diseaseLeukemiac-MYCAKT pathwayOncologyCancer researchSignal transductionbusinessProto-Oncogene Proteins c-aktResearch PaperNaphthoquinonesSignal TransductionOncotarget
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B-Raf-mediated signaling pathway regulates T cell development

2008

The activities of the Raf kinase family proteins control extracellular signal-regulated kinase (ERK) activation in many aspects of cellular responses. However, the relative contributions of individual isozymes to cellular functions including T cell responses are still unclear. In addition to Raf-1, another Raf family kinase, B-Raf, is expressed in murine thymocytes and peripheral T cells, and its activation was induced by TCR stimulation. Here, we investigated the function of B-Raf in development of T cells by generating chimeric mice in which a T cell-compromised host was reconstituted with fetal liver-derived cells from embryonic lethal B-Raf-deficient mice. Although B-Raf was dispensable…

MAPK/ERK pathwayProto-Oncogene Proteins B-rafT cellCellular differentiationT-LymphocytesImmunologyThymus GlandBiologyLymphocyte ActivationJurkat cellsArticleJurkat CellsMicemedicineImmunology and AllergyCytotoxic T cellAnimalsHumansExtracellular Signal-Regulated MAP KinasesCells CulturedRetrospective StudiesMice KnockoutZAP70T-cell receptorCell DifferentiationMolecular biologyCoculture TechniquesCell biologyMice Inbred C57BLmedicine.anatomical_structureEnzyme InductionCD8Signal Transduction
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Thapsigargin-stimulated MAP kinase phosphorylation via CRAC channels and PLD activation: inhibitory action of docosahexaenoic acid.

2004

AbstractThis study was conducted on human Jurkat T-cells to investigate the role of depletion of intracellular Ca2+ stores in the phosphorylation of two mitogen-activated protein kinases (MAPKs), i.e. extracellular signal-regulated kinase (ERK) 1 and ERK2, and their modulation by a polyunsaturated fatty acid, docosahexaenoic acid (DHA). We observed that thapsigargin (TG) stimulated MAPK activation by store-operated calcium (SOC) influx via opening of calcium release-activated calcium (CRAC) channels as tyrphostin-A9, a CRAC channel blocker, and two SOC influx inhibitors, econazole and SKF-96365, diminished the action of the former. TG-stimulated ERK1/ERK2 phosphorylation was also diminished…

MAPK/ERK pathwayThapsigarginDocosahexaenoic AcidsBiophysicschemistry.chemical_elementCalciumBiochemistryDiglycerideschemistry.chemical_compoundJurkat CellsStructural BiologyGeneticsPhospholipase DHumansPhosphorylationMolecular BiologyProtein kinase CProtein Kinase CDiacylglycerol kinaseMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Phospholipase CChemistryKinasePhospholipase DRyanodine Receptor Calcium Release ChannelCell BiologyJurkat T-cellCell biologyEnzyme Activationenzymes and coenzymes (carbohydrates)Docosahexaenoic acidFatty Acids UnsaturatedThapsigarginlipids (amino acids peptides and proteins)CalciumMitogen-Activated Protein KinasesFEBS letters
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Differential inhibition of TRAIL-mediated DR5-DISC formation by decoy receptors 1 and 2.

2006

International audience; Tumor necrosis factor (TNF)-related apoptosis-inducing ligand (TRAIL) is a member of the TNF family that induces cancer cell death by apoptosis with some selectivity. TRAIL-induced apoptosis is mediated by the transmembrane receptors death receptor 4 (DR4) (also known as TRAIL-R1) and DR5 (TRAIL-R2). TRAIL can also bind decoy receptor 1 (DcR1) (TRAIL-R3) and DcR2 (TRAIL-R4) that fail to induce apoptosis since they lack and have a truncated cytoplasmic death domain, respectively. In addition, DcR1 and DcR2 inhibit DR4- and DR5-mediated, TRAIL-induced apoptosis and we demonstrate here that this occurs through distinct mechanisms. While DcR1 prevents the assembly of the…

MESH : Hela CellsMESH: Membrane GlycoproteinsMESH: Membrane MicrodomainsDecoy Receptor 1ApoptosisMESH : Membrane GlycoproteinsReceptors Tumor Necrosis FactorTNF-Related Apoptosis-Inducing LigandMESH : TNF-Related Apoptosis-Inducing LigandJurkat Cells0302 clinical medicineMESH : Tumor Necrosis Factor Decoy ReceptorsMESH: Jurkat CellsDecoy receptorsReceptorCells CulturedMESH : Jurkat CellsMESH : Tumor Necrosis Factor-alpha0303 health sciencesMembrane GlycoproteinsMESH : Protein BindingArticlesMESH : Tumor Necrosis Factor Receptor-Associated Peptides and ProteinsTumor Necrosis Factor Receptor-Associated Peptides and ProteinsCell biology030220 oncology & carcinogenesisCaspasesDeath-inducing signaling complexApoptosis/drug effects; Apoptosis Regulatory Proteins/antagonists & inhibitors; Apoptosis Regulatory Proteins/pharmacology; Caspases/metabolism; Cells Cultured; Death Domain Receptor Signaling Adaptor Proteins; Enzyme Activation/drug effects; GPI-Linked Proteins; HeLa Cells; Humans; Jurkat Cells; Membrane Glycoproteins/antagonists & inhibitors; Membrane Glycoproteins/pharmacology; Membrane Microdomains/drug effects; Protein Binding/drug effects; Receptors TNF-Related Apoptosis-Inducing Ligand; Receptors Tumor Necrosis Factor/metabolism; TNF-Related Apoptosis-Inducing Ligand; Tumor Necrosis Factor Decoy Receptors; Tumor Necrosis Factor Receptor-Associated Peptides and Proteins/metabolism; Tumor Necrosis Factor-alpha/antagonists & inhibitors; Tumor Necrosis Factor-alpha/pharmacologyMESH : Apoptosis Regulatory ProteinsMESH: TNF-Related Apoptosis-Inducing LigandProtein BindingMESH: Cells CulturedDeath Domain Receptor Signaling Adaptor ProteinsMESH: Enzyme ActivationBiologyMESH: Tumor Necrosis Factor Receptor-Associated Peptides and ProteinsGPI-Linked Proteins03 medical and health sciencesMembrane MicrodomainsCell surface receptorMESH : Cells Cultured[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyReceptors Tumor Necrosis Factor Member 10cHumansMESH: Protein Binding[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH: Receptors TNF-Related Apoptosis-Inducing LigandMESH : Receptors TNF-Related Apoptosis-Inducing LigandMolecular Biology[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular Biology030304 developmental biologyDeath domainMESH: CaspasesMESH: HumansTumor Necrosis Factor-alphaMESH: Apoptosis Regulatory ProteinsMESH: ApoptosisMESH : HumansCell BiologyMESH: Receptors Tumor Necrosis FactorMESH: Tumor Necrosis Factor Decoy ReceptorsMESH : Receptors Tumor Necrosis FactorEnzyme ActivationMESH: Hela CellsReceptors TNF-Related Apoptosis-Inducing LigandTumor Necrosis Factor Decoy ReceptorsApoptosisMESH: Tumor Necrosis Factor-alphaMESH : Membrane MicrodomainsMESH : CaspasesApoptosis Regulatory ProteinsMESH : Enzyme ActivationMESH : ApoptosisMESH : Death Domain Receptor Signaling Adaptor ProteinsTumor Necrosis Factor Decoy ReceptorsHeLa CellsMESH: Death Domain Receptor Signaling Adaptor Proteins
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