Search results for "Phosphorylation"

showing 10 items of 975 documents

Loss of p53 Attenuates the Contribution of IL-6 Deletion on Suppressed Tumor Progression and Extended Survival in Kras-Driven Murine Lung Cancer

2013

Interleukin-6 (IL-6) is involved in lung cancer tumorigenesis, tumor progression, metastasis, and drug resistance. Previous studies show that blockade of IL-6 signaling can inhibit tumor growth and increase drug sensitivity in mouse models. Clinical trials in non-small cell lung cancer (NSCLC) reveal that IL-6 targeted therapy relieves NSCLC-related anemia and cachexia, although other clinical effects require further study. We crossed IL-6(-/-) mice with Kras(G12D) mutant mice, which develop lung tumors after activation of mutant Kras(G12D), to investigate whether IL-6 inhibition contributes to tumor progression and survival time in vivo. Kras(G12D); IL-6(-/-) mice exhibited increased tumor…

Lung Neoplasmsmedicine.medical_treatmentlcsh:Medicinemedicine.disease_causeMetastasisTargeted therapyMice0302 clinical medicineCarcinoma Non-Small-Cell LungNeoplasm MetastasisPhosphorylationlcsh:Science0303 health sciencesMultidisciplinary3. Good healthGene Expression Regulation Neoplastic030220 oncology & carcinogenesisDisease ProgressionKRASResearch ArticleSignal TransductionSTAT3 Transcription FactorMice TransgenicBiologyProto-Oncogene Proteins p21(ras)03 medical and health sciencesFLOXmedicineAnimalsHumansLung cancerneoplasms030304 developmental biologyChemokine CCL20Interleukin-6Tumor Necrosis Factor-alphalcsh:RCancermedicine.diseaseSurvival Analysisdigestive system diseasesrespiratory tract diseasesDisease Models AnimalTumor progressionMutationCancer researchChemokine CCL19lcsh:QTumor Suppressor Protein p53CarcinogenesisPLoS ONE
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Western blotting as a method for studying cell-biomaterial interactions: The role of protein collection

2000

Research of cell-biomaterial interactions is building on knowledge and methods available in cell and molecular biology. Western blotting is one of the options to characterize protein expression in cell populations. Method transfer to biomaterial model systems is not trivial because of the structure that exists in many biomaterials, preventing the collection of cell lysate by mechanical means. In this technical report, we describe the influence of different protein collection methods in a model system for cell-biomaterial interactions, consisting of endothelial cells exposed to different stimuli. In particular, the influence of trypsinization before lysis, and handling complexity were determ…

Lysismedicine.diagnostic_testCellBiomedical EngineeringTyrosine phosphorylationProtein tyrosine phosphataseProtein degradationBiologyTrypsinizationBiomaterialsBlotchemistry.chemical_compoundmedicine.anatomical_structureBiochemistrychemistryWestern blotmedicineJournal of Biomedical Materials Research
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Coupling of Contact Sensitizers to Thiol Groups is a Key Event for the Activation of Monocytes and Monocyte-Derived Dendritic Cells

2003

Strong contact sensitizers are able to induce distinct signal transduction mechanisms in antigen-presenting cells by coupling to cell proteins. The predominant target structures of haptens are thought to be thiol and amino groups in cysteine and lysine residues. We studied whether coupling of small reactive chemicals to thiol or amino groups might be responsible for the activation of monocytes and mature monocyte-derived dendritic cells. Human peripheral blood mononuclear cells were stimulated in vitro with subtoxic concentrations of the strong haptens 5-chloro-2-methylisothiazolinone plus 2-methylisothiazolinone and 2, 4, 6-trinitrochlorobenzene, the thiol-reactive reagents N-hydroxymaleim…

MAP Kinase Signaling SystemCD14SuccinimidesPicryl ChlorideDermatologyAcetatesPeripheral blood mononuclear cellBiochemistryamino groupsAntioxidantsMonocytesMaleimideschemistry.chemical_compoundAnti-Infective AgentsmedicineHumansCysteineSulfhydryl CompoundsPhosphorylationAntigen-presenting cellMolecular Biologythiol groupsChemistryMonocyteLysineSulfhydryl ReagentsTyrosine phosphorylationDendritic cellDendritic CellsCell BiologyThiazolesmedicine.anatomical_structureBiochemistryEthylmaleimidehaptenTyrosineSignal transductionsignal transductionCysteineInterleukin-1Journal of Investigative Dermatology
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p38 MAPK-dependent shaping of the keratin cytoskeleton in cultured cells

2007

Plasticity of the resilient keratin intermediate filament cytoskeleton is an important prerequisite for epithelial tissue homeostasis. Here, the contribution of stress-activated p38 MAPK to keratin network organization was examined in cultured cells. It was observed that phosphorylated p38 colocalized with keratin granules that were rapidly formed in response to orthovanadate. The same p38p recruitment was noted during mitosis, in various stress situations and in cells producing mutant keratins. In all these situations keratin 8 became phosphorylated on S73, a well-known p38 target site. To demonstrate that p38-dependent keratin phosphorylation determines keratin organization, p38 activity …

MAP Kinase Signaling SystemIntermediate filament cytoskeletonmacromolecular substancesBiologyp38 Mitogen-Activated Protein KinasesArticleKeratinHumansPhosphorylationCytoskeletonProtein Kinase InhibitorsMitosisResearch ArticlesCells CulturedCytoskeletonchemistry.chemical_classificationKeratin Filamentintegumentary systemCell BiologyCell biologyKeratin 5chemistryKeratin 8KeratinsPhosphorylationVanadatesJournal of Cell Biology
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Neuroprotection elicited by P2Y13 receptors against genotoxic stress by inducing DUSP2 expression and MAPK signaling recovery.

2014

AbstractNucleotides activating P2Y13 receptors display neuroprotective actions against different apoptotic stimuli in cerebellar granule neurons. In the present study, P2Y13 neuroprotection was analyzed in conditions of genotoxic stress. Exposure to cisplatin and UV radiation induced caspase-3-dependent apoptotic cell death, and p38 MAPK signaling de-regulation. Pre-treatment with P2Y13 nucleotide agonist, 2methyl-thio-ADP (2MeSADP), restored granule neuron survival and prevented p38 long-lasting activation induced by cytotoxic treatments. Microarray gene expression analysis in 2MeSADP-stimulated cells revealed over-representation of genes related to protein phosphatase activity. Among them…

MAPK/ERK pathwayAgonistmedicine.drug_classMAP Kinase Signaling SystemUltraviolet Raysp38 mitogen-activated protein kinasesDUSPp38Genotoxic StressCREBNeuroprotectionMAPK protein phosphataseModels Biologicalp38 Mitogen-Activated Protein KinasesNucleotide receptorP2Y13 receptorCa2+/calmodulin-dependent protein kinaseCerebellummedicineAnimalsPhosphorylationRats WistarReceptorMolecular BiologyCell NucleusNeuronsbiologyCell DeathCaspase 3Receptors Purinergic P2Dual Specificity Phosphatase 2Cell BiologyThionucleotidesNeuroprotectionCell biologyRatsAdenosine DiphosphateEnzyme ActivationNeuroprotective AgentsCytoprotectionbiology.proteinCisplatinDNA DamageBiochimica et biophysica acta
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The three α1-adrenoceptor subtypes show different spatio-temporal mechanisms of internalization and ERK1/2 phosphorylation

2013

AbstractWe analyzed the kinetic and spatial patterns characterizing activation of the MAP kinases ERK 1 and 2 (ERK1/2) by the three α1-adrenoceptor (α1-AR) subtypes in HEK293 cells and the contribution of two different pathways to ERK1/2 phosphorylation: protein kinase C (PKC)-dependent ERK1/2 activation and internalization-dependent ERK1/2 activation. The different pathways of phenylephrine induced ERK phosphorylation were determined by western blot, using the PKC inhibitor Ro 31-8425, the receptor internalization inhibitor concanavalin A and the siRNA targeting β-arrestin 2. Receptor internalization properties were studied using CypHer5 technology and VSV-G epitope-tagged receptors. Activ…

MAPK/ERK pathwayArrestinsmedia_common.quotation_subjectBlotting WesternKidneyReal-Time Polymerase Chain ReactionImmunoenzyme TechniquesConstitutive activityReceptors Adrenergic alpha-1Concanavalin AHumansRNA MessengerPKCEnzyme InhibitorsPhosphorylationRNA Small InterferingInternalizationProtein kinase AMolecular BiologyCells CulturedProtein Kinase Cbeta-ArrestinsProtein kinase Cmedia_commonMitogen-Activated Protein Kinase 1G protein-coupled receptor kinaseMitogen-Activated Protein Kinase 3ERK1/2biologyReverse Transcriptase Polymerase Chain ReactionKinaseChemistryCell Biologybeta-Arrestin 2Molecular biologyAdrenaline α1 receptorsEndocytosisMitogen-activated protein kinasebiology.proteinPhosphorylationInternalizationSignal TransductionBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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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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Potentiation of the antitumor effects of both selective cyclooxygenase-1 and cyclooxygenase-2 inhibitors in human hepatic cancer cells by inhibition …

2007

The molecular mechanisms behind the anti-neoplastic effects of non-steroidal anti-inflammatory drugs (NSAIDs) are not completely understood and cannot be explained by the inhibition of the cyclooxygenase (COX) enzymes COX-1 and COX-2 alone. We previously reported that both the selective COX-1 inhibitor SC-560 and the selective COX-2 inhibitor CAY10404 exhibit anti-tumor effects in human hepatoma cells. NSAID inhibitors have many COX-independent actions and, among others, the mitogen-activated protein kinase (MAPK) pathways are targets for NSAIDs. Here, we examined the role of MEK/ERK1/2 signaling in the anti-neoplastic effects of both selective COX-1 and COX-2 inhibitors in two human hepato…

MAPK/ERK pathwayCancer ResearchCarcinoma HepatocellularTime FactorsBlotting WesternApoptosisPharmacologyCOX-1 COX-2 NSAIDs MEK1/2 ERK1/2NitrilesButadienesTumor Cells CulturedHumansCyclooxygenase InhibitorsSulfonesEnzyme InhibitorsPhosphorylationProtein kinase ACell ProliferationPharmacologychemistry.chemical_classificationMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase KinasesMitogen-Activated Protein Kinase 3biologyDose-Response Relationship DrugLiver NeoplasmsCytochromes cLong-term potentiationDrug SynergismIsoxazolesFlow CytometryEnzymeOncologychemistryCyclooxygenase 2CaspasesCancer cellbiology.proteinCyclooxygenase 1Molecular MedicineMEK-ERK PathwayPyrazolesDrug Therapy CombinationCyclooxygenaseHepatoma cellCancer biologytherapy
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Mevalonate pathway inhibitors affect anticancer drug-induced cell death and DNA damage response of human sarcoma cells

2011

Lovastatin (Lov), bisphosphonates (BP) and metformin (Met) are widely used drugs, having in common that they interfere with the mevalonate pathway (MP). The MP generates isoprene moieties required for the function of regulatory GTPases controlling cell proliferation and survival. Here, we addressed the question whether MP inhibitors interfere with the anti-tumor efficacy of anticancer drugs. We comparatively analyzed the effect of equitoxic doses of Lov, BP and Met on cell viability, cell cycle progression, apoptosis and DNA damage response (DDR) of human osteo- and fibrosarcoma cells exposed to doxorubicin or cisplatin. We found that Lov, BP and Met modulated the anticancer drug sensitivit…

MAPK/ERK pathwayCancer ResearchDNA damageFibrosarcomaBlotting WesternMevalonic AcidAntineoplastic AgentsApoptosisBone NeoplasmsTumor Cells CulturedmedicineHumansDoxorubicinLovastatinRNA MessengerPhosphorylationCell ProliferationCisplatinOsteosarcomaDiphosphonatesbiologyReverse Transcriptase Polymerase Chain ReactionCell growthCell CycleMetforminOncologyDoxorubicinApoptosisHMG-CoA reductasebiology.proteinCancer researchMevalonate pathwayCisplatinTumor Suppressor Protein p53DNA DamageSignal Transductionmedicine.drugCancer Letters
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Interferon-α Suppresses cAMP to Disarm Human Regulatory T Cells

2013

Abstract IFN-α is an antineoplastic agent in the treatment of several solid and hematologic malignancies that exerts strong immune- and autoimmune-stimulating activity. However, the mechanisms of immune activation by IFN-α remain incompletely understood, particularly with regard to CD4+CD25highFoxp+ regulatory T cells (Treg). Here, we show that IFN-α deactivates the suppressive function of human Treg by downregulating their intracellular cAMP level. IFN-α–mediated Treg inactivation increased CD4+ effector T-cell activation and natural killer cell tumor cytotoxicity. Mechanistically, repression of cAMP in Treg was caused by IFN-α–induced MAP–ERK kinase (MEK)/extracellular signal-regulated ki…

MAPK/ERK pathwayCancer Researchmedicine.medical_treatmentGraft vs Host DiseaseAutoimmunitychemical and pharmacologic phenomenaBiologyLymphocyte ActivationT-Lymphocytes RegulatoryNatural killer cellMiceImmune systemDownregulation and upregulationT-Lymphocyte SubsetsCyclic AMPmedicineAnimalsHumansIL-2 receptorPhosphorylationExtracellular Signal-Regulated MAP KinasesCells CulturedMitogen-Activated Protein Kinase KinasesInterleukin-2 Receptor alpha SubunitInterferon-alphaFOXP3hemic and immune systemsDNA-Binding ProteinsKiller Cells NaturalSTAT Transcription Factorsmedicine.anatomical_structureCytokineOncologyHumanized mouseImmunologyCancer researchCancer Research
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