Search results for "PROTEIN KINASES"

showing 10 items of 427 documents

Central Modulatory Neurons Control Fuel Selection in Flight Muscle of Migratory Locust

2003

Insect flight is one of the most intense and energy-demanding physiological activities. High carbohydrate oxidation rates are necessary for take-off, but, to spare the limited carbohydrate reserves, long-distance flyers, such as locusts, soon switch to lipid as the main fuel. We demonstrate that before a flight, locust muscles are metabolically poised for take-off by the release of octopamine from central modulatory dorsal unpaired median (DUM) neurons, which increases the levels of the potent glycolytic activator fructose 2,6-bisphosphate in flight muscle. Because DUM neurons innervating the flight muscles are active during rest but selectively inhibited during flight, they stimulate carbo…

Central Nervous SystemMalemedicine.medical_specialtyGrasshoppersBrief CommunicationInsect flightCarbohydrate catabolismInternal medicinemedicineFructosediphosphatesPremovement neuronal activityAnimalsGlycolysisProtein kinase AMuscle SkeletalOctopamineNeuronsbiologyGeneral NeuroscienceMigratory locustbiology.organism_classificationCyclic AMP-Dependent Protein KinasesEndocrinologyFlight AnimalOctopamine (neurotransmitter)FemaleGlycolysisLocustSignal Transduction
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Mechanisms of ceramide-induced COX-2-dependent apoptosis in human ovarian cancer OVCAR-3 cells partially overlapped with resveratrol.

2013

Ceramide is a member of the sphingolipid family of bioactive molecules demonstrated to have profound, diverse biological activities. Ceramide is a potential chemotherapeutic agent via the induction of apoptosis. Exposure to ceramide activates extracellular-signal-regulated kinases (ERK)1/2- and p38 kinase-dependent apoptosis in human ovarian cancer OVCAR-3 cells, concomitant with an increase in the expression of COX-2 and p53 phosphorylation. Blockade of cyclooxygenase-2 (COX-2) activity by siRNA or NS398 correspondingly inhibited ceramide-induced p53 Ser-15 phosphorylation and apoptosis; thus COX-2 appears at the apex of the p38 kinase-mediated signaling cascade induced by ceramide. Induct…

CeramideMAP Kinase Signaling Systemp38 mitogen-activated protein kinasesApoptosisBiologyResveratrolCeramidesBiochemistryp38 Mitogen-Activated Protein KinasesGene Expression Regulation Enzymologicchemistry.chemical_compoundCell Line TumorStilbenesHumansPhosphorylationRNA Small InterferingMolecular BiologyNitrobenzenesCaspase 7Membrane Potential MitochondrialOvarian NeoplasmsSulfonamidesKinaseCaspase 3Anti-Inflammatory Agents Non-SteroidalCell BiologyLipid signalingSphingolipidCell biologyGene Expression Regulation NeoplasticchemistryApoptosisCyclooxygenase 2ResveratrolFemaleSignal transductionTumor Suppressor Protein p53Journal of cellular biochemistry
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Anandamide-induced apoptosis in Chang liver cells involves ceramide and JNK/AP-1 pathway

2006

In the present study we demonstrate that anandamide, the most important endogenous cannabinoid, markedly induced apoptosis in Chang liver cells, an immortalized non-tumor cell line derived from normal liver tissue, while it induced only modest effects in a number of hepatoma cell lines. The apoptotic effect was reduced by methyl-beta-cyclodextrin, a membrane cholesterol depletor, suggesting an interaction between anandamide and the membrane microdomains named lipid rafts. Anandamide effects were mediated by the production of ceramide, as demonstrated by experiments performed with the sphingomyelinase inhibitor, desipramine, or with the sphingomyelinase activator, melittin. This conclusion w…

CeramideProgrammed cell deathFas Ligand ProteinCell SurvivalPolyunsaturated AlkamidesLiver cytologyp38 mitogen-activated protein kinasesBlotting WesternApoptosisArachidonic AcidsBiologyCeramidesCell LineMembrane Potentialschemistry.chemical_compoundCell Line TumorProto-Oncogene ProteinsGeneticsHumansEnzyme InhibitorsMembrane GlycoproteinsBcl-2-Like Protein 11Dose-Response Relationship DrugDesipramineJNK Mitogen-Activated Protein KinasesMembrane ProteinsFree Radical ScavengersGeneral MedicineAnandamideEndocannabinoid systemAcetylcysteineCell biologyEnzyme ActivationTranscription Factor AP-1cannabinoids apoptosis tumor cells JNK/AP1LiverchemistryApoptosisCaspasesMitochondrial MembranesTumor Necrosis FactorsApoptosis Regulatory ProteinsSphingomyelinEndocannabinoidsSignal TransductionInternational Journal of Molecular Medicine
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Ras-related GTPase Rhob represses NF-kappaB signaling.

2000

rhoB encoding a Ras-related GTPase is immediate-early inducible by genotoxic treatments, indicating that it is part of the cellular stress response. Here, we investigated the influence of RhoB on signal pathways that are rapidly evoked by genotoxic compounds. The data obtained show that wild-type RhoB neither affects activation of mitogen-activated protein kinases nor AP-1-dependent gene expression. However, RhoB inhibited both basal and genotoxic agent-stimulated activity of the transcription factor nuclear factor kappaB (NF-kappaB). Thus, RhoB attenuated alkylation-induced increase in the DNA binding activity of NF-kappaB and abrogated NF-kappaB-driven gene expression. Furthermore, RhoB i…

ChemistryKinaseRHOBNF-kappa BCell BiologyGTPaseTransfectionGenotoxic Stress3T3 CellsTransfectionBiochemistryRatsMiceCellular stress responseGene expressionCancer researchAnimalsMitogen-Activated Protein KinasesrhoB GTP-Binding ProteinMolecular BiologyTranscription factorMonomeric GTP-Binding ProteinsSignal TransductionThe Journal of biological chemistry
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Dissection of the elements of osmotic stress response transcription factor Hot1 involved in the interaction with MAPK Hog1 and in the activation of t…

2013

Abstract The response to hyperosmotic stress is mediated by the HOG pathway. The MAP kinase Hog1 activates several transcription factors, regulates chromatin-modifying enzymes and, through its interaction with RNA polymerase II, it directs this enzyme to osmotic stress-controlled genes. For such targeting, this kinase requires the interaction with transcription factors Hot1 and Sko1. However, phosphorylation of these proteins by Hog1 is not required for their functionality. In this study, we aim to identify the Hot1 elements involved in Hog1-binding and in the activation of transcription. Two-hybrid experiments demonstrated that the Hot1 sequence between amino acids 340 and 534 and the CD e…

Chromatin ImmunoprecipitationSaccharomyces cerevisiae ProteinsTranscription GeneticResponse elementBiophysicsRNA polymerase IIE-boxSaccharomyces cerevisiaeReal-Time Polymerase Chain ReactionResponse ElementsBiochemistryOsmoregulationStructural BiologyGene Expression Regulation FungalGeneticsImmunoprecipitationRNA MessengerPhosphorylationPromoter Regions GeneticMolecular BiologyTranscription factorRNA polymerase II holoenzymeGeneral transcription factorbiologyReverse Transcriptase Polymerase Chain ReactionChromatinBiochemistrybiology.proteinTranscription factor II DMitogen-Activated Protein KinasesTranscription factor II BProtein BindingTranscription FactorsBiochimica et biophysica acta
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The Saccharomyces cerevisiae Hot1p regulated gene YHR087W (HGI1) has a role in translation upon high glucose concentration stress.

2012

Abstract Background While growing in natural environments yeasts can be affected by osmotic stress provoked by high glucose concentrations. The response to this adverse condition requires the HOG pathway and involves transcriptional and posttranscriptional mechanisms initiated by the phosphorylation of this protein, its translocation to the nucleus and activation of transcription factors. One of the genes induced to respond to this injury is YHR087W. It encodes for a protein structurally similar to the N-terminal region of human SBDS whose expression is also induced under other forms of stress and whose deletion determines growth defects at high glucose concentrations. Results In this work …

Chromatin ImmunoprecipitationTranslation<it>Saccharomyces cerevisiae</it>Saccharomyces cerevisiae Proteinslcsh:QH426-470Monosaccharide Transport ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiaeBiologyGene YHR087WHog1pTranscripció genèticaEukaryotic translationStress PhysiologicalPolysomeGene Expression Regulation FungalGene expressionProtein biosynthesisHigh glucose osmotic stresslcsh:QH573-671Transcription factorMolecular BiologyRegulation of gene expressionGenetic transcriptionlcsh:CytologyComputational BiologyTranslation (biology)biology.organism_classificationBlotting NorthernExpressió gènicaYeastlcsh:GeneticsGlucoseBiochemistryMicroscopy FluorescencePolyribosomesProtein BiosynthesisPolysomesGene <it>YHR087W</it>Gene expressionLlevatsMitogen-Activated Protein KinasesHot1pTranscription FactorsResearch ArticleBMC molecular biology
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Metabolomics of the effect of AMPK activation by AICAR on human umbilical vein endothelial cells

2011

AMP-activated protein kinase (AMPK) is a metabolic master switch expressed in a great number of cells and tissues. AMPK is thought to modulate the cellular response to different stresses that increase cellular AMP concentration. The adenosine analog, 5-aminoimidazole-4-carboxamide-1-β-D-ribofuranoside (AICAR) is an AMPK activator used in many studies to assess the effects of AMPK activation on cellular metabolism and function. However, the effect of AICAR on cell metabolism reaches many different pathways and metabolites, some of which do not seem to be fully related to AMPK activation. We have now for the first time used NMR metabolomics on human umbilical vein endothelial cells (HUVEC) fo…

Citric Acid CycleMetabolic networkAMP-Activated Protein KinasesBiologyUmbilical veinMetabolomicsHuman Umbilical Vein Endothelial CellsGeneticsmedicineHumansMetabolomicsProtein kinase ANuclear Magnetic Resonance BiomolecularCells CulturedPhospholipidsAnalysis of VarianceActivator (genetics)AMPKGeneral MedicineMetabolismAminoimidazole CarboxamideAdenosineCell biologyEnzyme ActivationBiochemistryMetabolomeRibonucleosidesGlycolysisMetabolic Networks and Pathwaysmedicine.drugInternational Journal of Molecular Medicine
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MAP kinase p38 and its relation to T cell anergy and suppressor function of regulatory T cells

2008

Diverse regulatory T cell populations (Treg) are important for the control of self tolerance and immune homeostasis. These include naturally occurring CD4+CD25+ Treg (nTreg) and induced Treg (iTreg). Tolerogenic dendritic cells, modulated by IL-10, are able to convert peripheral T cells into iTreg. These are anergic and characterized by a G(1) cell cycle arrest, dependent on elevated levels of the cdk inhibitor p27(Kip1). Novel data revealed a distinct pattern of MAP kinase activation in iTreg different from clonal T cell anergy, with enhanced activation of the p38-MAPKAP-K2/3 pathway. p38 is involved in cell cycle control and its activity is a prerequisite for the induction and maintenance…

Clonal AnergyCell cycle checkpointClonal anergyRegulatory T cellT cellCell CycleCell BiologyBiologyCell cycleT-Lymphocytes Regulatoryp38 Mitogen-Activated Protein KinasesCell biologymedicine.anatomical_structuremedicineAnimalsHumansCytotoxic T cellIL-2 receptorAntigen-presenting cellMolecular BiologyCyclin-Dependent Kinase Inhibitor p27Developmental BiologyCell Cycle
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Aryl hydrocarbon receptor activation by cAMP vs. dioxin: divergent signaling pathways.

2005

Even before the first vertebrates appeared on our planet, the aryl hydrocarbon receptor ( AHR ) gene was present to carry out one or more critical life functions. The vertebrate AHR then evolved to take on functions of detecting and responding to certain classes of environmental toxicants. These environmental pollutants include polycyclic aromatic hydrocarbons (e.g., benzo[ a ]pyrene), polyhalogenated hydrocarbons, dibenzofurans, and the most potent small-molecular-weight toxicant known, 2,3,7,8-tetrachlorodibenzo- p -dioxin (TCDD or dioxin). After binding of these ligands, the activated AHR translocates rapidly from the cytosol to the nucleus, where it forms a heterodimer with aryl hydroc…

Conservation of Natural ResourcesAryl hydrocarbon receptor nuclear translocatorPolychlorinated DibenzodioxinsTime FactorsTranscription GeneticGenetic VectorsGreen Fluorescent ProteinsImmunoblottingActive Transport Cell NucleusEnvironmentDioxinsLigandschemistry.chemical_compoundMiceCytosolGenes ReporterCell Line TumorCyclic AMPAnimalsImmunoprecipitationReceptorFluorescent Antibody Technique IndirectCell NucleusMultidisciplinarybiologyChemistryColforsinEndogenous mediatorrespiratory systemBiological SciencesAryl hydrocarbon receptorCyclic AMP-Dependent Protein KinasesCytosolProtein TransportBiochemistryBucladesineMicroscopy FluorescenceReceptors Aryl HydrocarbonSecond messenger systembiology.proteinProstaglandinsEnvironmental PollutantsSignal transductionDimerizationToxicantPlasmidsProtein BindingSignal TransductionProceedings of the National Academy of Sciences of the United States of America
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Heme oxygenase-1 inhibits apoptosis in Caco-2 cells via activation of Akt pathway

2005

Heme oxygenase-1 can play a protective role against cellular stress. In colon cancer cells, these effects would be relevant to oncogenesis and resistance to chemotherapy. The aim of the study was to examine the effects of heme oxygenase-1 induction on cell survival in a human colon cancer cell line, Caco-2. Serum deprivation induced apoptosis, reduced Akt and p38 phosphorylation, and increased p21(Cip/WAF1) levels. Heme oxygenase-1 induction by treatment with cobalt protoporphyrin IX resulted in resistance to apoptosis, activation of Akt, reduction in p21(Cip/WAF1) levels and modification of bcl2/bax ratio towards survival. Indomethacin reduced apoptosis but in contrast to heme oxygenase-1,…

Cyclin-Dependent Kinase Inhibitor p21BiliverdinCell SurvivalChemistryBilirubinp38 mitogen-activated protein kinasesProtoporphyrinsApoptosisCell BiologyBiochemistryCulture Media Serum-FreeCell biologyHeme oxygenasechemistry.chemical_compoundApoptosisEnzyme InductionHumansCaco-2 CellsProto-Oncogene Proteins c-aktHemeProtein kinase BHeme Oxygenase-1PI3K/AKT/mTOR pathwayThe International Journal of Biochemistry &amp; Cell Biology
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