Search results for "Mitogen-Activated Protein Kinases"

showing 10 items of 246 documents

Pore-forming toxins activate MAPK p38 by causing loss of cellular potassium.

2009

Mitogen activated protein kinase (MAPK) p38 has emerged as a survival protein in cells that are attacked by bacterial toxins forming small membrane pores. Activation of p38 by pore forming toxins (PFT) has been attributed to osmotic stress, but here we show that loss of K+ is likely to be the critical parameter. Several lines of evidence support this conclusion: first, osmoprotection did not prevent p38-phosphorylation in alpha-toxin-loaded cells. Second, treatment of cells with a K+ ionophore, or simple incubation in K+-free medium sufficed to cause robust p38-phosphorylation. Third, media containing high [K+] prevented p38-activation by Staphylococcus aureus alpha-toxin, Vibrio cholerae c…

Pore Forming Cytotoxic ProteinsOsmotic shockp38 mitogen-activated protein kinasesBacterial ToxinsBiophysicsBiologyHemolysin ProteinsBiochemistryp38 Mitogen-Activated Protein KinasesCell LineCell membraneHemolysin ProteinsmedicineHumansPhosphorylationMolecular BiologyPore-forming toxinEscherichia coli ProteinsCell MembraneHemolysinEpithelial CellsCell BiologyCell biologyEnzyme Activationmedicine.anatomical_structureBiochemistryPotassiumStreptolysinCalciumCytolysinBiochemical and biophysical research communications
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Antitumor effects of dehydroxymethylepoxyquinomicin, a novel nuclear factor-kappaB inhibitor, in human liver cancer cells are mediated through a reac…

2009

Activation of the nuclear transcription factor-kappa B (NF-kappa B) has been implicated in liver tumorigenesis. We evaluated the effects of a novel NF-kappa B inhibitor, dehydroxymethylepoxyquinomicin (DHMEQ), in two human liver cancer cell lines HA22T/VGH and HuH-6. DHMEQ treatment dose dependently decreased the DNA-binding capacity of the NF-kappa B p65 subunit, inhibited cell growth and proliferation, and increased apoptosis as shown by caspase activation, release of cytochrome c, poly(ADP-ribose) polymerase cleavage, and down-regulation of survivin. DHMEQ also induced a dose-dependent activation of mitogen-activated protein kinase kinase/extracellular signal-regulated kinase signaling, …

Programmed cell deathCarcinoma HepatocellularBIOLOGICAL-ACTIVITIESDrug Evaluation PreclinicalDown-RegulationAntineoplastic AgentsApoptosisBiologymedicine.disease_causeACTIVATIONchemistry.chemical_compoundHYDROGEN-PEROXIDEENDOPLASMIC-RETICULUM STRESSCell Line TumorSurvivinNADPH OXIDASEmedicineHumansOXIDATIVE STRESSProtein kinase AEndoplasmic Reticulum Chaperone BiPINDUCED APOPTOSISCell ProliferationPharmacologySettore MED/12 - GastroenterologiaDose-Response Relationship DrugUNFOLDED PROTEIN RESPONSECell growthCyclohexanonesINDUCTIONLiver NeoplasmsDEATHNF-kappa BCytochromes cMolecular biologyCell biologyEnzyme ActivationchemistryApoptosisCaspasesCancer cellBenzamidesSettore BIO/14 - FarmacologiaMolecular MedicineGrowth inhibitionMitogen-Activated Protein KinasesPoly(ADP-ribose) PolymerasesReactive Oxygen SpeciesOxidative stressMolecular pharmacology
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DNA damage-induced cell death by apoptosis

2006

Following the induction of DNA damage, a prominent route of cell inactivation is apoptosis. During the last ten years, specific DNA lesions that trigger apoptosis have been identified. These include O6-methylguanine, base N-alkylations, bulky DNA adducts, DNA cross-links and DNA double-strand breaks (DSBs). Repair of these lesions are important in preventing apoptosis. An exception is O6-methylguanine-thymine lesions, which require mismatch repair for triggering apoptosis. Apoptosis induced by many chemical genotoxins is the consequence of blockage of DNA replication, which leads to collapse of replication forks and DSB formation. These DSBs are thought to be crucial downstream apoptosis-tr…

Programmed cell deathDNA RepairDNA repairDNA damageApoptosisp38 Mitogen-Activated Protein KinasesAnimalsHumansE2F1Molecular BiologybiologyCaspase 2DNA replicationDNAProliferating cell nuclear antigenCaspasesbiology.proteinCancer researchMolecular MedicineDNA mismatch repairTumor Suppressor Protein p53biological phenomena cell phenomena and immunityProto-Oncogene Proteins c-aktAtaxia telangiectasia and Rad3 relatedDNA DamageMutagensSignal TransductionTrends in Molecular Medicine
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Deglycosylated bleomycin induces apoptosis in lymphoma cell via c-jun NH2-terminal kinase but not reactive oxygen species

2007

Bleomycin (BLM) has demonstrated potent activity in treating malignant lymphomas but its therapeutic efficacy is hampered by induction of lung fibrosis. This side effect is related to the ability of the drug to generate reactive oxygen species in lung cells. In the present study, we evaluated the consequences of deglycosylation of BLM in term of cytotoxic activity and generation of reactive oxygen species. When tested on U937 human lymphoma cells, both compounds generated a typical apoptotic phenotype. Cell death induction was associated with Bax oligomerization, dissipation of the mitochondrial membrane potential, release of cytochrome c, caspase activation, chromatin condensation and inte…

Programmed cell deathFas Ligand ProteinLymphomaCellApoptosisDNA FragmentationBiologymedicine.disease_causeBiochemistryTNF-Related Apoptosis-Inducing LigandBleomycinmedicineHumansDeath domainPharmacologychemistry.chemical_classificationReactive oxygen speciesAntibiotics AntineoplasticU937 cellCytochrome cJNK Mitogen-Activated Protein KinasesU937 CellsMolecular biologymedicine.anatomical_structurechemistryBiochemistryApoptosisCaspasesbiology.proteinReactive Oxygen SpeciesOxidative stressBiochemical Pharmacology
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Differential Roles of JNK in ConA/GalN and ConA-Induced Liver Injury in Mice

2008

Tumor necrosis factor-alpha-mediated liver injury can be induced by several different means; however, the signaling events and mechanisms of cell death are likely different. We investigated the mechanism of both apoptotic and necrotic hepatocyte cell death as well as the role of c-Jun NH2-terminal kinase (JNK) in the ConA and ConA/D-galactosamine (GalN) models of murine liver injury. ConA alone induced primarily necrotic cell death with no caspase activation, whereas ConA/GalN induced apoptosis in addition to necrotic cell death. The bi-modal death pattern in the ConA/GalN model was confirmed by the use of transgenic mice expressing a dominant-negative form of Fas-associated death domain in…

Programmed cell deathNecrosisFas-Associated Death Domain ProteinApoptosisGalactosamineMitochondria Liverchemical and pharmacologic phenomenaCaspase 8Pathology and Forensic MedicineMiceNecrosisConcanavalin AmedicineAnimalsPhosphorylationDeath domainLiver injuryCaspase 8biologyLiver DiseasesJNK Mitogen-Activated Protein Kinasesmedicine.diseaseMolecular biologyEnzyme ActivationMice Inbred C57BLDisease Models Animalmedicine.anatomical_structureConcanavalin AApoptosisHepatocytebiology.proteinMutant ProteinsChemical and Drug Induced Liver Injurymedicine.symptomGene DeletionRegular ArticlesBH3 Interacting Domain Death Agonist ProteinThe American Journal of Pathology
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Calcium in plant defence‐signalling pathways

2006

In plant cells, the calcium ion is a ubiquitous intracellular second messenger involved in numerous signalling pathways. Variations in the cytosolic concentration of Ca2+ ([Ca2+]cyt) couple a large array of signals and responses. Here we concentrate on calcium signalling in plant defence responses, particularly on the generation of the calcium signal and downstream calcium-dependent events participating in the establishment of defence responses with special reference to calcium-binding proteins.

Programmed cell deathPhysiologyGene Expressionchemistry.chemical_elementPlant ScienceBiologyCalciumNitric OxideCytosolPhytoalexinsCalcium-binding proteinCalcium SignalingPhosphorylationPlant DiseasesPlant ProteinsCalcium signalingCell DeathPlant ExtractsTerpenesCalcium-Binding ProteinsPlantsPlant cellElicitorCytosolchemistryBiochemistryCalciumMitogen-Activated Protein KinasesSignal transductionReactive Oxygen SpeciesSesquiterpenesNew Phytologist
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Kel1 is a phosphorylation-regulated noise suppressor of the pheromone signaling pathway.

2021

Abstract Mechanisms have evolved that allow cells to detect signals and generate an appropriate response. The accuracy of these responses relies on the ability of cells to discriminate between signal and noise. How cells filter noise in signaling pathways is not well understood. We have analyzed noise suppression in the yeast pheromone signaling pathway. By combining synthetic genetic array screening, mass spectrometry and single-cell time-resolved microscopy, we discovered that the poorly characterized protein Kel1 serves as a major noise suppressor of the pathway. At the molecular level, Kel1 suppresses spontaneous activation of the pheromone response by inhibiting membrane recruitment of…

Programmed cell deathSaccharomyces cerevisiae ProteinsChemistryCellbiologiCell BiologySaccharomyces cerevisiaeSynthetic genetic arrayGeneral Biochemistry Genetics and Molecular BiologyPheromonesCell biologylaw.inventionlawFus3SuppressorPhosphorylationPheromoneSignal transductionMitogen-Activated Protein KinasesPhosphorylationNoiseSte5Adaptor Proteins Signal TransducingCyclin-Dependent Kinase Inhibitor ProteinsSignal TransductionCell reports
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Calcitonin gene-related peptide partly protects cultured smooth muscle cells from apoptosis induced by an oxidative stress via activation of ERK1/2 M…

2003

Abstract Oxidative stress induced by a glucose/glucose oxidase (G/GO) generator system dose-dependently decreased the viability of cultured vascular smooth muscle cells (VSMC) as estimated by MTT assay. Cell death was induced in 40% of cells exposed to 0.2 IU/ml of the free radical generating mixture. Annexin-V labeling, Hoechst staining together with DNA laddering demonstrated that apoptosis was responsible for this cell loss. Pretreatment of the cells with 10−8 M calcitonin gene-related peptide (CGRP) significantly attenuated the damaging effect of the oxidative stress. Indeed, cell viability was estimated to be 80% in CGRP-treated group, instead of 60% in absence of CGRP treatment. This …

Programmed cell deathVascular smooth musclep38 mitogen-activated protein kinasesCalcitonin Gene-Related PeptideMyocytes Smooth MuscleApoptosisBiologyDNA ladderingCalcitonin gene-related peptidemedicine.disease_causeProtective AgentsMuscle Smooth VascularmedicineAnimalsHumansCGRPViability assayRats WistarMolecular BiologyCells CulturedMitogen-Activated Protein Kinase 3integumentary systemSAPKCell BiologyHydrogen PeroxideMAPKMolecular biologyRatsUp-RegulationNeuropeptideOxidative StressMitogen-activated protein kinaseVascular smooth muscle cellbiology.proteinMitogen-Activated Protein KinasesOxidative stressReceptors Calcitonin Gene-Related PeptideSignal TransductionBiochimica et biophysica acta
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Fatty acids liberated from low-density lipoprotein trigger endothelial apoptosis via mitogen-activated protein kinases.

2005

Enzymatic modification of low-density lipoprotein (LDL) as it probably occurs in the arterial intima drastically increases its cytotoxicity, which could be relevant for the progression of atherosclerotic lesions. LDL was treated with a protease and cholesterylesterase to generate a derivative similar to lesional LDL, with a high content of free cholesterol and fatty acids. Exposure of endothelial cells to the enzymatically modified lipoprotein (E-LDL), but not to native or oxidized LDL, resulted in programmed cell death. Apoptosis was triggered by apoptosis signal-regulating kinase 1 dependent phosphorylation of p38. Depletion and reconstitution experiments identified free fatty acids (FFA)…

Programmed cell deathp38 mitogen-activated protein kinasesBlotting WesternApoptosisDNA FragmentationBiologyFatty Acids NonesterifiedMAP Kinase Kinase Kinase 5p38 Mitogen-Activated Protein Kinaseschemistry.chemical_compoundHumansPhosphorylationMolecular BiologyCells CulturedCaspase 7Cell growthKinaseCaspase 3Cell BiologyCell biologyLipoproteins LDLchemistryBiochemistryApoptosisLow-density lipoproteinCaspasesPhosphorylationlipids (amino acids peptides and proteins)Endothelium VascularLipoproteinOleic AcidCell death and differentiation
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Glucocorticoids inhibit MAP kinase via increased expression and decreased degradation of MKP-1

2001

Glucocorticoids inhibit the proinflammatory activities of transcription factors such as AP-1 and NF-kappa B as well as that of diverse cellular signaling molecules. One of these signaling molecules is the extracellular signal-regulated kinase (Erk-1/2) that controls the release of allergic mediators and the induction of proinflammatory cytokine gene expression in mast cells. The mechanism of inhibition of Erk-1/2 activity by glucocorticoids is unknown. Here we report a novel dual action of glucocorticoids for this inhibition. Glucocorticoids increase the expression of the MAP kinase phosphatase-1 (MKP-1) gene at the promoter level, and attenuate proteasomal degradation of MKP-1, which we re…

Proteasome Endopeptidase ComplexCell signalingMitogen-Activated Protein Kinase 3Cell Cycle ProteinsBiologyDexamethasoneGene Expression Regulation EnzymologicArticleGeneral Biochemistry Genetics and Molecular BiologyCell LineImmediate-Early ProteinsProinflammatory cytokineMiceGlucocorticoid receptorMultienzyme ComplexesProtein Phosphatase 1Phosphoprotein PhosphatasesAnimalsEnzyme InhibitorsPhosphorylationMolecular BiologyTranscription factorDNA PrimersMitogen-Activated Protein Kinase 1Regulation of gene expressionMitogen-Activated Protein Kinase 3Base SequenceGeneral Immunology and MicrobiologyKinaseHydrolysisGeneral NeuroscienceDual Specificity Phosphatase 1Cell biologyMice Inbred C57BLCysteine EndopeptidasesMitogen-activated protein kinasebiology.proteinMitogen-Activated Protein KinasesProtein Tyrosine PhosphatasesThe EMBO Journal
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