Search results for " Mitogen-Activated Protein Kinases"

showing 10 items of 175 documents

Differences in the signaling pathways of α(1A)- and α(1B)-adrenoceptors are related to different endosomal targeting.

2013

AIMS: To compare the constitutive and agonist-dependent endosomal trafficking of α(1A)- and α(1B)-adrenoceptors (ARs) and to establish if the internalization pattern determines the signaling pathways of each subtype. METHODS: Using CypHer5 technology and VSV-G epitope tagged α(1A)- and α(1B)-ARs stably and transiently expressed in HEK 293 cells, we analyzed by confocal microscopy the constitutive and agonist-induced internalization of each subtype, and the temporal relationship between agonist induced internalization and the increase in intracellular calcium (determined by FLUO-3 flouorescence), or the phosphorylation of ERK1/2 and p38 MAP kinases (determined by Western blot). RESULTS AND C…

MAPK signaling cascadesEndosomemedia_common.quotation_subjecteducationIntracellular Spacelcsh:MedicineEndosomesSignal transductionERK signaling cascadeBiologyEndocytosisp38 Mitogen-Activated Protein KinasesSignaling PathwaysCell LineMolecular cell biologyReceptors Adrenergic alpha-1Calcium-Mediated Signal TransductionHumansMembrane Receptor SignalingCalcium SignalingInternalizationlcsh:ScienceBiologyCalcium signalingmedia_commonMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3MultidisciplinaryHEK 293 cellslcsh:RNeurotransmitter Receptor SignalingSignaling cascadesNeurotransmittersLipid signalingEndocytosisCell biologyTransport proteinProtein TransportHEK293 CellsCalcium signaling cascadeMembranes and Sortinglcsh:QAdrenergic alpha-1 Receptor AgonistsMolecular NeuroscienceSignal transductionResearch ArticleAdrenergic Signal TransductionNeurosciencePLoS ONE
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Oestradiol or genistein rescues neurons from amyloid beta-induced cell death by inhibiting activation of p38.

2007

Oestrogenic compounds have been postulated as neuroprotective agents. This prompted us to investigate their mechanism action in neurons in primary culture. Cells were pretreated with physiological concentrations of 17-beta estradiol (0.2 nm) or with nutritionally relevant concentrations of genistein (0.5 microm), and 48 h later treated with 5 microm of amyloid beta (Abeta) for 24 h. We found that Abeta increased oxidative stress, measured as peroxide levels or oxidized glutathione/reduced glutathione ratio, which in turn, caused phosphorylation of p38 MAP kinase. Amyloid beta subsequently induced neuronal death. Inhibiting the MAP kinase pathway prevented cell death, confirming the role of …

MAPK/ERK pathwayAgingProgrammed cell deathmedicine.medical_specialtyAmyloid betaCell Survivalp38 mitogen-activated protein kinasesGenisteinPhytoestrogensIn Vitro Techniquesmedicine.disease_causeNeuroprotectionp38 Mitogen-Activated Protein Kinaseschemistry.chemical_compoundInternal medicinemedicineAnimalsCells CulturedCerebral CortexNeuronsAmyloid beta-PeptidesbiologyCell DeathEstradiolEstrogensCell BiologyGlutathioneGenisteinMitochondriaRatsOxidative StressEndocrinologychemistrybiology.proteinOxidation-ReductionOxidative stressAging cell
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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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Three-dimensional invasion of human glioblastoma cells remains unchanged by X-ray and carbon ion irradiation in vitro.

2012

Purpose Cell invasion represents one of the major determinants that treatment has failed for patients suffering from glioblastoma. Contrary findings have been reported for cell migration upon exposure to ionizing radiation. Here, the migration and invasion capability of glioblastoma cells on and in collagen type I were evaluated upon irradiation with X-rays or carbon ions. Methods and Materials Migration on and invasion in collagen type I were evaluated in four established human glioblastoma cell lines exposed to either X-rays or carbon ions. Furthermore, clonogenic radiation survival, proliferation (5-bromo-2-deoxyuridine positivity), DNA double-strand breaks (γH2AX/53BP1-positive foci), a…

MAPK/ERK pathwayCancer ResearchCell signalingMMP2MAP Kinase Kinase 4p38 Mitogen-Activated Protein KinasesCollagen Type IExtracellular matrixHistonesPhosphatidylinositol 3-KinasesCell MovementMedicineHumansRadiology Nuclear Medicine and imagingDNA Breaks Double-StrandedNeoplasm InvasivenessClonogenic assayPI3K/AKT/mTOR pathwayCell ProliferationRadiationbusiness.industryCell growthBrain NeoplasmsIntegrin beta1Intracellular Signaling Peptides and ProteinsCell migrationCarbonOncologyBromodeoxyuridineImmunologyCancer researchbusinessCell Migration AssaysGlioblastomaTumor Suppressor p53-Binding Protein 1International journal of radiation oncology, biology, physics
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p38α MAPK is required for contact inhibition

2005

Proliferation of nontransformed cells is regulated by cell-cell contacts, which are referred to as contact-inhibition. Despite its generally accepted importance for cell cycle control, knowledge about the intracellular signalling pathways involved in contact inhibition is scarce. In the present work we show that p38alpha mitogen-activated protein kinase (MAPK) is involved in the growth-inhibitory signalling cascade of contact inhibition in fibroblasts. p38alpha activity is increased in confluent cultures of human fibroblasts compared to proliferating cultures. Time course studies show a sustained activation of p38alpha in response to cell-cell contacts in contrast to a transient activation …

MAPK/ERK pathwayCancer ResearchContact InhibitionCell growthp38 mitogen-activated protein kinasesCell Culture TechniquesContact inhibitionFibroblastsBiologyCell biologyMitogen-Activated Protein Kinase 14Cell Transformation Neoplasticmedicine.anatomical_structureCell cultureNeoplasmsGeneticsmedicineHumansSignal transductionProtein kinase AFibroblastMolecular BiologyCell ProliferationSignal TransductionOncogene
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TCDD induces c-jun expression via a novel Ah (dioxin) receptor-mediated p38–MAPK-dependent pathway

2005

The aryl hydrocarbon receptor (AhR) has a fundamental role during postnatal liver development and is essential for mediating dioxin toxicity. However, the genetic programs mediating, both, the toxic and physiological effects downstream of the transcription factor AhR are in major parts unknown. We have identified the proto-oncogene c-jun as a novel target gene of AhR. Induction of c-jun depends on activation of p38-mitogen-activated protein kinase (MAPK) by an AhR-dependent mechanism. None of the kinases that are known to phosphorylate p38-MAPK is activated by AhR. Neither the dephosphorylation rate of p38-MAPK is reduced. Furthermore, increased p38-MAPK phosphorylation in response to dioxi…

MAPK/ERK pathwayCancer ResearchPolychlorinated DibenzodioxinsProto-Oncogene Proteins c-junp38 mitogen-activated protein kinasesBiologyTransfectionProto-Oncogene Masp38 Mitogen-Activated Protein KinasesGenes ReporterCell Line TumorGeneticsHumansRNA NeoplasmRNA Small InterferingProtein kinase AMolecular BiologyTranscription factorDNA PrimersBase SequenceKinasec-junrespiratory systemAryl hydrocarbon receptorrespiratory tract diseasesGene Expression Regulation NeoplasticReceptors Aryl HydrocarbonMitogen-activated protein kinasebiology.proteinCancer researchOncogene
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Effects of two organotin(IV)(sulfonato phenyl)porphynates on the MAPKs and on the growth of A375 human melanoma cells

2009

Previously we showed apoptotic induction in A375 human melanoma cells using two complexes of the meso-tetra(4-sulfonatophenyl)porphinate (TPPS), (Bu 2 Sn) 2 TPPS and (Bu 3 Sn) 4 TPPS. To understand how these compounds activate apoptosis in melanoma cells we studied MAPKs and the (Bu 2 Sn) 2 TPPS and (Bu 3 Sn) 4 TPPS cellular uptake. Western blotting experiments showed activated protein kinases ERK 1/2, JNK and p38 in 10 μM (Bu 2 Sn) 2 TPPS- and 1 μM (Bu 3 Sn) 4 TPPS-treated melanoma cells, which suggests that the three MAP kinases are involved in the apoptotic death of A375-treated cells. By taking advantage of the porphyrin fluorescence, we found a fast concentration of (Bu 2 Sn) 2 TPPS an…

MAPK/ERK pathwayCancer ResearchPorphyrinsp38 mitogen-activated protein kinasesBlotting WesternAntineoplastic AgentsApoptosischemistry.chemical_compoundCell Line TumorOrganotin CompoundsHumansMelanomaCell ProliferationbiologyKinaseCell growthGeneral MedicineA375 melamoma cells meso-tetra(4-sulfonato phenyl)porphinate MAPKs FAK cell growthMolecular biologyPorphyrinIn vitroMicroscopy Fluorescence MultiphotonOncologyBiochemistrychemistryApoptosisSettore CHIM/03 - Chimica Generale E InorganicaMitogen-activated protein kinasebiology.proteinMitogen-Activated Protein Kinases
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Manganese overload affects p38 MAPK phosphorylation and metalloproteinase activity during sea urchin embryonic development.

2014

Abstract In the marine environment, manganese represents a potential emerging contaminant, resulting from an increased production of manganese-containing compounds. In earlier reports we found that the exposure of Paracentrotus lividus sea urchin embryos to manganese produced phenotypes with no skeleton. In addition, manganese interfered with calcium uptake, perturbed extracellular signal-regulated kinase (ERK) signaling, affected the expression of skeletogenic genes, and caused an increase of the hsc70 and hsc60 protein levels. Here, we extended our studies focusing on the temporal activation of the p38 mitogen-activated protein kinase (p38 MAPK) and the proteolytic activity of metalloprot…

MAPK/ERK pathwayEmbryo NonmammalianAquatic ScienceBiologyMatrix metalloproteinaseOceanographyp38 Mitogen-Activated Protein KinasesParacentrotus lividusbiology.animalECM ERK Embryo-toxicity Immunoblotting MAPK MMPs Marine organisms' calcification Mn SDS-PAGE Zymography extracellular matrix extracellular signal-regulated kinase manganese metalloproteinases mitogen-activated protein kinase p38 MAPK sodium dodecyl sulfate-polyacrylamide gel electrophoresisAnimalsSettore BIO/06 - Anatomia Comparata E CitologiaPhosphorylationProtein kinase ASea urchinManganeseKinaseGeneral Medicinebiology.organism_classificationPollutionMatrix MetalloproteinasesBiochemistryMitogen-activated protein kinasebiology.proteinParacentrotusPhosphorylationWater Pollutants ChemicalMarine environmental research
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RNF2 Mediates Hepatic Stellate Cells Activation by Regulating ERK/p38 Signaling Pathway in LX-2 Cells

2021

The therapeutic approach of liver fibrosis is still an unsolved clinical problem worldwide. Notably, the accumulation of extracellular matrix (ECM) in the liver is mediated by the production of cytokines and growth factors, such as transforming growth factor-β1 (TGF-β1) in hepatic stellate cells (HSCs). Ring finger protein 2 (RNF2) was identified as the catalytic subunit of polycomb repressive complex 1 (PRC1), mediating the monoubiquitination of histone H2A. In recent years, a growing amount of evidence suggests that RNF2 may play an important role in multiple pathological processes involved in cancer. Here, we explored the role of RNF2 in liver fibrogenesis and its potential mechanisms. T…

MAPK/ERK pathwayGene knockdownChemistryCell growthp38 mitogen-activated protein kinasesapoptosisRNF2Cell BiologyCell biologyExtracellular matrixCell and Developmental BiologyLX-2 cellslcsh:Biology (General)Downregulation and upregulationinflammationMAPK signaling pathwayHepatic stellate cellSignal transductionlcsh:QH301-705.5Original Researchliver fibrosisDevelopmental BiologyFrontiers in Cell and Developmental Biology
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Protective dendritic cell responses against listeriosis induced by the short form of the deubiquitinating enzyme CYLD are inhibited by full-length CY…

2015

The deubiquitinating enzyme CYLD is an important tumor suppressor and inhibitor of immune responses. In contrast to full-length CYLD, the immunological function of the naturally occurring short splice variant of CYLD (sCYLD) is insufficiently described. Previously, we showed that DCs, which lack full-length CYLD but express sCYLD, exhibit augmented NF-κB and DC activation. To explore the function of sCYLD in infection, we investigated whether DC-specific sCYLD regulates the pathogenesis of listeriosis. Upon Listeria monocytogenes infection of CD11c-Cre Cyld(ex7/8 fl/fl) mice, infection of CD8α(+) DCs, which are crucial for the establishment of listeriosis in the spleen, was not affected. Ho…

MAPK/ERK pathwayImmune systemp38 mitogen-activated protein kinasesImmunologyCancer researchImmunology and AllergyTumor necrosis factor alphaDendritic cellBiologyAcquired immune systemCD8Deubiquitinating Enzyme CYLDMicrobiologyEuropean Journal of Immunology
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