Search results for "Phosphorylation"

showing 10 items of 975 documents

Specific tyrosine phosphorylation in response to bile in Fasciola hepatica and Echinostoma friedi

2003

Protein tyrosine phosphorylation (PY) is a well-known signalling mechanism which is also involved in host-parasite interactions. Despite its transcendence, PY has been poorly studied in parasitic helminths. The aim of this study is to examine the effect of bile salts on the PY pattern in parasitic trematodes. Two distinct adult models were analysed: Echinostoma friedi, of intestinal habitat, and Fasciola hepatica, naturally inhabitant of host biliary channels. Our results show that bile salts induce specific and distinct protein PY in both trematode species, indicating that this signalling process seems to be also involved in host-trematode relationships.

ImmunologyBile Acids and Saltschemistry.chemical_compoundCricetinaeEchinostomaparasitic diseasesAnimalsFasciola hepaticaParasite hostingPhosphorylationTyrosinebiologyHost (biology)Tyrosine phosphorylationGeneral MedicineFasciola hepaticabiology.organism_classificationInfectious DiseaseschemistryBiochemistryTyrosinePhosphorylationCattleParasitologyTrematodaEchinostomaExperimental Parasitology
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Novel Paraoxonase 2-Dependent Mechanism Mediating the Biological Effects of the Pseudomonas aeruginosa Quorum-Sensing Molecule N-(3-Oxo-Dodecanoyl)-l…

2015

ABSTRACT Pseudomonas aeruginosa produces N -(3-oxo-dodecanoyl)- l -homoserine lactone (3OC12), a crucial signaling molecule that elicits diverse biological responses in host cells thought to subvert immune defenses. The mechanism mediating many of these responses remains unknown. The intracellular lactonase paraoxonase 2 (PON2) hydrolyzes and inactivates 3OC12 and is therefore considered a component of host cells that attenuates 3OC12-mediated responses. Here, we demonstrate in cell lines and in primary human bronchial epithelial cells that 3OC12 is rapidly hydrolyzed intracellularly by PON2 to 3OC12 acid, which becomes trapped and accumulates within the cells. Subcellularly, 3OC12 acid acc…

ImmunologyBlotting WesternHomoserineMitochondrionMicrobiologyCell LineHost-Parasite Interactionschemistry.chemical_compoundLactonesLactonaseHomoserineHumansImmunoprecipitationPseudomonas InfectionsChromatography High Pressure LiquidCellular Microbiology: Pathogen-Host Cell Molecular InteractionsMicroscopy ConfocalbiologyKinaseAryldialkylphosphataseQuorum SensingQuorum sensingCytosolInfectious DiseasesBiochemistrychemistryPseudomonas aeruginosabiology.proteinPhosphorylationParasitologyRNA InterferenceIntracellular
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Cross-Inhibition of Interferon-Induced Signals by GM-CSF Through a Block in Stat1 Activation

2007

We investigated the effects of granulocyte-macrophage colony-stimulating factor (GM-CSF) on biologic signals induced by interferon-alpha (IFN-alpha) and IFN-gamma. In hematopoietic cell lines, IFN-induced signaling was investigated by Western blotting, electrophoretic mobility shift assays (EMSA), flow cytometry, protein-tyrosine phosphatase (PTP) assays, and RT-PCR. GM-CSF inhibited IFN-alpha-induced and IFN-gamma-induced Stat1 tyrosine phosphorylation in a time-dependent manner. EMSA showed that GM-CSF inhibited IFN-alpha-induced and IFN-gamma-induced IFN-gamma activator sequence (GAS) binding activity. As a consequence, IFN-induced transcription of the early response gene, IFN-stimulated…

ImmunologyPhosphataseSuppressor of Cytokine Signaling ProteinsProtein tyrosine phosphataseBiologyCell Linechemistry.chemical_compoundVirologyGranulocyte Colony-Stimulating FactorHumansPhosphorylationHistocompatibility Antigens Class IGranulocyte-Macrophage Colony-Stimulating FactorTyrosine phosphorylationDNACell BiologyMolecular biologySTAT1 Transcription FactorIRF1chemistryTyrosine kinase 2PhosphorylationInterleukin-3InterferonsSignal transductionInterferon Regulatory Factor-1Signal TransductionTranscription FactorsProto-oncogene tyrosine-protein kinase SrcJournal of Interferon & Cytokine Research
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Protein Kinase C μ Is Regulated by the Multifunctional Chaperon Protein p32

2000

We identified the multifunctional chaperon protein p32 as a protein kinase C (PKC)-binding protein interacting with PKCalpha, PKCzeta, PKCdelta, and PKC mu. We have analyzed the interaction of PKC mu with p32 in detail, and we show here in vivo association of PKC mu, as revealed from yeast two-hybrid analysis, precipitation assays using glutathione S-transferase fusion proteins, and reciprocal coimmunoprecipitation. In SKW 6.4 cells, PKC mu is constitutively associated with p32 at mitochondrial membranes, evident from colocalization with cytochrome c. p32 interacts with PKC mu in a compartment-specific manner, as it can be coimmunoprecipitated mainly from the particulate and not from the so…

ImmunoprecipitationRecombinant Fusion ProteinsGolgi ApparatusSaccharomyces cerevisiaeSpodopteraMitogen-activated protein kinase kinaseBiologyTransfectionBiochemistryCell LineMitochondrial ProteinsAnimalsHumansCloning MolecularKinase activityMolecular BiologyProtein Kinase CProtein kinase CGlutathione TransferaseB-LymphocytesBinding SitesMembrane GlycoproteinsKinaseAutophosphorylationJNK Mitogen-Activated Protein KinasesCell BiologyFusion proteinMitochondriaReceptors ComplementCell biologybody regionsHyaluronan ReceptorsProtein kinase domainBiochemistryMitogen-Activated Protein KinasesCarrier ProteinsMolecular ChaperonesProtein BindingJournal of Biological Chemistry
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Intrinsic fluorescence of the clinically approved multikinase inhibitor nintedanib reveals lysosomal sequestration as resistance mechanism in FGFR-dr…

2017

Background Studying the intracellular distribution of pharmacological agents, including anticancer compounds, is of central importance in biomedical research. It constitutes a prerequisite for a better understanding of the molecular mechanisms underlying drug action and resistance development. Hyperactivated fibroblast growth factor receptors (FGFRs) constitute a promising therapy target in several types of malignancies including lung cancer. The clinically approved small-molecule FGFR inhibitor nintedanib exerts strong cytotoxicity in FGFR-driven lung cancer cells. However, subcellular pharmacokinetics of this compound and its impact on therapeutic efficacy remain obscure. Methods 3-dimens…

IndolesLung NeoplasmsNintedanibResistancelcsh:RC254-282FluorescenceMiceCell Line TumorAntineoplastic Combined Chemotherapy ProtocolsAnimalsHumansPhosphorylationLungCell ProliferationAntineoplastic Combined Chemotherapy ProtocolAnimalResearchDrug Synergismlcsh:Neoplasms. Tumors. Oncology. Including cancer and carcinogensLysosomeReceptors Fibroblast Growth FactorXenograft Model Antitumor AssaysLung NeoplasmFGFR1IndoleSettore CHIM/03 - Chimica Generale E InorganicaMacrolidesMacrolideLysosomesHumanSignal Transduction
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Fluvastatin stabilizes the blood–brain barrier in vitro by nitric oxide-dependent dephosphorylation of myosin light chains

2006

Inhibition of the 3-hydroxy-3-methylglutaryl-coenzyme-A reductase and the downstream mevalonate pathway is in part responsible for the beneficial effects that statins exert on the cardiovascular system. In this study we aimed at analysing the stabilizing effects of fluvastatin on the blood-brain barrier (BBB) integrity, using an in vitro co-culture model of ECV304 and C6, or primary bovine endothelial cells and rat astrocytes. Fluvastatin dose-dependently (1-25 micromol/l) increased barrier integrity as analysed by measurements of transendothelial electrical resistance (TEER). This effect (117.4+/-2.6% at 25 micromol/l) was significantly reduced by the nitric oxide (NO) synthase inhibitor L…

IndolesMyosin Light ChainsMyosin light-chain kinaseGeranylgeranyl pyrophosphatePhosphataseFarnesyl pyrophosphateBiologyNitric OxideBlood–brain barrierAntioxidantsCapillary PermeabilityFatty Acids MonounsaturatedDephosphorylationMiceCellular and Molecular Neurosciencechemistry.chemical_compoundElectric ImpedancemedicineAnimalsDrug InteractionsEnzyme InhibitorsFluvastatinCells CulturedPharmacologyAnalysis of VarianceMicroscopy Confocalomega-N-MethylarginineDose-Response Relationship DrugEndothelial CellsBiological TransportMolecular biologyCoculture TechniquesRatsmedicine.anatomical_structurechemistryBiochemistryBlood-Brain BarrierAstrocytesModels AnimalCattleMevalonate pathwayFluvastatinmedicine.drugNeuropharmacology
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Fluvastatin prevents glutamate-induced blood-brain-barrier disruption in vitro.

2008

Abstract Glutamate is an important excitatory amino acid in the central nervous system. Under pathological conditions glutamate levels dramatically increase. Aim of the present study was to examine whether the HMG-CoA inhibitor fluvastatin prevents glutamate-induced blood-brain-barrier (BBB) disruption. Measurements of transendothelial electrical resistance (TEER) were performed to analyze BBB integrity in an in vitro co-culture model of brain endothelial and glial cells. Myosin light chain (MLC) phosphorylation was detected by immunohistochemistry, or using the in-cell western technique. Intracellular Ca 2+ and reactive oxygen species (ROS) levels were analyzed using the fluorescence dyes …

IndolesMyosin Light ChainsTime FactorsIntracellular SpaceGlutamic AcidBiologymedicine.disease_causeNitric OxideReceptors N-Methyl-D-AspartateGeneral Biochemistry Genetics and Molecular BiologyNitric oxideCell LineFatty Acids Monounsaturatedchemistry.chemical_compoundBAPTAmedicineElectric ImpedanceAnimalsGeneral Pharmacology Toxicology and PharmaceuticsPhosphorylationFluvastatinDose-Response Relationship DrugGlutamate receptorEndothelial CellsGeneral MedicineCell biologyRatsOxidative StresschemistryBiochemistryBlood-Brain BarrierApocyninNMDA receptorCalciumNAD+ kinaseReactive Oxygen SpeciesOxidative stressFluvastatinmedicine.drugSignal TransductionLife sciences
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Diacylglycerols containing Omega 3 and Omega 6 fatty acids bind to RasGRP and modulate MAP kinase activation.

2003

We elucidated the effects of different diacylglycerols (DAGs), i.e. 1-stearoyl-2-arachidonoyl-sn-glycerol (SAG), 1-stearoyl-2-docosahexaenoyl-sn-glycerol (SDG), and 1-stearoyl-2-eicosapentaenoyl-sn-glycerol (SEG), on [3H]PDBu binding to RasGRP. The competition studies with these DAGs on [3H]PDBu binding to RasGRP revealed different Ki values for these DAG molecular species. Furthermore, we transfected human Jurkat T cells by a plasmid containing RasGRP and assessed the implication of endogenous DAGs on activation of MAP kinases ERK1/ERK2, induced by phorbol-12-myristate-13-acetate (PMA). In control cells, GF109203X, a protein kinase C inhibitor, inhibited ERK1/ERK2 activation. However, this…

IndolesTime FactorsBiochemistryJurkat cellsMaleimideschemistry.chemical_compoundJurkat CellsGuanine Nucleotide Exchange FactorsEnzyme InhibitorsMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3KinaseFatty AcidsBrainTransfectionCell biologyDNA-Binding ProteinsBiochemistryEicosapentaenoic AcidDocosahexaenoic acidMitogen-activated protein kinasePhosphorylationTetradecanoylphorbol Acetatelipids (amino acids peptides and proteins)Arachidonic acidMitogen-Activated Protein KinasesPlasmidsProtein BindingDNA ComplementaryDocosahexaenoic AcidsMAP Kinase Signaling SystemImmunoblottingBiologyTransfectionBinding CompetitiveDiglyceridesInhibitory Concentration 50Fatty Acids Omega-6Fatty Acids Omega-3Escherichia coliAnimalsHumansCalphostinMolecular BiologyDose-Response Relationship Drugurogenital systemCell BiologyRatsEnzyme ActivationKineticschemistrybiology.proteinThe Journal of biological chemistry
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Imidazo[2,1-b] [1,3,4]thiadiazoles with antiproliferative activity against primary and gemcitabine-resistant pancreatic cancer cells

2020

A new series of eighteen imidazo [2,1-b] [1,3,4]thiadiazole derivatives was efficiently synthesized and screened for antiproliferative activity against the National Cancer Institute (NCI-60) cell lines panel. Two out of eighteen derivatives, compounds 12a and 12h, showed remarkably cytotoxic activity with the half maximal inhibitory concentration values (IC50) ranging from 0.23 to 11.4 μM, and 0.29–12.2 μM, respectively. However, two additional compounds, 12b and 13g, displayed remarkable in vitro antiproliferative activity against pancreatic ductal adenocarcinoma (PDAC) cell lines, including immortalized (SUIT-2, Capan-1, Panc-1), primary (PDAC-3) and gemcitabine-resistant (Panc-1R), elici…

Inhibition of migrationAntimetabolites AntineoplasticEpithelial-Mesenchymal Transition3Modulation of EMTPTK2VimentinAntineoplastic AgentsApoptosisThiophenesAntiproliferative activity1-b][1DeoxycytidinePancreatic ductal adenocarcinomaThiadiazolesSDG 3 - Good Health and Well-beingCell MovementPancreatic cancerDrug DiscoveryThiadiazolesmedicineTumor Cells CulturedImidazo[21-b][134]thiadiazole derivativesHumansPTK2/FAKIC50Cell ProliferationImidazo[2Pharmacologybiology4]thiadiazole derivativesChemistryOrganic ChemistryDrug SynergismGeneral Medicinemedicine.diseaseGemcitabinePancreatic NeoplasmsCell cultureDrug Resistance NeoplasmImidazo[21-b][134]thiadiazole derivatives Pancreatic ductal adenocarcinoma Antiproliferative activity Inhibition of migration Spheroids shrinkage Modulation of EMT PTK2/FAKbiology.proteinCancer research/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_beingPhosphorylationSpheroids shrinkageTyrosine kinaseCarcinoma Pancreatic DuctalEuropean Journal of Medicinal Chemistry
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Supported Single Atom Catalysts for C−H Activation: Selective C−H Oxidations, Dehydrogenations and Oxidative C−H/C−H Couplings

2021

Inorganic ChemistryChemistryOrganic ChemistryAtom (order theory)Oxidative coupling of methaneOxidative phosphorylationPhysical and Theoretical ChemistryHeterogeneous catalysisMedicinal chemistryCatalysisCatalysisChemCatChem
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