Search results for "Enzyme Activation"

showing 10 items of 304 documents

β1D Integrin Inhibits Cell Cycle Progression in Normal Myoblasts and Fibroblasts

1998

Integrins are alphabeta heterodimeric transmembrane receptors involved in the regulation of cell growth and differentiation. The beta1 integrin subunit is widely expressed in vivo and is represented by four alternatively spliced cytoplasmic domain isoforms. beta1D is a muscle-specific variant of beta1 integrin and a predominant beta1 isoform in striated muscles. In the present study we showed that expression of the exogenous beta1D integrin in C2C12 myoblasts and NIH 3T3 or REF 52 fibroblasts inhibited cell proliferation. Unlike the case of the common beta1A isoform, adhesion of beta1D-transfected C2C12 myoblasts specifically via the expressed integrin did not activate mitogen-activated pro…

IntegrinsRecombinant Fusion ProteinsMolecular Sequence DataIntegrinSignal transductionTransfectionCell adhesion; Integrins; Signal transduction; Alternative splicing isoforms; Cell proliferation; MyodifferentiationBiochemistryCD49cCell LineCollagen receptorMiceAlternative splicing isoformsCell surface receptorAnimalsAmino Acid SequenceMuscle SkeletalMolecular BiologyCell proliferationMyodifferentiationbiologyCell growthIntegrin beta1Cell CycleCell adhesionCell DifferentiationReceptors Interleukin-2Cell BiologyImmunohistochemistryMolecular biologyCell biologyEnzyme ActivationProto-Oncogene Proteins c-rafAlternative SplicingGenes rasIntegrin alpha MCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinIntegrin beta 6C2C12Journal of Biological Chemistry
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Docosahexaenoic Acid Induces Increases in [Ca2+]ivia Inositol 1,4,5-Triphosphate Production and Activates Protein Kinase Cγ and -δ via Phosphatidylse…

2007

We investigated, in monocytic leukemia U937 cells, the effects of docosahexaenoic acid (DHA; 22:6 n-3) on calcium signaling and determined the implication of phospholipase C (PLC) and protein kinase C (PKC) in this pathway. DHA induced dose-dependent increases in [Ca2+]i, which were contributed by intracellular pool, via the production of inositol-1,4,5-triphosphate (IP3) and store-operated Ca2+ (SOC) influx, via opening of Ca2+ release-activated Ca2+ (CRAC) channels. Chemical inhibition of PLC, PKCgamma, and PKCdelta, but not of PKCbeta I/II, PKCalpha, or PKCbetaI, significantly diminished DHA-induced increases in [Ca2+]i. In vitro PKC assays revealed that DHA induced a approximately 2-fol…

Intracellular FluidDocosahexaenoic AcidsApoptosisInositol 145-TrisphosphatePhosphatidylserinesBiologyEnzyme activatorchemistry.chemical_compoundHumansCalcium SignalingPhosphatidylserine bindingProtein Kinase CProtein kinase CCalcium signalingPharmacologyBinding SitesPhospholipase CU937 CellsPhosphatidylserineMolecular biologyCell biologyEnzyme ActivationProtein Kinase C-deltachemistryDocosahexaenoic acidApoptosisMolecular Medicinelipids (amino acids peptides and proteins)Molecular Pharmacology
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Potassium regulates IL-1 beta processing via calcium-independent phospholipase A2.

2000

Abstract We report that potassium leakage from cells leads to activation of the Ca2+-independent phospholipase A2 (iPLA2), and the latter plays a pivotal role in regulating the cleavage of pro-IL-1β by the IL-converting enzyme caspase-1 in human monocytes. K+ efflux led to increases of cellular levels of glycerophosphocholine, an unambiguous indicator of phospholipase A2 activation. Both maturation of IL-1β and formation of glycerophosphocholine were blocked by bromoenol lactone, the specific iPLA2 inhibitor. Bromoenol lactone-dependent inhibition of IL-1β processing was not due to perturbation of the export machinery for pro-IL-1β and IL-1β or to caspase-1 suppression. Conspicuously, activ…

Intracellular FluidPotassiumImmunologychemistry.chemical_elementNaphthalenesCleavage (embryo)MonocytesPhospholipases APhospholipase A2Calcium-Independent Phospholipase A2Immunology and AllergyHumansCells Culturedchemistry.chemical_classificationCalcium metabolismbiologyTumor Necrosis Factor-alphaCaspase 1Biological TransportCaspase InhibitorsCell biologyEnzyme ActivationPhospholipases A2EnzymechemistryPyronesbiology.proteinPotassiumCalciumEffluxBromoenol lactoneProtein Processing Post-TranslationalImmunosuppressive AgentsInterleukin-1Journal of immunology (Baltimore, Md. : 1950)
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Activation of metabotropic glutamate receptors induces propagating network oscillations in the intact cerebral cortex of the newborn mouse.

2006

Activation of metabotropic glutamate receptors (mGluRs) with (1S,3R)-1-aminocyclopentane-1,3-dicarboxylic acid (ACPD) elicited in the frontal or occipital pole of the intact cerebral cortex preparation of the newborn mouse (P0-P3) a transient oscillatory field potential activity in the frequency range of 11-14Hz. These oscillations propagated over the whole cortical hemisphere and were blocked by tetrodotoxin, indicating that action potentials are required for the generation of this activity. Blockade of GABA-A receptors with gabazine did not influence the ACPD-induced network activity, but the glycine antagonist strychnine caused a significant decrease in the frequency, amplitude and durat…

Kainate receptorCholinergic AgonistsReceptors Metabotropic GlutamateCellular and Molecular Neurosciencechemistry.chemical_compoundMiceKynurenic acidmedicineAnimalsLong-term depressionPharmacologyCerebral CortexDose-Response Relationship DrugDioxolanesEnzyme ActivationMice Inbred C57BLchemistryAnimals NewbornMetabotropic glutamate receptorPurinesCNQXGabazineACPDNMDA receptorCarbacholNerve NetNeuroscienceExcitatory Amino Acid Antagonistsmedicine.drugNeuropharmacology
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Differential role of p38 mitogen activated protein kinase for cellular recovery from attack by pore-forming S. aureus alpha-toxin or streptolysin O.

2006

Following the observation that cells are able to recover from membrane lesions incurred by Staphylococcus aureus alpha-toxin and streptolysin O (SLO), we investigated the role of p38 in this process. p38 phosphorylation occurred in response to attack by both toxins, commencing within minutes after toxin treatment and waning after several hours. While SLO reportedly activates p38 via ASK1 and ROS, we show that this pathway does not play a major role for p38 induction in alpha-toxin-treated cells. Strikingly divergent effects of p38 blockade were noted depending on the toxin employed. In the case of alpha-toxin, inhibition of p38 within the time frame of its activation led to disruption of th…

KeratinocytesProgrammed cell deathStaphylococcus aureusCell Membrane Permeabilityp38 mitogen-activated protein kinasesBacterial ToxinsBiophysicsBiologymedicine.disease_causeMAP Kinase Kinase Kinase 5Biochemistryp38 Mitogen-Activated Protein KinasesMicrobiologyHemolysin ProteinsAdenosine TriphosphateBacterial ProteinsProto-Oncogene ProteinsmedicineHumansASK1PhosphorylationMolecular BiologyCells CulturedPore-forming toxinToxinCell MembraneCell BiologyProtein-Tyrosine KinasesBlockadeCell biologyEnzyme ActivationStreptolysinsPhosphorylationStreptolysinBiochemical and biophysical research communications
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Liver X Receptor ligand cytotoxicity in colon cancer cells and not in normal colon epithelial cells depends on LXRβ subcellular localization

2015

Increasing evidence indicates that Liver X Receptors (LXRs) have some anticancer properties. We recently demonstrated that LXR ligands induce colon cancer cell pyroptosis through an LXRβ-dependent pathway. In the present study, we showed that human colon cancer cell lines presented differential cytoplasmic localizations of LXRβ. This localization correlated with caspase-1 activation and cell death induction under treatment with LXR ligand. The association of LXRβ with the truncated form of RXRα (t-RXRα) was responsible for the sequestration of LXRβ in the cytoplasm in colon cancer cells. Moreover t-RXRα was not expressed in normal colon epithelial cells. These cells presented a predominantl…

LXRβCytoplasmmedicine.medical_specialtyHydrocarbons FluorinatedColonColorectal cancerCaspase 1BiologyLigandsCell Line03 medical and health sciences0302 clinical medicineCell Line TumorInternal medicineRXRαsubcellular localizationmedicineHumansIntestinal MucosaLiver X receptorCytotoxicityLiver X Receptors030304 developmental biologySulfonamides0303 health sciencesRetinoid X Receptor alphaRetinoid X receptor alphaCaspase 1PyroptosisEpithelial CellsHCT116 CellsOrphan Nuclear ReceptorsSubcellular localizationmedicine.disease3. Good healthEnzyme ActivationGene Expression Regulation NeoplasticEndocrinologycolon cancerOncologyCell culture030220 oncology & carcinogenesisColonic NeoplasmsCancer researchPriority Research PaperOncotarget
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eNOS S-nitrosylates β-actin on Cys374 and regulates PKC-θ at the immune synapse by impairing actin binding to profilin-1.

2017

The actin cytoskeleton coordinates the organization of signaling microclusters at the immune synapse (IS); however, the mechanisms involved remain poorly understood. We show here that nitric oxide (NO) generated by endothelial nitric oxide synthase (eNOS) controls the coalescence of protein kinase C-¿ (PKC-¿) at the central supramolecular activation cluster (c-SMAC) of the IS. eNOS translocated with the Golgi to the IS and partially colocalized with F-actin around the c-SMAC. This resulted in reduced actin polymerization and centripetal retrograde flow of ß-actin and PKC-¿ from the lamellipodium-like distal (d)-SMAC, promoting PKC-¿ activation. Furthermore, eNOS-derived NO S-nitrosylated ß-…

Life Sciences & Biomedicine - Other Topics0301 basic medicinePOLARIZATIONIMMUNOLOGICAL SYNAPSEImmunological SynapsesT-LymphocytesPROTEINGolgi ApparatusCYTOSKELETONRetrograde FlowBiochemistryARP2/3 COMPLEXT-CELL-ACTIVATIONProfilinsWhite Blood CellsContractile ProteinsFluorescence MicroscopyAnimal CellsMedicine and Health SciencesPseudopodiaBiology (General)Post-Translational ModificationCells CulturedProtein Kinase CMicroscopyT CellsGeneral NeuroscienceLight MicroscopyNeurochemistryRecombinant Proteins3. Good healthIsoenzymesPOLYMERIZATIONProtein TransportCell ProcessesRNA InterferenceCellular TypesNeurochemicalsGeneral Agricultural and Biological SciencesLife Sciences & BiomedicineResearch ArticleBiochemistry & Molecular BiologyNitric Oxide Synthase Type IIIQH301-705.5Imaging TechniquesRecombinant Fusion ProteinsImmune CellsImmunologyLibrary scienceAntigen-Presenting Cellsmacromolecular substancesBiologyNitric OxideResearch and Analysis MethodsGeneral Biochemistry Genetics and Molecular BiologyCell Line03 medical and health sciencesFluorescence ImagingHumansCysteineNITRIC-OXIDE SYNTHASEBiologyScience & TechnologyBlood CellsRECEPTORGeneral Immunology and MicrobiologyBiology and Life SciencesProteinsCell BiologyActinsS-NitrosylationEnzyme ActivationLuminescent ProteinsCytoskeletal Proteins030104 developmental biologyAmino Acid SubstitutionRETROGRADE FLOWProtein Kinase C-thetaMutationProtein Processing Post-TranslationalNeuroscienceActin PolymerizationPLoS biology
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Voluntary distance running prevents TNF-mediated liver injury in mice through alterations of the intrahepatic immune milieu

2017

AbstractPhysical activity confers a broad spectrum of health benefits. Beyond the obvious role in metabolically driven diseases, the role of physical activity in acute liver injury is poorly explored. To study the role of physical activity in acute liver injury, a novel model of voluntary distance running in mice was developed and mice were subjected to acute liver injury induced by N-galactosamine (GalN) and lipopolysaccharide (LPS). Analyses included histological stains, immunoblotting, qRT-PCR and FACS analysis. Voluntary distance running increased to an average of 10.3 km/day after a learning curve. Running lead to a decrease in the absolute numbers of intrahepatic CD4+ T and B lymphocy…

Lifestyle modification0301 basic medicineLipopolysaccharidesMaleCancer ResearchChemokineApoptosisGalactosamineLiver Function TestsAlarminsLiver injurybiologymedicine.diagnostic_testChemotaxisNF-kappa Bmedicine.anatomical_structureLiverReceptors Pattern RecognitionModels AnimalCytokinesTumor necrosis factor alphaOriginal Articlemedicine.symptomChemokinesInflammation Mediatorsmedicine.medical_specialtyImmunologyInflammationCCL2Proinflammatory cytokine03 medical and health sciencesCellular and Molecular NeuroscienceInternal medicinePhysical Conditioning AnimalmedicineAnimalsLiver diseasesInflammationbusiness.industryTumor Necrosis Factor-alphaMonocyteBody WeightJNK Mitogen-Activated Protein KinasesCell BiologyLiver Failure Acutemedicine.diseaseEnzyme ActivationMice Inbred C57BL030104 developmental biologyEndocrinologyImmunologybiology.proteinLiver function testsbusinessCell Death & Disease
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Chitosomes loaded with cranberry proanthocyanidins attenuate the bacterial lipopolysaccharide-induced expression of iNOS and COX-2 in raw 264.7 macro…

2009

Chitosan binds to negatively charged soy lecithin liposomes by an electrostatic interaction driven by its positively charged amino group. This interaction allows stable covered vesicles (chitosomes) to be developed as a suitable targeted carrier and controlled release system. This study investigated the effect of chitosomes on the activation of cranberry proanthocyanidins (PAC) in Raw 264.7 macrophages. Chitosomes were characterized according to size, zeta potential, PAC-loading, and release properties. Results showed an increase in the net positive charge and size of the liposomes as the concentration of chitosan was increased, suggesting an effective covering of the vesicles by means of e…

LipopolysaccharidesLipopolysaccharideNitric Oxide Synthase Type IIPharmaceutical ScienceInflammationEndocytosisCell LineMicechemistry.chemical_compoundmedicineAnimalsMacrophageProanthocyanidinsTransport VesiclesChitosanLiposomeMolecular StructurebiologyMacrophagesVesicleControlled releaseMolecular biologyEnzyme ActivationNitric oxide synthaseVaccinium macrocarponchemistryBiochemistryCyclooxygenase 2Spectrometry Mass Matrix-Assisted Laser Desorption-Ionizationbiology.proteinmedicine.symptomJournal of Liposome Research
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Rho protein inhibition blocks protein kinase C translocation and activation.

1998

Small GTP-binding proteins of the Ras and Rho family participate in various important signalling pathways. Large clostridial cytotoxins inactivate GTPases by UDP-glucosylation. Using Clostridium difficile toxin B-10463 (TcdB) for inactivation of Rho proteins (RhoA/Rac/Cdc42) and Clostridium sordellii lethal toxin-1522 (TcsL) for inactivation of Ras-proteins (Ras/Rac/Ral, Rap) the role of these GTPases in protein kinase C (PKC) stimulation was studied. Phorbol-myristate-acetate (PMA) induced a rapid PKC translocation to and activation in the particulate cell fraction as determined by PKC-activity measurements and Western blots for PKC alpha. These effects were blocked by TcdB inhibiting Rho …

LipopolysaccharidesRHOASwineBiophysicsClostridium difficile toxin ABronchiCell Cycle ProteinsGTPaseCDC42PKC alphaBiochemistryGTP-Binding ProteinsRHO protein GDP dissociation inhibitorAnimalsHumanscdc42 GTP-Binding ProteinMolecular BiologyProtein kinase CCells CulturedProtein Kinase CbiologyEpithelial CellsCell BiologyMolecular biologyCell biologyEnzyme ActivationCdc42 GTP-Binding Proteinbiology.proteinras ProteinsTetradecanoylphorbol AcetateEndothelium VascularrhoA GTP-Binding ProteinBiochemical and biophysical research communications
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