Search results for "PROTEIN KINASE"

showing 10 items of 1188 documents

Inhibitory effect of nonviable preparations from human immunodeficiency virus 1 on inositol phospholipid metabolism

1989

Previously it was established [Pahwa, S., Pahwa, R., Saxinger, C., Gallo, R. C. & Good, R. A. (1985) Proc. Natl Acad. Sci. USA 82, 8198] that nonviable preparations of human immunodeficiency virus 1 (HIV-1) abolish the proliferative response of human lymphocytes to phytohemagglutinin A. Now we describe that this effect might be, at least partially, due to an impairment of the function of phospholipase C. It was found that addition of HIV-1 preparation to lymphocytes diminished the stimulation of phosphatidylinositol phosphorylation caused by phytohemagglutinin A. Moreover, this preparation completely abolished the phytohemagglutinin-A-stimulated release of inositol trisphosphate and prevent…

Inositol PhosphatesInositol 145-TrisphosphateBiologyPhospholipasePhosphatidylinositolsBiochemistrychemistry.chemical_compoundCytosolCyclic AMPPhosphatidylinositol phosphorylationHumansInositolLymphocytesPhosphorylationPhytohemagglutininsInositol phosphateProtein kinase AProtein Kinase CProtein kinase Cchemistry.chemical_classificationCell MembraneVirionBiological TransportInositol trisphosphateMolecular biologyCytosolchemistryBiochemistryType C PhospholipasesHIV-1Sugar PhosphatesCell DivisionEuropean Journal of Biochemistry
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cGMP-Dependent Protein Kinase I Mediates the Negative Inotropic Effect of cGMP in the Murine Myocardium

2002

To study the role of cGMP-dependent protein kinase I (cGKI) for cardiac contractility, force of contraction (F c ) was studied in electrically driven heart muscle from wild-type (WT) mice and from conventional and conditional cGKI knockout mice. Both 8-Br-cGMP and 8-pCPT-cGMP reduced Fc in cardiac muscle from juvenile WT but not from juvenile cGKI-null mutants. Similarly, the cGMP analogues reduced F c in forskolin-stimulated ventricular muscle from WT mice but not from cGKI-null mutants. In contrast, carbachol reduced F c in both groups of animals. 8-Br-cGMP reduced F c also in heart muscle from adult WT mice but not from adult cardiomyocyte-specific cGKI-knockout mice. These results demo…

Inotropemedicine.medical_specialtyCarbacholContraction (grammar)GenotypePhysiologyMice Inbred StrainsBiologyContractilityMiceInternal medicineCyclic GMP-Dependent Protein KinasesmedicineAnimalsProtein kinase ACyclic GMPMice KnockoutMyocardiumCardiac muscleThionucleotidesMyocardial ContractionMice Inbred C57BLmedicine.anatomical_structureEndocrinologyKnockout mouseSignal transductionCardiology and Cardiovascular Medicinemedicine.drugCirculation Research
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The collagen receptor integrins have distinct ligand recognition and signaling functions

2000

Distinct collagen subtypes are recognized by specific cell surface receptors. Two of the best known collagen receptors are members of the integrin family and are named alpha1beta1 and alpha2beta1. Integrin alpha1beta1 is abundant on smooth muscle cells, whereas the alpha2beta1 integrin is the major collagen receptor on epithelial cells and platelets. Many cell types, such as fibroblasts, osteoblasts, chondrocytes, endothelial cells, and lymphocytes may concomitantly express both of the receptors. We have studied the cell biology of these integrins at two levels. First, we have analyzed their ligand binding mechanism and specificity. Second, we have studied their signaling function inside th…

IntegrinsCell typeReceptors CollagenbiologyCell adhesion moleculeIntegrinLigandsLigand (biochemistry)p38 Mitogen-Activated Protein KinasesMolecular biologyIntegrin alpha1beta1Collagen receptorCell biologybiology.proteinAnimalsHumansPlateletMitogen-Activated Protein KinasesSignal transductionReceptorMolecular BiologySignal TransductionMatrix Biology
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Integrin alpha 2 beta 1 promotes activation of protein phosphatase 2A and dephosphorylation of Akt and glycogen synthase kinase 3 beta.

2002

The integrins are a large family of heterodimeric transmembrane receptors composed of α and β subunits (22). In addition to mediating cell-matrix interactions, integrins have been shown to activate intracellular signaling pathways which, in collaboration with growth factor-induced signals, regulate cellular functions (46). Some integrin signaling cascades are activated via the β subunit cytoplasmic domain, and they are therefore triggered by several integrin heterodimers. These signals include the activation of protein tyrosine kinases of the Src and focal adhesion kinase (FAK) families (9, 47). More-recent studies have revealed signaling events that are activated specifically by an α subun…

IntegrinsReceptors CollagenIntegrinProtein Serine-Threonine KinasesCD49cp38 Mitogen-Activated Protein KinasesCollagen receptorGlycogen Synthase Kinase 3Proto-Oncogene ProteinsCell AdhesionPhosphoprotein PhosphatasesHumansIntegrin-linked kinaseProtein Phosphatase 2cdc42 GTP-Binding ProteinMolecular BiologyCell Growth and DevelopmentCells CulturedbiologyAkt/PKB signaling pathwayCell adhesion moleculeGlycogen Synthase KinasesCell BiologyCell biologyEnzyme ActivationBiochemistryIntegrin alpha MCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinIntegrin beta 6CollagenMitogen-Activated Protein KinasesProto-Oncogene Proteins c-aktProtein BindingSignal TransductionMolecular and cellular biology
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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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Signal transduction pathways involved in the mechanical responses to protease-activated receptors in rat colon.

2002

Recording simultaneously in vitro the changes of endoluminal pressure (index of circular muscle activity) and isometric tension (index of longitudinal muscle activity), we examined the mechanisms responsible for the apamin-sensitive relaxant and contractile responses induced by protease-activated receptor (PAR)-1 and PAR-2 activating peptides, SFLLRN-NH2 and SLIGRL-NH2, respectively, in rat colon. In the circular muscle, the inhibitory effects of SFLLRN-NH2 and SLIGRL-NH2 were significantly reduced by ryanodine, an inhibitor of Ca2+ release from the sarcoplasmic reticulum, but unaffected by 1-[6-[[17beta-methoxyestra-1,3,5(10)-trien-17-yl]amino]hexyl]-1H-pyrrole-2,5-dione (U73122), a phosph…

Intracellular FluidMalemedicine.medical_specialtyColonGenisteinBiologyIn Vitro Techniqueschemistry.chemical_compoundInternal medicinemedicineAnimalsReceptor PAR-2Receptor PAR-1Rats WistarReceptorProtein kinase CPharmacologyPhospholipase CRyanodine receptorNeural InhibitionRatsEndocrinologychemistryType C PhospholipasesMolecular MedicineCalciumReceptors ThrombinSignal transductionmedicine.symptomExtracellular SpaceTyrosine kinaseMuscle contractionMuscle ContractionSignal TransductionThe Journal of pharmacology and experimental therapeutics
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mGluR2/3 agonist LY379268, by enhancing the production of GDNF, induces a time-related phosphorylation of RET receptor and intracellular signaling Er…

2011

In the present study we aimed to verify if the enhancement of glial cell line-derived neurotrophic factor (GDNF) production in mouse striatum following treatment with LY379268 may also induce in the nigrostriatal system a time-related activation of RET receptor and its specific intracellular signaling. For this purpose, we have investigated the effects of LY379268 treatment on RET phosphorylation at the Tyr1062 and on downstream signaling Erk1/2, Akt and PLCγ1 pathway activation. The results showed that treatment with LY379268 (3 mg/kg) induces a significant increase of GDNF levels and time-related RET and Erk1/2 phosphorylation in the striatum. These increases were detected at 24 h and 48 …

Intracellular FluidMalemedicine.medical_specialtyTime FactorsMAP Kinase Signaling SystemSubstantia nigraStriatumReceptors Metabotropic GlutamateSettore BIO/09 - FisiologiaCellular and Molecular NeuroscienceMiceErk1/2Neurotrophic factorsInternal medicinemedicineGlial cell line-derived neurotrophic factorAnimalsGlial Cell Line-Derived Neurotrophic FactorAmino AcidsPhosphorylationReceptormGluR2/3Protein kinase BPharmacologyMitogen-Activated Protein Kinase 3biologyChemistryProto-Oncogene Proteins c-retLY379268Bridged Bicyclo Compounds HeterocyclicGDNFCorpus StriatumUp-RegulationMice Inbred C57BLEndocrinologynervous systembiology.proteinPhosphorylationTrK phosphorylationRETGDNF family of ligandsNeuropharmacology
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Modulation of NMDA receptor function by cyclic AMP in cerebellar neurones in culture

2004

The signal transduction pathways involved in NMDA receptor modulation by other receptors remain unclear. cAMP could be involved in this modulation. The aim of this work was to analyse the contribution of cAMP to NMDA receptor modulation in cerebellar neurones in culture. Forskolin increases cAMP and results in increased intracellular calcium and cGMP that are prevented by blocking NMDA receptors. Similar effects were induced by two cAMP analogues, indicating that cAMP leads to NMDA receptor activation. It has been reported that phosphorylation of Ser897 of the NR1 subunit of NMDA receptors by cAMP-dependent protein kinase (PKA) activates the receptors. Forskolin increases Ser897 phosphoryla…

Intracellular Fluidmedicine.medical_specialty8-Bromo Cyclic Adenosine MonophosphateBiologyReceptors N-Methyl-D-AspartateBiochemistryCellular and Molecular Neurosciencechemistry.chemical_compoundCerebellumInternal medicineCyclic AMPmedicineAnimalsCyclic adenosine monophosphateNerve Growth FactorsEnzyme InhibitorsPhosphorylationRats WistarProtein kinase AReceptorLong-term depressionCyclic GMPCells CulturedNeuronsNeurotransmitter AgentsForskolinColforsinNeuropeptidesCyclic AMP-Dependent Protein KinasesRatsPituitary adenylate cyclase-activating peptideEndocrinologynervous systemchemistryPituitary Adenylate Cyclase-Activating PolypeptideNMDA receptorCalciumSignal transductionExcitatory Amino Acid AntagonistsSignal TransductionJournal of Neurochemistry
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Chronic exposure to ammonia induces isoform-selective alterations in the intracellular distribution and NMDA receptor-mediated translocation of prote…

2004

Hyperammonemia is responsible for most neurological alterations in patients with hepatic encephalopathy by mechanisms that remain unclear. Hyperammonemia alters phosphorylation of neuronal protein kinase C (PKC) substrates and impairs NMDA receptor-associated signal transduction. The aim of this work was to analyse the effects of hyperammonemia on the amount and intracellular distribution of PKC isoforms and on translocation of each isoform induced by NMDA receptor activation in cerebellar neurons. Chronic hyperammonemia alters differentially the intracellular distribution of PKC isoforms. The amount of all isoforms (except PKC zeta) was reduced (17-50%) in the particulate fraction. The con…

Intracellular Fluidmedicine.medical_specialtyN-MethylaspartateChromosomal translocationBiologyPKC alphaBiochemistryReceptors N-Methyl-D-AspartateCellular and Molecular NeuroscienceAmmoniaInternal medicineCerebellummedicineAnimalsHyperammonemiaRats WistarProtein kinase CCells CulturedProtein Kinase CDiacylglycerol kinaseNeuronsPhospholipase CDose-Response Relationship DrugHyperammonemiamedicine.diseaseCell biologyRatsIsoenzymesCytosolProtein TransportEndocrinologySignal transductionJournal of neurochemistry
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