Search results for "protein kinase A"

showing 10 items of 231 documents

Molecular cloning of rat G-protein-coupled receptor kinase 6 (GRK6) from brain tissue, and its mRNA expression in different brain regions and periphe…

1997

The rat G-protein-coupled receptor kinase 6 (GRK6) cDNA was cloned from rat brain tissue by a combination of reverse-transcription polymerase chain reactions (RT-PCR), based on homology to the cloned human GRK6, and rapid amplification of cDNA ends (RACE-PCR). We obtained a clone of 2817 bp with an open reading frame of 1731 bp encoding for a protein of 576 amino acids that is 96.7% identical and 97.9% similar to its human counterpart. mRNA was detectable in all brain areas examined. In addition, GRK6 was expressed in skeletal muscle, small intestine, aorta, liver, heart, lung, thymus, stomach, uterus and kidney.

DNA ComplementaryTranscription GeneticMolecular Sequence DataProtein Serine-Threonine KinasesMolecular cloningBiologyPolymerase Chain ReactionOpen Reading FramesCellular and Molecular NeuroscienceRapid amplification of cDNA endsGTP-Binding ProteinsComplementary DNAGene expressionAnimalsHumansAmino Acid SequenceRNA MessengerCloning MolecularProtein kinase AMolecular BiologyG protein-coupled receptor kinaseMessenger RNABase SequenceSequence Homology Amino AcidBrainReceptor Protein-Tyrosine KinasesG-Protein-Coupled Receptor KinasesMolecular biologyRatsOpen reading frameOrgan SpecificityFemaleSequence AlignmentMolecular Brain Research
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Drug insight: novel small molecules and drugs for immunosuppression.

2006

Gastrointestinal diseases can result from the inadequate or excessive response of the immune system to self or innocuous antigens. Moreover, the physiologic activation of the immune system against non-self antigens is a major clinical problem in liver organ transplantation. At present, many drugs are available that suppress the activation of the immune system, although most of the currently used immunosuppressive drugs lack specificity in terms of their molecular targets and, therefore, have the potential to generate numerous side effects. The advances that have been made in understanding the molecular events that underlie the activation of the immune system have led to the development of a…

Drugmedicine.medical_specialtyHepatologybusiness.industryGastrointestinal Diseasesmedia_common.quotation_subjectJanus kinase 3medicine.medical_treatmentGastroenterologyImmunosuppressionGeneral MedicineSmall moleculeOrgan transplantationMolecular WeightImmune systemAntigenImmune SystemImmunologymedicineAnimalsHumansProtein kinase AbusinessImmunosuppressive Agentsmedia_commonNature clinical practice. Gastroenterologyhepatology
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Oligomeric Sensor Kinase DcuS in the Membrane of Escherichia coli and in Proteoliposomes: Chemical Cross-linking and FRET Spectroscopy

2010

The DcuSR (dicarboxylate uptake sensor and regulator) system of Escherichia coli is a typical two-component system consisting of a membranous sensor kinase (DcuS) and a cytoplasmic response regulator (DcuR) (11, 26, 48). DcuS responds to C4-dicarboxylates like fumarate, malate, or succinate (19). In the presence of the C4-dicarboxlates, the expression of the genes of anaerobic fumarate respiration (dcuB, fumB, and frdABCD) and of aerobic C4-dicarboxylate uptake (dctA) is activated. DcuS is a histidine protein kinase composed of two transmembrane helices with an intermittent sensory PAS domain in the periplasm (PASP) that was also termed the PDC domain (for PhoQ/DcuS/DctB/CitA domain or fold…

Escherichia coli ProteinsProteolipidsCell MembraneGreen Fluorescent ProteinsHistidine kinaseAutophosphorylationBiologyMicrobiologyLuminescent ProteinsResponse regulatorTransmembrane domainSpectrometry FluorescenceProtein kinase domainBiochemistryPAS domainEscherichia coliFluorescence Resonance Energy TransferKinase activityProtein kinase AProtein KinasesMolecular BiologySignal TransductionJournal of Bacteriology
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2001

Background Ethylene is a widely distributed alkene product which is formed enzymatically (e.g., in plants) or by photochemical reactions (e.g., in the upper oceanic layers from dissolved organic carbon). This gaseous compound was recently found to induce in cells from the marine sponge Suberites domuncula, an increase in intracellular Ca2+ level ([Ca2+]i) and an upregulation of the expression of two genes, the potential ethylene-responsive gene, SDERR, and a Ca2+/calmodulin-dependent protein kinase.

Ethylenebiologychemistry.chemical_elementCell BiologyCalciumbiology.organism_classification3T3 cellsCalcium in biologyCell biologySuberites domunculachemistry.chemical_compoundmedicine.anatomical_structureBiochemistrychemistryDownregulation and upregulationmedicineProtein kinase AIntracellularBMC Cell Biology
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Ras-pathway has a dual role in yeast galactose metabolism

2007

AbstractIn the yeast Saccharomyces cerevisiae the genes involved in galactose metabolism (GAL1,7,10) are transcriptionally activated more than a 1000-fold in the presence of galactose as the sole carbon source in the culture media. In the present work, we monitored the activity of the GAL10 gene promoter in different Ras-cAMP genetic backgrounds. We demonstrate that overexpression of C-terminus of the nucleotide exchange factor Cdc25p stimulates GAL10 transcription in yeast strains carrying the contemporary deletion of both RAS genes. Moreover, the deletion of the chromosomal CDC25 gene provokes impaired growth on galactose based media in yeast strain lacking both RAS genes and adenylate cy…

Galactose metabolismSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeBiophysicsGene ExpressionSaccharomyces cerevisiaeRas glucose and galactose metabolism cancerGTP-binding proteinSignal transductionBiochemistryLeloir pathwaychemistry.chemical_compoundRas-GRF1Protein kinase AStructural BiologyGenes ReporterGene Expression Regulation FungalGeneticsRNA MessengerProtein kinase APromoter Regions GeneticMolecular BiologyChromosomal DeletionAllelesbiologyras-GRF1GalactosePromoterCell Biologybiology.organism_classificationLeloir pathwayExchange factorPhenotypechemistryBiochemistryGalactoseras ProteinsSignal transductionGene DeletionAdenylyl CyclasesPlasmidsFEBS Letters
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Tristetraprolin Regulates the Expression of the Human Inducible Nitric-Oxide Synthase Gene

2005

The expression of human inducible NO synthase (iNOS) is regulated both by transcriptional and post-transcriptional mechanisms. Stabilization of mRNAs often depends on activation of p38 mitogen-activated protein kinase (p38 MAPK). In human DLD-1 cells, inhibition of p38 MAPK by the compound 4-(4-fluorophenyl)-2-(4-methylsulfinylphenyl)-5-(4-pyridyl)1H-imidazole (SB203580) or by overexpression of a dominant-negative p38 MAPKalpha protein resulted in a reduction of human iNOS mRNA and protein expression, whereas human iNOS promoter activity was not affected. An important RNA binding protein regulated by the p38 MAPK pathway and involved in the regulation of the stability of several mRNAs is tr…

ImmunoprecipitationRNA Stabilityp38 mitogen-activated protein kinasesTristetraprolinNitric Oxide Synthase Type IIRNA-binding proteinGene Expression Regulation EnzymologicCell LineImmediate-Early ProteinsTristetraprolinEnzyme StabilityHumansRNA MessengerProtein kinase APharmacologyRegulation of gene expressionbiologyChemistryZinc FingersTransfectionMolecular biologyDNA-Binding ProteinsNitric oxide synthasebiology.proteinMolecular MedicineNitric Oxide SynthaseMolecular Pharmacology
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A Protein-Interaction Array Inside a Living Cell

2013

Cell phenotype is determined by protein network states that are maintained by the dynamics of multiple protein interactions.1 Fluorescence microscopy approaches that measure protein interactions in individual cells, such as by Forster resonant energy transfer (FRET), are limited by the spectral separation of fluorophores and thus are most suitable to analyze a single protein interaction in a given cell. However, analysis of correlations between multiple protein interactions is required to uncover the interdependence of protein reactions in dynamic signal networks. Available protein-array technologies enable the parallel analysis of interacting proteins from cell extracts, however, they can …

ImmunoprecipitationRecombinant Fusion Proteinsprotein-protein interactionsImmobilized Nucleic AcidsProtein Array AnalysisreceptorsDNA Single-StrandedCatalysisProtein–protein interactionReceptors G-Protein-CoupledBimolecular fluorescence complementationProtein Array AnalysisChlorocebus aethiopsFluorescence microscopeFluorescence Resonance Energy TransferAnimalsProtein Interaction MapsProtein kinase Amultiplexed assayChemistryProteinsProtein-protein interactions Dip Pen Nanolithography Protein KinaseDNA directed immobilizationGeneral MedicineGeneral ChemistryCommunicationssurface-immobilizationKineticsLuminescent ProteinsFörster resonance energy transferBiochemistryMicroscopy FluorescenceCOS CellsBiophysicsSignal transductionAntibodies Immobilizedsignal transduction
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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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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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