Search results for "protein kinase"

showing 10 items of 1188 documents

Pro-inflammatory effects of interleukin-17A on vascular smooth muscle cells involve NAD(P)H- oxidase derived reactive oxygen species.

2010

T cells are known for their contribution to the inflammatory element of atherosclerosis. Recently, it has been demonstrated that the Th17 derived cytokine IL-17 is involved in the pro-inflammatory response of vascular smooth muscle cells (VSMC). The aim of the present study was to examine whether reactive oxygen species (ROS) might be involved in this context. The effect of IL-17A on ROS generation was examined using the fluorescent dye 2′7′-dichlorodihydrofluorescein (H<sub>2</sub>DCF) in primary murine VSMC. IL-17A induced an increase in H<sub>2</sub>DCF fluorescence in VSMC, and this effect was blocked by the NAD(P)H-oxidase inhibitor apocynin and siRNA targeting …

Vascular smooth musclePhysiologymedicine.medical_treatmentAorta Thoracicmedicine.disease_causep38 Mitogen-Activated Protein KinasesMuscle Smooth Vascularchemistry.chemical_compoundMiceCell MovementmedicineAnimalsEnzyme InhibitorsRNA Small InterferingCells Culturedchemistry.chemical_classificationReactive oxygen speciesNADPH oxidaseMembrane GlycoproteinsbiologyInterleukin-17AcetophenonesNADPH OxidasesCell DifferentiationMolecular biologyMice Inbred C57BLOxidative StressCytokinechemistryBiochemistryNAD(P)H oxidaseNADPH Oxidase 4ApocyninNADPH Oxidase 2cardiovascular systembiology.proteinCytokinesNAD+ kinaseCardiology and Cardiovascular MedicineReactive Oxygen SpeciesOxidative stressJournal of vascular research
researchProduct

Biochemistry and pharmacology of novel anthranilic acid derivatives activating heme-oxidized soluble guanylyl cyclase.

2005

The heme-enzyme soluble guanylyl cyclase (sGC) is an ubiquitous NO receptor, which mediates NO downstream signaling by the generation of cGMP. We studied the mechanism of action of the anthranilic acid derivatives 5-chloro-2-(5-chloro-thiophene-2-sulfonylamino-N-(4-(morpholine-4-sulfonyl)-phenyl)-benzamide sodium salt (HMR1766) (proposed international nonproprietary name, ataciguat sodium) and 2-(4-chloro-phenylsulfonylamino)-4,5-dimethoxy-N-(4-(thiomorpholine-4-sulfonyl)-phenyl)-benzamide (S3448) as a new class of sGC agonists. Both compounds activated different sGC preparations (purified from bovine lung, or crude from human corpus cavernosum) in a concentration-dependent and quickly reve…

Vasodilator AgentsBlood PressureHemePharmacologychemistry.chemical_compoundEnzyme activatorAnthranilic acidmedicineCyclic GMP-Dependent Protein KinasesAnimalsortho-AminobenzoatesReceptorHemePharmacologySulfonamidesProtoporphyrin IXActivator (genetics)Enzyme ActivationchemistryMechanism of actionBiochemistryGuanylate CyclaseMolecular MedicineCattlemedicine.symptomSoluble guanylyl cyclaseOxidation-ReductionMolecular pharmacology
researchProduct

Polar Localization of a Tripartite Complex of the Two-Component System DcuS/DcuR and the Transporter DctA in Escherichia coli Depends on the Sensor K…

2014

The C4-dicarboxylate responsive sensor kinase DcuS of the DcuS/DcuR two-component system of E. coli is membrane-bound and reveals a polar localization. DcuS uses the C4-dicarboxylate transporter DctA as a co-regulator forming DctA/DcuS sensor units. Here it is shown by fluorescence microscopy with fusion proteins that DcuS has a dynamic and preferential polar localization, even at very low expression levels. Single assemblies of DcuS had high mobility in fast time lapse acquisitions, and fast recovery in FRAP experiments, excluding polar accumulation due to aggregation. DctA and DcuR fused to derivatives of the YFP protein are dispersed in the membrane or in the cytosol, respectively, when …

Yellow fluorescent proteinCardiolipinslcsh:MedicineMicrobiologyMreBMicrobial PhysiologyBacterial Physiologylcsh:ScienceCytoskeletonMicrobial MetabolismDicarboxylic Acid TransportersMultidisciplinaryEscherichia coli K12biologyBacterial GrowthEscherichia coli Proteinslcsh:RMicrobial Growth and DevelopmentBiology and Life SciencesFluorescence recovery after photobleachingBacteriologyFusion proteinTwo-component regulatory systemBacterial BiochemistryTransport proteinDNA-Binding ProteinsProtein TransportBiochemistryCytoplasmMultiprotein ComplexesBiophysicsbiology.proteinlcsh:QProtein KinasesResearch ArticleDevelopmental BiologyTranscription FactorsPLoS ONE
researchProduct

Polar accumulation of the metabolic sensory histidine kinases DcuS and CitA in Escherichia coli

2008

Signal transduction in prokaryotes is frequently accomplished by two-component regulatory systems in which a histidine protein kinase is the sensory component. Many of these sensory kinases control metabolic processes that do not show an obvious requirement for inhomogeneous distribution within bacterial cells. Here, the sensory kinases DcuS and CitA, two histidine kinases of Escherichia coli, were investigated. Both are membrane-integral and involved in the regulation of carboxylate metabolism. The two-component sensors were fused with yellow fluorescent protein (YFP) and live images of immobilized cells were obtained by confocal laser fluorescence microscopy. The fluorescence of the fusio…

Yellow fluorescent proteinbiologyKinaseEscherichia coli ProteinsRecombinant Fusion ProteinsCell PolarityMicrobiologyFusion proteinLuminescent ProteinsProtein TransportBacterial ProteinsBiochemistryCytoplasmEscherichia colibiology.proteinSignal transductionCell fractionationProtein kinase AProtein KinasesHistidineMicrobiology
researchProduct

The evolution of nitric oxide signalling diverges between the animal and the green lineages

2019

AbstractNitric oxide (NO) is a ubiquitous signalling molecule with widespread distribution in prokaryotes and eukaryotes where it is involved in countless physiological processes. While the mechanisms governing nitric oxide (NO) synthesis and signalling are well established in animals, the situation is less clear in the green lineage. Recent investigations have shown that NO synthase, the major enzymatic source for NO in animals, is absent in land plants but present in a limited number of algae. The first detailed analysis highlighted that these new NO synthases are functional but display specific structural features and probably original catalytic activities. Completing this picture, analy…

[SDE] Environmental Sciences0106 biological sciencesAlgaePhysiologyLineage (evolution)[SDV]Life Sciences [q-bio]RegulatorPlant ScienceSignalling01 natural sciencesNitric oxideEvolution Molecular03 medical and health scienceschemistry.chemical_compoundcyclic nucleotide-gated channel[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyAnimals[SDV.BV] Life Sciences [q-bio]/Vegetal BiologyPhosphodiesteraseCyclic GMPComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesCGMPbiologyMechanism (biology)KinaseNitric oxide synthaseNitric oxidePlantPlantsGuanylate cyclaseCell biology[SDV] Life Sciences [q-bio]Nitric oxide synthaseSignallingchemistrycGMP-dependent protein kinase[SDE]Environmental Sciencesbiology.proteincGMP-dependent protein kinase010606 plant biology & botanySignal Transduction
researchProduct

Calcium, calmodulin-dependent protein phosphorylation in Neurospora crassa

1984

Abstract A calcium, calmodulin-dependent protein kinase activity has been partially purified by calmodulin-Sepharose affinity chromatography from the soluble fraction of Neurospora crassa . The phosphorylated peptide has an apparent molecular mass on SDS-polyacrylamide gel of 47 kDa. The apparent half maximal phosphorylation is obtained after 1.5 min at 30° C in the presence of calcium and calmodulin. The apparent half maximal activation of the phosphorylation is obtained at 1 μM calcium, and 0.1 or 0.2 μM calmodulin from bovine brain or Neurospora , respectively. The 32 P incorporation is enhanced about 10-fold by calmodulin.

[SDE] Environmental SciencesCalmodulin[SDV]Life Sciences [q-bio]Biophysicschemistry.chemical_elementCalciumBiochemistryNeurosporaProtein kinaseNeurospora crassa03 medical and health sciencesAffinity chromatographyCalmodulinStructural BiologyGenetics[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyProtein phosphorylation[SDV.BV] Life Sciences [q-bio]/Vegetal BiologyProtein kinase AMolecular BiologyComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesbiologyNeurospora crassa030306 microbiologyCell Biologybiology.organism_classification[SDV] Life Sciences [q-bio]chemistryBiochemistry[SDE]Environmental Sciencesbiology.proteinPhosphorylationCalcium
researchProduct

Bruton tyrosine kinase-like protein, BtkSD, is present in the marine sponge Suberites domuncula.

2003

Sponges, the simplest and most ancient phylum of Metazoa, encode in their genome complex and highly sophisticated proteins that evolved together with multicellularity and are found only in metazoan animals. We report here the finding of a Bruton tyrosine kinase (BTK)-like protein in the marine sponge Suberites domuncula (Demospongiae). The nucleotide sequence of one sponge cDNA predicts a 700-aa-long protein, which contains all of the characteristic domains for the Tec family of protein tyrosine kinases (PTKs). The highest homology (38% identity, 55% overall similarity) was found with human BTK and TEC PTKs. Sponge PTK was therefore named BtkSD. Human BTK is involved in the maturation of B …

animal structuresDNA ComplementaryeducationMolecular Sequence DataHomology (biology)immune system diseaseshemic and lymphatic diseasesComplementary DNAGeneticsAgammaglobulinaemia Tyrosine KinaseBruton's tyrosine kinaseAnimalsHumansAmino Acid SequenceProtein kinase ACaenorhabditis elegansGeneCaenorhabditis elegansGeneticsbiologySequence Homology Amino AcidKinaseProtein-Tyrosine Kinasesbiology.organism_classificationPoriferaSuberites domunculaMutationbiology.proteinGenomics
researchProduct

Sea urchin deciliation induces thermoresistance and activates the p38 mitogen-activated protein kinase pathway.

2003

In this study, we demonstrate by a variety of approaches (ie, morphological analysis, Western blots, immunolocalization, and the use of specific antibodies) that hyperosmotic deciliation stress of sea urchin embryos induces a thermotolerant response. Deciliation is also able to activate a phosphorylation signaling cascade the effector of which might be the p38 stress-activated protein kinase because we found that the administration of the p38 inhibitor SB203580 to sea urchin deciliated gastrula embryos makes the hyperosmotic deciliation stress lethal.

animal structuresHot TemperaturePyridinesp38 mitogen-activated protein kinasesSEA URCHIN DECILIATION p38MAP KINASEBiochemistryp38 Mitogen-Activated Protein KinasesEnzyme activatorStress Physiologicalbiology.animalAnimalsCiliaSettore BIO/06 - Anatomia Comparata E CitologiaPhosphorylationProtein kinase ASea urchinbiologyEffectorImidazolesAntibodies MonoclonalCell BiologyGastrulaOriginal ArticlesMolecular biologyBlotEnzyme ActivationSea Urchinsembryonic structuresPhosphorylationElectrophoresis Polyacrylamide GelSignal transductionMitogen-Activated Protein KinasesSignal TransductionCell stresschaperones
researchProduct

Cabut, a C2H2 zinc finger transcription factor, is required during Drosophila dorsal closure downstream of JNK signaling.

2005

AbstractDuring dorsal closure, the lateral epithelia on each side of the embryo migrate dorsally over the amnioserosa and fuse at the dorsal midline. Detailed genetic studies have revealed that many molecules are involved in this epithelial sheet movement, either with a signaling function or as structural or motor components of the process. Here, we report the characterization of cabut (cbt), a new Drosophila gene involved in dorsal closure. cbt is expressed in the yolk sac nuclei and in the lateral epidermis. The Cbt protein contains three C2H2-type zinc fingers and a serine-rich domain, suggesting that it functions as a transcription factor. cbt mutants die as embryos with dorsal closure …

animal structuresMorphogenesisBiologyCabutZinc fingerMorphogenesismedicineAnimalsDrosophila ProteinsDorsal closureYolk sacMolecular BiologyTranscription factorYolk nucleiCytoskeletonGeneticsZinc fingerEpidermis (botany)C2H2 Zinc FingerJNK Mitogen-Activated Protein KinasesZinc FingersCell BiologyDorsal closureCell biologymedicine.anatomical_structureDrosophila melanogasterEpidermal Cellsembryonic structuresMutationJNK cascadeDrosophilaJNKDevelopmental BiologySignal TransductionTranscription FactorsDevelopmental biology
researchProduct

Plexin-B1 activates NF-κB and IL-8 to promote a pro-angiogenic response in endothelial cells.

2011

Background The semaphorins and their receptors, the plexins, are proteins related to c-Met and the scatter factors that have been implicated in an expanding signal transduction network involving co-receptors, RhoA and Ras activation and deactivation, and phosphorylation events. Our previous work has demonstrated that Semaphorin 4D (Sema4D) acts through its receptor, Plexin-B1, on endothelial cells to promote angiogenesis in a RhoA and Akt-dependent manner. Since NF-κB has been linked to promotion of angiogenesis and can be activated by Akt in some contexts, we wanted to examine NF-κB in Sema4D treated cells to determine if there was biological significance for the pro-angiogenic phenotype o…

animal structuresRHOAProto-Oncogene Proteins c-aktAngiogenesisSignaling in cellular processesG-protein signalingCancer TreatmentSEMA4Dlcsh:MedicineSignal transductionBiology03 medical and health sciencesMolecular cell biology0302 clinical medicineSemaphorinSettore BIO/10 - BiochimicaAkt Signaling CascadeMembrane Receptor SignalingInterleukin 8lcsh:ScienceBiologyProtein kinase BGTPase signalingRas signaling030304 developmental biology0303 health sciencesMultidisciplinaryMechanisms of Signal Transductionlcsh:RSignaling Cascades3. Good healthCell biologyPlexin B1RNA interferencepro-angiogenicendothelial cellsOncology030220 oncology & carcinogenesisembryonic structuresCancer researchbiology.proteinMedicinelcsh:QAntiangiogenesis TherapyAntiapoptotic signalingSignal transductionResearch ArticlePLoS ONE
researchProduct