Search results for "PROTEIN KINASES"

showing 10 items of 427 documents

Function of DcuS from Escherichia coli as a Fumarate-stimulated Histidine Protein Kinase in Vitro

2002

The two-component regulatory system DcuSR of Escherichia coli controls the expression of genes of C(4)-dicarboxylate metabolism in response to extracellular C(4)- dicarboxylates such as fumarate or succinate. DcuS is a membrane-integral sensor kinase, and the sensory and kinase domains are located on opposite sides of the cytoplasmic membrane. The intact DcuS protein (His(6)-DcuS) was overproduced and isolated in detergent containing buffer. His(6)-DcuS was reconstituted into liposomes made from E. coli phospholipids. Reconstituted His(6)-DcuS catalyzed, in contrast to the detergent-solubilized sensor, autophosphorylation by [gamma-(33)P]ATP with an approximate K(D) of 0.16 mm for ATP. Up t…

Time FactorsHistidine KinaseProteolipidsDetergentsBiologymedicine.disease_causeModels BiologicalBiochemistryAdenosine TriphosphateFumaratesEscherichia colimedicinePhosphorylationPromoter Regions GeneticProtein kinase AMolecular BiologyEscherichia coliDose-Response Relationship DrugKinaseEscherichia coli ProteinsCell MembraneAutophosphorylationDNACell BiologyTransmembrane proteinDNA-Binding ProteinsKineticsResponse regulatorBiochemistryLiposomesPhosphorylationSignal transductionProtein KinasesProtein BindingSignal TransductionTranscription FactorsJournal of Biological Chemistry
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In human endothelial cells rapamycin causes mTORC2 inhibition and impairs cell viability and function.

2008

Aim Drug-eluting stents are widely used to prevent restenosis but are associated with late endothelial damage. To understand the basis for this effect, we have studied the consequences of a prolonged incubation with rapamycin on the viability and functions of endothelial cells. Methods and results Human umbilical vein or aorta endothelial cells were exposed to rapamycin in the absence or in the presence of tumour necrosis factor α (TNFα). After a 24 h-incubation, rapamycin (100 nM) caused a significant cell loss associated with the increase of both apoptosis and necrosis, as quantified by propidium iodide staining, caspase 3 activity, and lactate dehydrogenase release. Rapamycin also impair…

Time FactorsPhysiologyApoptosismTORC1Polymerase Chain Reactionchemistry.chemical_compoundCell MovementStress FibersMicroscopy ConfocalCaspase 3TOR Serine-Threonine KinasesNitric Oxide Synthase Type IIIRibosomal Protein S6 Kinases 70-kDaUp-RegulationEndothelial stem cellmedicine.anatomical_structureBiochemistryCardiology and Cardiovascular MedicineE-SelectinEndotheliumNitric Oxide Synthase Type IIICell SurvivalBlotting WesternEnzyme-Linked Immunosorbent AssayBiologyMechanistic Target of Rapamycin Complex 1Nitric OxideTacrolimusNecrosisTheophyllinePhysiology (medical)medicineHumansImmunoprecipitationViability assayPropidium iodideProtein kinase BAdaptor Proteins Signal TransducingSirolimusDose-Response Relationship DrugL-Lactate DehydrogenaseTumor Necrosis Factor-alphaEndothelial CellsProteinsCardiovascular AgentsRegulatory-Associated Protein of mTORMolecular biologyRapamycin-Insensitive Companion of mTOR ProteinchemistryMultiprotein ComplexesTOR Serine-Threonine KinasesCarrier ProteinsProtein KinasesTranscription FactorsCardiovascular research
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Enzymatically hydrolyzed low-density lipoprotein modulates inflammatory responses in endothelial cells

2009

SummaryThere is evidence that low-density lipoprotein (LDL) is modified by hydrolytic enzymes,and that the product (E-LDL) induces selective production of interleukin 8 (IL-8) in endothelial cells. Since nuclear factor-kappaB (NF-κB) is a major regulator of IL-8 transcription, we studied its activation in endothelial cells treated with E-LDL. Unexpectedly,the modified lipoprotein not only failed to activate NF-κB, but completely blocked its activation by tumour necrosis factor-alpha (TNF-α) in EA.hy926-cells, as assessed by electrophoretic mobility shift assays and immunofluorescence. Inhibition occurred upstream of NF-κB translocation, as inhibitor of NF-κB- (IκB)-phosphorylation was suppr…

Time FactorsProto-Oncogene Proteins c-junPyridinesmedicine.medical_treatmentFatty Acids NonesterifiedBiologyp38 Mitogen-Activated Protein KinasesCell Linechemistry.chemical_compoundNF-KappaB Inhibitor alphamedicineHumansTrypsinInterleukin 8PhosphorylationPromoter Regions GeneticProtein Kinase InhibitorsTranscription factorInflammationTumor Necrosis Factor-alphaActivator (genetics)HydrolysisInterleukin-8ImidazolesTranscription Factor RelAEndothelial CellsNF-κBHematologySterol EsteraseMolecular biologyLipoproteins LDLTranscription Factor AP-1Endothelial stem cellCytokineBiochemistrychemistryLow-density lipoproteinI-kappa B ProteinsLipoproteinThrombosis and Haemostasis
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TheSCH9 protein kinase mRNA contains a long 5′ leader with a small open reading frame

1993

The SCH9 yeast gene, that was previously identified as a suppressor of cdc25 and ras1- ras2-ts temperature-sensitive mutants, encodes a putative protein kinase that positively regulates the progression of yeast cells through the G1 phase of the cell cycle. We have determined the structure of the SCH9 transcription unit, using primer extension and S1 mapping techniques. The corresponding mRNA included an unusually long 5' region of more than 600 nucleotides preceding the major open reading frame (ORF). While the latter corresponded to a protein of 824 amino acids, an upstream open reading frame (uORF) within the 5' leader could potentially encode a 54 amino acid peptide. To investigate the r…

Transcription GeneticFive prime untranslated regionMolecular Sequence DataSaccharomyces cerevisiaeBioengineeringSaccharomyces cerevisiaeBiologyApplied Microbiology and BiotechnologyBiochemistryOpen Reading FramesGene Expression Regulation FungalUpstream open reading frameGeneticsAmino Acid SequenceRNA MessengerGenes SuppressorAllelesGeneticsMessenger RNABase SequenceG1 PhaseNucleic acid sequenceRNA Fungalbiology.organism_classificationFusion proteinOpen reading frameRegulatory sequenceMutationProtein KinasesBiotechnologyYeast
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mTOR Driven Gene Transcription Is Required for Cholesterol Production in Neurons of the Developing Cerebral Cortex

2021

AbstractDysregulated mammalian target of rapamycin (mTOR) activity is associated with various neurodevelopmental disorders ranging from idiopathic autism spectrum disorders to syndromes caused by single gene defects. This suggests that maintaining mTOR activity levels in a physiological range is essential for brain development and functioning. Upon activation, mTOR regulates a variety of cellular processes such as cell growth, autophagy and metabolism. On a molecular level, however, the consequences of mTOR activation in the brain are not well understood.Low levels of cholesterol are associated with a wide variety of neurodevelopmental disorders. We here describe numerous genes of the stero…

Transcription GeneticQH301-705.5Primary Cell CulturemTORC1Mechanistic Target of Rapamycin Complex 1BiologySREBPCatalysisArticleInorganic ChemistryMiceAutophagyTranscriptional regulationmedicineAnimalsPhysical and Theoretical ChemistryBiology (General)Molecular BiologyTranscription factorQD1-999mTORC1SpectroscopyPI3K/AKT/mTOR pathwayCerebral CortexNeuronsSterol Regulatory Element Binding ProteinsCell growthTOR Serine-Threonine KinasesOrganic Chemistrycholesterol ; NF-Y ; neurogenesis ; mTOR ; mTORC1 ; SP1 ; SREBPAutophagyGene Expression Regulation DevelopmentalcholesterolGeneral MedicineComputer Science ApplicationsSterol regulatory element-binding proteinCell biologySP1Chemistryneurogenesismedicine.anatomical_structureCCAAT-Binding FactorCerebral cortexmTORNF-YProtein KinasesSignal TransductionInternational Journal of Molecular Sciences
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ADR1 and SNF1 Mediate Different Mechanisms in Transcriptional Regulation of Yeast POT1 Gene

1994

We studied the consequences of adr1 and snf1 mutations on POT1 gene expression in different growth conditions. The results obtained reveal that ADR1 and SNF1 genes affect POT1 transcription in different ways: ADR1 has a minor role in derepression in low concentration of glucose but is essential for activation in stationary phase whereas SNF1 is essential for derepression and activation, although it does not seem to be directly involved in the molecular mechanism of activation in stationary phase.

Transcription GeneticRecombinant Fusion ProteinsGenes FungalBiophysicsSaccharomyces cerevisiaeBiologyMicrobodiesBiochemistryTranscription (biology)Gene Expression Regulation FungalGene expressionTranscriptional regulationAcetyl-CoA C-AcetyltransferaseLuciferasesMolecular BiologyGeneDerepressionRegulation of gene expressionGeneticsfungiGene Transfer TechniquesCell BiologyYeastCulture MediaCell biologycarbohydrates (lipids)GlucoseStationary phaseMutationProtein KinasesBiochemical and Biophysical Research Communications
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Ethylene modulates gene expression in cells of the marine sponge Suberites domuncula and reduces the degree of apoptosis.

1999

Sponges (phylum Porifera) live in an aqueous milieu that contains dissolved organic carbon. This is degraded photochemically by ultraviolet radiation to alkenes, particularly to ethylene. This study demonstrates that sponge cells (here the demosponge Suberites domuncula has been used), which have assembled to primmorphs, react to 5 microM ethylene with a significant up-regulation of intracellular Ca(2+) concentration and with a reduction of starvation-induced apoptosis. In primmorphs from S. domuncula the expression of two genes is up-regulated after exposure to ethylene. The cDNA of the first gene (SDERR) isolated from S. domuncula encodes a potential ethylene-responsive protein, termed ER…

Transcriptional ActivationEthyleneMolecular Sequence DataApoptosisMarine BiologyBiochemistryEvolution Molecularchemistry.chemical_compoundComplementary DNAGene expressionBotanyAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyGenePlant Proteinschemistry.chemical_classificationbiologySequence Homology Amino AcidKinaseProteinsCell BiologySequence Analysis DNAEthylenesbiology.organism_classificationAmino acidPoriferaSuberites domunculaSpongechemistryBiochemistryGene Expression RegulationProtein BiosynthesisCalcium-Calmodulin-Dependent Protein KinasesCalcium-Calmodulin-Dependent Protein Kinase Type 2Food DeprivationSignal TransductionThe Journal of biological chemistry
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Cadmium effects on p38/MAPK isoforms in MDA-MB231 breast cancer cells

2009

Emerging evidence seems to indicate that the heavy metal cadmium (Cd) is able to regulate gene expression, drastically affecting the pattern of transcriptional activity in normal and pathological eukaryotic cells, also affecting intracellular signalization events. Human p38 is a family of mitogen-activated protein kinases consisting of four isoforms (alpha, beta, gamma and delta) which mediate signal transduction cascades controlling several aspects of cell physiology. In this study we examined whether exposure of MDA-MB231 tumor cells from the human breast to Cd may exert some effect on p38 isoform expression and accumulation, as well as on p38 activation. Employing a combination of prolif…

Transcriptional ActivationGene isoformCadmium SB203580 p38 isoforms p38 activation Gene expressionCell SurvivalPyridinesp38 mitogen-activated protein kinasesBreast NeoplasmsBiologyp38 Mitogen-Activated Protein KinasesGene Expression Regulation EnzymologicGeneral Biochemistry Genetics and Molecular BiologyBiomaterialsStructure-Activity RelationshipGene expressionTumor Cells CulturedHumansSettore BIO/06 - Anatomia Comparata E CitologiaCell ProliferationRegulation of gene expressionDose-Response Relationship DrugKinaseImidazolesMetals and AlloysMolecular biologyCell biologyIsoenzymesCell cultureDrug Screening Assays AntitumorSignal transductionGeneral Agricultural and Biological SciencesIntracellularCadmiumBioMetals
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The Streptococcal Exotoxin Streptolysin O Activates Mast Cells To Produce Tumor Necrosis Factor Alpha by p38 Mitogen-Activated Protein Kinase- and Pr…

2003

ABSTRACTStreptolysin O (SLO), a major virulence factor of pyogenic streptococci, binds to cholesterol in the membranes of eukaryotic cells and oligomerizes to form large transmembrane pores. While high toxin doses are rapidly cytocidal, low doses are tolerated because a limited number of lesions can be resealed. Here, we report that at sublethal doses, SLO activates primary murine bone marrow-derived mast cells to degranulate and to rapidly induce or enhance the production of several cytokine mRNAs, including tumor necrosis factor alpha (TNF-α). Mast cell-derived TNF-α plays an important protective role in murine models of acute inflammation, and the production of this cytokine was analyzed…

Transcriptional ActivationImmunologyBiologyp38 Mitogen-Activated Protein KinasesMicrobiologyMiceBacterial ProteinsmedicineAnimalsASK1Mast CellsRNA MessengerProtein kinase AProtein Kinase CProtein kinase CMice Inbred BALB CDose-Response Relationship DrugTumor Necrosis Factor-alphaMast cellMolecular PathogenesisProtein kinase RMolecular biologyInterleukin 33Infectious Diseasesmedicine.anatomical_structureStreptolysinsParasitologyTumor necrosis factor alphaStreptolysinMitogen-Activated Protein KinasesInfection and Immunity
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Histamine Upregulates Gene Expression of Endothelial Nitric Oxide Synthase in Human Vascular Endothelial Cells

2003

Background— Histamine has a short-term, transient, stimulating effect on endothelial nitric oxide synthase (eNOS) activity; however, long-term effects on eNOS have not been described yet. In addition, the vascular effect of histamine seems to depend critically on eNOS functionality. Therefore, we studied the effects of histamine on eNOS gene expression and function. Methods and Results— In human umbilical vein endothelial cells (HUVECs) and HUVEC-derived EA.hy 926 cells, histamine upregulated eNOS mRNA (RNase protection assay) and protein (electron microscopic immunocytochemistry) expression. The upregulation of eNOS could be prevented by mepyramine, a selective antagonist at the H 1 recep…

Transcriptional Activationmedicine.medical_specialtyNitric Oxide Synthase Type IIIEndotheliumHistamine H1 receptorNitric OxideCell LineNitric oxidechemistry.chemical_compoundEnosPhysiology (medical)Internal medicinemedicineHumansRNA MessengerReceptors Histamine H1Enzyme InhibitorsPromoter Regions GeneticProtein Kinase InhibitorsCells CulturedDose-Response Relationship DrugbiologyNitric Oxide Synthase Type IIIbiology.organism_classificationMolecular biologyUp-RegulationNitric oxide synthaseKineticsOxidative StressEndocrinologymedicine.anatomical_structurechemistryEnzyme InductionCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinEndothelium VascularNitric Oxide SynthaseHistamine H3 receptorCalcium-Calmodulin-Dependent Protein Kinase Type 2Reactive Oxygen SpeciesCardiology and Cardiovascular MedicineHistamineHistamineCirculation
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