Search results for "protein kinase C"

showing 10 items of 180 documents

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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Regulation of the peroxisomal β-oxidation-dependent pathway by peroxisome proliferator-activated receptor α and kinases

2000

The first PPAR (peroxisome proliferator-activated receptor) was cloned in 1990 by Issemann and Green (Nature 347:645-650). This nuclear receptor was so named since it is activated by peroxisome proliferators including several drugs of the fibrate family, plasticizers, and herbicides. This receptor belongs to the steroid receptor superfamily. After activation by a specific ligand, it binds to a DNA response element, PPRE (peroxisome proliferator response element), which is a DR-1 direct repeat of the consensus sequence TGACCT x TGACCT. This mechanism leads to the transcriptional activation of target genes (Motojima et al., J Biol Chem 273:16710-16714, 1998). After the first discovery, severa…

Transcriptional ActivationPeroxisome proliferator-activated receptor gammamedicine.drug_classReceptors Cytoplasmic and NuclearPeroxisome proliferator-activated receptorFibrateBiologyBiochemistryPhosphatidylinositol 3-KinasesmedicineAnimalsHumansPhosphorylationProtein kinase AProtein Kinase CPharmacologychemistry.chemical_classificationPeroxisomeNuclear receptorchemistryBiochemistryPeroxisome Proliferatorslipids (amino acids peptides and proteins)Peroxisome proliferator-activated receptor alphaSignal transductionSignal TransductionTranscription FactorsBiochemical Pharmacology
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Differential roles of PKCα and PKCɛ in controlling the gene expression of Nox4 in human endothelial cells

2007

NADPH oxidases are major sources of superoxide in the vascular wall. This study investigates the role of protein kinase C (PKC) in regulating gene expression of NADPH oxidases. Treatment of human umbilical vein endothelial cells (HUVEC) and HUVEC-derived EA.hy 926 endothelial cells with phorbol 12-myristate 13-acetate (PMA) or phorbol 12,13-dibutyrate led to a PKC-dependent biphasic expression of the gp91phox homolog Nox4. A downregulation of Nox4 was observed at 6 h and an upregulation at 48 h after phorbol ester treatment. The early Nox4 downregulation was associated with a reduced superoxide production, whereas the late Nox4 upregulation was accompanied by a clear enhancement of superoxi…

Umbilical VeinsProtein Kinase C-alphaAngiogenesisDown-RegulationProtein Kinase C-epsilonBiochemistrychemistry.chemical_compoundDownregulation and upregulationSuperoxidesPhysiology (medical)HumansRNA Small InterferingCells CulturedPhorbol 1213-DibutyrateProtein kinase CGene knockdownNADPH oxidasebiologyurogenital systemSuperoxideEndothelial CellsNADPH OxidasesNOX4Molecular biologyUp-RegulationGene Expression RegulationchemistryNADPH Oxidase 4cardiovascular systembiology.proteinPhorbolTetradecanoylphorbol AcetateFree Radical Biology and Medicine
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Activation of protein kinase C alpha and/or epsilon enhances transcription of the human endothelial nitric oxide synthase gene.

1998

In primary human umbilical vein endothelial cells (HUVECs), incubation with phorbol-12-myristate-13-acetate (PMA) enhanced basal and bradykinin-stimulated nitric oxide production. In the HUVEC-derived cell line EA.hy 926, PMA and phorbol-12,13-dibutyrate stimulated endothelial nitric oxide synthase (NOS III) mRNA expression in a concentration- and time-dependent manner. Maximal mRNA expression (3.3-fold increase) was observed after 18 hr. NOS III protein and activity were increased to a similar extent. The specific protein kinase C (PKC) inhibitors bisindolylmaleimide I (1 microM), Gö 6976 [12-(2 cyanoethyl)-6,7,12, 13-tetrahydro-13-methyl-5-oxo-5H-indolo[2,3-a]pyrrolo-[3, 4-c]carbazole] (1…

Umbilical VeinsProtein Kinase C-alphaTime FactorsEndotheliumTranscription GeneticDown-RegulationProtein Kinase C-epsilonBiologyBradykininTransfectionNitric oxidechemistry.chemical_compoundEnzyme StabilitymedicineHumansRNA MessengerEnzyme InhibitorsProtein kinase APromoter Regions GeneticCyclic GMPProtein kinase CCells CulturedProtein Kinase CPharmacologyKinaseMethane sulfonateBiological TransportMolecular biologyUp-RegulationEnzyme ActivationIsoenzymesmedicine.anatomical_structureChelerythrinechemistryGene Expression RegulationCell cultureMolecular MedicineTetradecanoylphorbol AcetateEndothelium VascularNitric Oxide SynthaseMolecular pharmacology
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The 3'-UTR of the mRNA coding for the major protein kinase C substrate MARCKS contains a novel CU-rich element interacting with the mRNA stabilizing …

2003

The expression of the major protein kinase C substrate MARCKS (myristoylated alanine-rich C kinase substrate) is controlled by the stability of its mRNA. While the MARCKS mRNA is long living in quiescent fibroblasts (t1/2 = 14 h), its half-life time is drastically reduced (t1/2 = 2 h) in cells treated with phorbol esters to activate protein kinase C (PKC) or treated with growth factors. In a first step to study the underlying mechanism we identified both a cis-element on the MARCKS mRNA and the corresponding trans-acting factors. Fusing the complete 3'-UTR or specific regions of the 3'-UTR of the MARCKS gene to a luciferase reporter gene caused a drastic decrease in luciferase expression to…

Untranslated regionRecombinant Fusion ProteinsELAV-Like Protein 1Down-RegulationNerve Tissue ProteinsELAV-Like Protein 4BiologyBiochemistryELAV-Like Protein 1MiceGenes ReporterAnimalsRNA MessengerMARCKSLuciferasesMyristoylated Alanine-Rich C Kinase Substrate3' Untranslated RegionsProtein Kinase CProtein kinase CAU-rich elementMessenger RNAThree prime untranslated regionIntracellular Signaling Peptides and ProteinsMembrane ProteinsProteinsRNA-Binding Proteins3T3 CellsFibroblastsMolecular biologyELAV ProteinsAntigens SurfaceMARCKS GeneEuropean Journal of Biochemistry
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Protein kinase C   promotes angiogenic activity of human endothelial cells via induction of vascular endothelial growth factor

2008

Aims Protein kinase C (PKC) plays an important role in the regulation of angiogenesis. However, downstream targets of PKC in endothelial cells are poorly defined. Methods and results mRNA expression of vascular endothelial growth factor (VEGF) was analysed by quantitative real-time RT-PCR in human umbilical vein endothelial cells (HUVEC) and HUVEC-derived EA.hy 926 cells. siRNA was used to knockdown PKC isoforms and VEGF. Matrigel tube formation assay was used to analyse the angiogenic activity of endothelial cells. Phorbol-12-myristate-13-acetate (PMA) enhanced the ability of HUVEC to organize into tubular networks when plated on Matrigel, a phenomenon that could be prevented by PKC inhibi…

Vascular Endothelial Growth Factor Amedicine.medical_specialtyProtein Kinase C-alphaTime FactorsPhysiologyAngiogenesismedicine.medical_treatmentBlotting WesternCarbazolesNeovascularization PhysiologicBiologyPolymerase Chain ReactionCell Linechemistry.chemical_compoundPhysiology (medical)Internal medicinemedicineHumansRNA MessengerRNA Small InterferingCell ShapeProtein Kinase InhibitorsCells CulturedProtein kinase CTube formationMatrigelStem CellsGrowth factorEndothelial CellsUp-RegulationCell biologyEnzyme ActivationEndothelial stem cellVascular endothelial growth factorAutocrine CommunicationVascular endothelial growth factor AReceptors Vascular Endothelial Growth FactorEndocrinologychemistryTetradecanoylphorbol AcetateAngiogenesis Inducing AgentsFibroblast Growth Factor 2RNA InterferenceCardiology and Cardiovascular MedicineCardiovascular Research
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Transmembrane signalling mechanisms regulating expression of cationic amino acid transporters and inducible nitric oxide synthase in rat vascular smo…

1999

The signalling mechanisms involved in the induction of nitric oxide synthase and l-arginine transport were investigated in bacterial lipopolysaccharide (LPS)- and interferon-gamma (IFN-gamma)-stimulated rat cultured aortic smooth muscle cells (RASMCs). The expression profile of transcripts for cationic amino acid transporters (CATs) and their regulation by LPS and IFN-gamma were also examined. Control RASMCs expressed mRNA for CAT-1, CAT-2A and CAT-2B. Levels of all three transcripts were significantly elevated in activated cells. Stimulated CAT mRNA expression and l-arginine transport occurred independently of protein kinase C (PKC), protein tyrosine kinase (PTK) and p44/42 mitogen-activat…

Vascular smooth muscleKinasep38 mitogen-activated protein kinasesCell BiologyBiologyBiochemistryNitric oxideCell biologyNitric oxide synthasechemistry.chemical_compoundchemistrybiology.proteinSignal transductionMolecular BiologyTyrosine kinaseProtein kinase CBiochemical Journal
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Early evolution of metazoan serine/threonine and tyrosine kinases: identification of selected kinases in marine sponges.

1997

The phylum Porifera (sponges) was the first to diverge from the common ancestor of the Metazoa. In this study, six cDNAs coding for protein-serine/threonine kinases (PS/TKs) are presented; they have been isolated from libraries obtained from the demosponges Geodia cydonium and Suberites domuncula and from the calcareous sponge Sycon raphanus. Sequence alignments of the catalytic domains revealed that two major families of PS/TK, the "conventional" (Ca(2+)-dependent) protein kinase C (PKC), the cPKC subfamily, as well as the "novel" (Ca(2+)-independent) PKC (nPKC), form two separate clusters. In each cluster, the sequence from S. raphanus diverges first. To approach the question about the or…

animal structuresSubfamilyDNA ComplementaryMolecular Sequence DataProtein Serine-Threonine KinasesEvolution MolecularSpecies SpecificityGeneticsAnimalsSycon raphanusAmino Acid SequenceCloning MolecularProtein kinase AMolecular BiologyEcology Evolution Behavior and SystematicsProtein kinase CPhylogenyProtein Kinase CCalcareous spongebiologySequence Homology Amino AcidKinaseProtein-Tyrosine Kinasesbiology.organism_classificationPoriferaSuberites domunculaBiochemistryTyrosine kinaseMolecular biology and evolution
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Modulation of protein phosphorylation by natural products

2002

Studies carried out to determine the influence of phosphorylation and dephosphorylation of proteins in a variety of physiological events are of increasing interest. The activity of kinases and phosphatases and their respective inhibition by endogenous mediators and by pharmacological agents regulates a huge number of biochemical pathways involved in cellular proliferation, apoptosis, inflammation, hormonal activity, and gene transcription, amongother processes. This article focuses on the recently described natural products able to interfere negatively with the activity of serine/threonine and tyrosine kinases. These agents are classified, according to theirbiosynthetic origin and chemical …

biologyMAP kinase kinase kinaseBiochemistryCyclin-dependent kinaseKinasebiology.proteinmedicineStaurosporineProtein phosphorylationKinase activityProtein kinase AProtein kinase Cmedicine.drug
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Alterations inras-gene expression and intracellular distribution of protein kinase C in the spongeGeodia cydonium in response to marine pollution

1990

The siliceous spongeGeodia cydonium Jameson was used to study the influence of pollution in marine environments on selected parameters of the intracellular signal transduction pathway. The parameters chosen were: intracellular distribution of protein kinase C (PK-C),ras-gene expression and DNA polymerasealpha (DNA Polalpha) activity. Both PK-C andras-gene product (ras-protein) have previously been established to be key molecules in the intracellular signalling pathway in sponges; increased level ofras-protein mediates events following sponge cell-cell contact. Three unpolluted and three polluted sites in the off-shore seawater around Rovinj (Yugoslavia) were selected for the study in 1989. …

chemistry.chemical_classificationEcologybiologyCell growthAquatic Sciencebiology.organism_classificationTransplantationSpongeCytosolEnzymeBiochemistrychemistryGene expressionEcology Evolution Behavior and SystematicsProtein kinase CIntracellularMarine Biology
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