Search results for "Protein Kinase C-epsilon"

showing 4 items of 4 documents

n-3 PUFAs modulate T-cell activation via protein kinase C-α and -ε and the NF-κB signaling pathway

2005

We elucidated the mechanisms of action of two n-3 PUFAs, eicosapentaenoic acid (EPA) and docosahexaenoic acid (DHA), in Jurkat T-cells. Both DHA and EPA were principally incorporated into phospholipids in the following order: phosphatidylcholine < phosphatidylethanolamine < phosphatidylinositol/phosphatidylserine. Furthermore, two isoforms of phospholipase A(2) (i.e., calcium-dependent and calcium-independent) were implicated in the release of DHA and EPA, respectively, during activation of these cells. The two fatty acids inhibited the phorbol 12-myristate 13-acetate (PMA)-induced plasma membrane translocation of protein kinase C (PKC)-alpha and -epsilon. The two n-3 PUFAs also inhibited t…

PhosphatidylethanolaminePhospholipase Amitogen-activated protein kinaseProtein Kinase C-epsilonQD415-436Cell BiologyPhosphatidylserineBiologyfatty acidsBiochemistryJurkat cellsCell biologychemistry.chemical_compoundEndocrinologychemistryBiochemistryDocosahexaenoic acidlipids (amino acids peptides and proteins)Phosphatidylinositolnuclear factor κBProtein kinase Cpolyunsaturated fatty acidsJournal of Lipid Research
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Cell Susceptibility to Baculovirus Transduction and Echovirus Infection Is Modified by Protein Kinase C Phosphorylation and Vimentin Organization

2013

ABSTRACT Some cell types are more susceptible to viral gene transfer or virus infection than others, irrespective of the number of viral receptors or virus binding efficacy on their surfaces. In order to characterize the cell-line-specific features contributing to efficient virus entry, we studied two cell lines (Ea.hy926 and MG-63) that are nearly nonpermissive to insect-specific baculovirus (BV) and the human enterovirus echovirus 1 (EV1) and compared their characteristics with those of a highly permissive (HepG2) cell line. All the cell lines contained high levels of viral receptors on their surfaces, and virus binding was shown to be efficient. However, in nonpermissive cells, BV and it…

Protein Kinase C-alphaImmunologyVimentinProtein Kinase C-epsilonBiologyModels BiologicalMicrobiologyFilamentous actinCell LineSyndecan 1MiceTransduction (genetics)Transduction GeneticViral entryVirologyAnimalsHumansVimentinPhosphorylationProtein kinase CVirulenceHEK 293 cellsHep G2 CellsVirus InternalizationMolecular biologyvirologyCulture MediaEnterovirus B HumanVirus-Cell InteractionsHEK293 CellsvirologiaCell cultureInsect ScienceHost-Pathogen Interactionsbiology.proteinReceptors VirusSyndecan-1Integrin alpha2beta1BaculoviridaeJournal of Virology
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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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