Search results for "messenger"

showing 10 items of 1493 documents

Docosahexaenoic acid inhibits cancer cell growth via p27Kip1, CDK2, ERK1/ERK2, and retinoblastoma phosphorylation

2006

Docosahexaenoic acid (DHA), a PUFA of the n-3 family, inhibited the growth of FM3A mouse mammary cancer cells by arresting their progression from the late-G(1) to the S phase of the cell cycle. DHA upregulated p27(Kip1) levels by inhibiting phosphorylation of mitogen-activated protein (MAP) kinases, i.e., ERK1/ERK2. Indeed, inhibition of ERK1/ERK2 phosphorylation by DHA, U0126 [chemical MAPK extracellularly signal-regulated kinase kinase (MEK) inhibitor], and MEK(SA) (cells expressing dominant negative constructs of MEK) resulted in the accumulation of p27(Kip1). MAP kinase (MAPK) inhibition by DHA did not increase p27(Kip1) mRNA levels. Rather, this fatty acid stabilized p27(Kip1) contents…

MAPK/ERK pathwayDocosahexaenoic AcidsMammary Neoplasms AnimalQD415-436fatty acidsenvironment and public healthBiochemistryMiceEndocrinologyCyclin-dependent kinaseCyclin EAnimalsRNA MessengerPhosphorylationCells CulturedCell ProliferationMAPK14biologyKinaseCyclin-dependent kinase 4Cyclin-Dependent Kinase 2Cyclin-dependent kinase 2Retinoblastomafood and beveragesCell BiologyUp-RegulationCell biologyenzymes and coenzymes (carbohydrates)cyclin-dependent kinaseCyclin-dependent kinase complexbiology.proteinPhosphorylationcell cyclelipids (amino acids peptides and proteins)Mitogen-Activated Protein KinasesCyclin-Dependent Kinase Inhibitor p27Journal of Lipid Research
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The stimulation of arginine transport by TNFα in human endothelial cells depends on NF-κB activation

2004

In human saphenous vein endothelial cells (HSVECs), tumor necrosis factor-alpha (TNFalpha) and bacterial lipopolysaccharide (LPS), but neither interferon gamma (IFNgamma) nor interleukin 1beta (IL-1beta), stimulate arginine transport. The effects of TNFalpha and LPS are due solely to the enhancement of system y+ activity, whereas system y+L is substantially unaffected. TNFalpha causes an increased expression of SLC7A2/CAT-2B gene while SLC7A1/CAT-1 expression is not altered by the cytokine. The suppression of PKC-dependent transduction pathways, obtained with the inhibitor chelerytrhine, the inhibitor peptide of PKCzeta isoform, or chronic exposure to phorbol esters, does not prevent TNFalp…

MAPK/ERK pathwayLipopolysaccharidesmedicine.medical_specialtyUmbilical VeinsTime FactorsCAT transporterArginineTranscription Geneticp38 mitogen-activated protein kinasesmedicine.medical_treatmentBiophysicsPharmacologyBiologyArgininePolymerase Chain Reactionp38 Mitogen-Activated Protein KinasesBiochemistryInterferon-gammaInternal medicineCationsmedicineTNFαHumansInterferon gammaRNA MessengerCationic Amino Acid Transporter 2Cells CulturedProtein Kinase CArginine transportReverse Transcriptase Polymerase Chain ReactionTumor Necrosis Factor-alphaNF-kappa BBiological TransportCell BiologyCytokineEndocrinologySLC7 geneAmino Acid Transport Systems BasicCytokinesTumor necrosis factor alphaEndothelium VascularSignal transductionMitogen-Activated Protein KinasesPeptidesmedicine.drugInterleukin-1Signal TransductionNFκBBiochimica et Biophysica Acta (BBA) - Biomembranes
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Down-regulation of human CYP3A4 by the inflammatory signal interleukin-6: molecular mechanism and transcription factors involved.

2002

The hepatic drug-metabolizing cytochrome P-450 (CYP) enzymes are down-regulated during inflammation. In vitro studies with hepatocytes have shown that the cytokines released during inflammatory responses are largely responsible for this CYP repression. However, the signaling pathways and the cytokine-activated factors involved remain to be properly identified. Our research has focused on the negative regulation of CYP3A4 (the major drug-metabolizing human CYP) by interleukin 6 (IL-6) (the principal regulator of the hepatic acute-phase response). CYP3A4 down-regulation by IL-6 requires activation of the glycoprotein receptor gp130; however, it does not proceed through the JAK/STAT pathway, a…

MAPK/ERK pathwaySTAT3 Transcription FactorMAP Kinase Signaling Systemp38 mitogen-activated protein kinasesDown-RegulationBiologyBiochemistryTransactivationCytochrome P-450 Enzyme SystemAntigens CDGeneticsCCAAT-Enhancer-Binding Protein-alphaCytokine Receptor gp130Tumor Cells CulturedCytochrome P-450 CYP3AHumansRNA MessengerSTAT3Molecular BiologyTranscription factorCells CulturedMembrane GlycoproteinsDose-Response Relationship DrugInterleukin-6Reverse Transcriptase Polymerase Chain ReactionCCAAT-Enhancer-Binding Protein-betaJAK-STAT signaling pathwayProtein-Tyrosine KinasesGlycoprotein 130Molecular biologyDNA-Binding ProteinsGene Expression Regulationbiology.proteinHepatocytesTrans-ActivatorsSignal transductionBiotechnologyAcute-Phase ProteinsSignal TransductionTranscription FactorsFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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Global Functional Analyses of Cellular Responses to Pore-Forming Toxins

2011

Here we present the first global functional analysis of cellular responses to pore-forming toxins (PFTs). PFTs are uniquely important bacterial virulence factors, comprising the single largest class of bacterial protein toxins and being important for the pathogenesis in humans of many Gram positive and Gram negative bacteria. Their mode of action is deceptively simple, poking holes in the plasma membrane of cells. The scattered studies to date of PFT-host cell interactions indicate a handful of genes are involved in cellular defenses to PFTs. How many genes are involved in cellular defenses against PFTs and how cellular defenses are coordinated are unknown. To address these questions, we pe…

MAPK/ERK pathwayTranscription GeneticImmunology/Innate ImmunityMessengerInteractomeInfectious Diseases/Bacterial InfectionsRNA interference2.1 Biological and endogenous factorsAetiologyBiology (General)Genes HelminthCaenorhabditis elegansOligonucleotide Array Sequence AnalysisGenetics0303 health sciencesGenomebiologyReverse Transcriptase Polymerase Chain ReactionGenetics and Genomics/Functional Genomics030302 biochemistry & molecular biologyrespiratory systemCell biologyInfectious DiseasesMedical MicrobiologyRNA InterferenceSignal transductionDNA microarrayTranscriptionBiotechnologyResearch ArticleSignal TransductionPore Forming Cytotoxic ProteinsQH301-705.5Virulence FactorsMAP Kinase Signaling System1.1 Normal biological development and functioningBacterial ToxinsImmunologyMicrobiologyDNA-binding proteinCell Line03 medical and health sciencesBacterial ProteinsGeneticUnderpinning researchVirologyEscherichia coliHelminthGeneticsAnimalsHumansRNA MessengerCaenorhabditis elegansCaenorhabditis elegans ProteinsMolecular BiologyGene030304 developmental biologyGenome HelminthCell MembraneGenetics and GenomicsRC581-607biology.organism_classificationrespiratory tract diseasesTranscription Factor AP-1Emerging Infectious DiseasesGenesRNAParasitologyGeneric health relevanceRNA HelminthImmunologic diseases. AllergyPLoS Pathogens
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Effect of oxidative stress on UDP-glucuronosyltransferases in rat astrocytes.

2012

WOS:000309170300003; International audience; The present work reports data regarding effects of an induced oxidative stress on the mainly expressed isoforms of UDP-glucuronosyltransferases (UGTs) in the brain. UGT1A6 and UGT1A7 expression and enzymatic activities toward the 1-naphthol were analyzed in rat cultured astrocytes following the exposure for 48 h to redox-cycling xenobiotic compounds such as quinones and bipyridinium ions. The expression of NADPH:cytochrome P450 reductase and NAD(P)H:quinone oxidoreductase 1 (NQO1) was also investigated. Oxidative stress induced significant deleterious changes in astrocyte morphology, decreased cell viability and inhibited catalytic function of UG…

MESH : Oxidative StressMESH : RNA MessengerAntioxidantTranscription Geneticmedicine.medical_treatmentToxicologyNAD(P)H:quinone oxidoreductase 1MESH: GlucuronosyltransferaseAntioxidantsSubstrate SpecificityRats Sprague-Dawley0302 clinical medicineMESH: NADPH-Ferrihemoprotein ReductaseMESH: GlucuronidesNAD(P)H Dehydrogenase (Quinone)MESH : CatalysisMESH: AnimalsMESH : NAD(P)H Dehydrogenase (Quinone)GlucuronosyltransferaseCells Culturedchemistry.chemical_classificationMESH : Cell Survival0303 health sciencesMESH : Substrate SpecificityMESH : Animals NewbornCytochrome P450 reductaseGeneral MedicineMESH: Cell SurvivalMESH: Pyridinium CompoundsMESH : AntioxidantsMESH: Cells CulturedOxidative phosphorylationGene Expression Regulation EnzymologicMESH : QuinonesMESH : Glucuronides03 medical and health sciencesRNA MessengerCell ShapeNADPH-Ferrihemoprotein ReductaseMESH : Oxidation-ReductionMESH : Pyridinium CompoundsMESH: NaphtholsMESH : GlucuronosyltransferaseMESH: AntioxidantsMESH: CatalysischemistryOxidative stressAstrocytesReactive Oxygen Species030217 neurology & neurosurgeryMESH: Oxidation-ReductionTime Factors[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionMESH : Reactive Oxygen SpeciesNADPH:cytochrome P450 reductasePyridinium CompoundsNaphtholsMESH: Rats Sprague-DawleyProtein oxidationmedicine.disease_causeMESH: Animals NewbornMESH: NAD(P)H Dehydrogenase (Quinone)Protein CarbonylationMESH : OxidantsMESH: OxidantsMelatoninMESH: MelatoninMESH: Oxidative StressMESH : MelatoninMESH : RatsMESH: Gene Expression Regulation EnzymologicQuinonesMESH: Reactive Oxygen SpeciesOxidantsBiochemistryMESH : Protein CarbonylationOxidation-ReductionUDP-glucuronosyltransferaseMESH : Time FactorsMESH: Protein CarbonylationMESH: RatsCell SurvivalMESH : NaphtholsBiologyCatalysisMESH: QuinonesMESH : Gene Expression Regulation EnzymologicGlucuronidesMESH : Cells CulturedmedicineAnimalsMESH: Cell Shape030304 developmental biologyMESH: RNA MessengerReactive oxygen speciesMESH: Transcription GeneticMESH: Time FactorsMESH : AstrocytesMESH : Transcription GeneticNAD(P)H Dehydrogenase (Quinone)MESH : Rats Sprague-DawleyRatsMESH: AstrocytesAnimals NewbornMESH : NADPH-Ferrihemoprotein ReductaseMESH: Substrate SpecificityMESH : AnimalsNAD+ kinaseMESH : Cell Shape[SDV.AEN]Life Sciences [q-bio]/Food and NutritionOxidative stress
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Modulation of the hepatic fatty acid pool in peroxisomal 3-ketoacyl-CoA thiolase B-null mice exposed to the selective PPARalpha agonist Wy14,643

2009

10 pages; International audience; The peroxisomal 3-ketoacyl-CoA thiolase B (Thb) gene was previously identified as a direct target gene of PPARalpha, a nuclear hormone receptor activated by hypolipidemic fibrate drugs. To better understand the role of ThB in hepatic lipid metabolism in mice, Sv129 wild-type and Thb null mice were fed or not the selective PPARalpha agonist Wy14,643 (Wy). Here, it is shown that in contrast to some other mouse models deficient for peroxisomal enzymes, the hepatic PPARalpha signaling cascade in Thb null mice was normal under regular conditions. It is of interest that the hypotriglyceridemic action of Wy was reduced in Thb null mice underlining the conclusion t…

MESH : RNA MessengerMESH: Microsomes LiverMESH : PyrimidinesMono-unsaturated fatty acids n-7 and n-9MESH : Hepatocytes[SDV.BBM.BM] Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyMESH: Mice KnockoutPPARαBiochemistryMESH: Acetyl-CoA C-AcetyltransferaseStearoyl-CoA desaturase-1MESH: HepatocytesMicechemistry.chemical_compoundMESH : Lipid MetabolismWy14MESH: AnimalsPeroxisomal 3-ketoacyl-CoA thiolase BAcetyl-CoA C-AcetyltransferaseMESH: PPAR alphaMESH : Fatty AcidsMESH: Lipid MetabolismMice Knockoutchemistry.chemical_classificationThiolaseFatty Acids643General MedicinePeroxisomeMESH : Stearoyl-CoA DesaturaseMESH: Fatty AcidsMESH : Microsomes LiverMESH : Acetyl-CoA C-AcetyltransferaseMicrosomes LiverMono-unsaturated fatty acids n-7 and n-9; Peroxisomal 3-ketoacyl-CoA thiolase B; PPARα; Stearoyl-CoA desaturase-1; Wy14643lipids (amino acids peptides and proteins)Stearoyl-CoA DesaturasePolyunsaturated fatty acidmedicine.medical_specialtyMESH : PPAR alphaMESH : Mice Inbred C57BL[ SDV.BBM.BM ] Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyBiologyMESH: Mice Inbred C57BLInternal medicineMESH : MicePeroxisomesmedicineAnimalsHumansPPAR alphaRNA MessengerMESH: MiceMESH: RNA MessengerSCP2MESH: HumansMESH : HumansFatty acid[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyStearoyl-CoALipid MetabolismMESH: PeroxisomesSterol regulatory element-binding proteinMice Inbred C57BLPyrimidinesEndocrinologychemistryMESH: PyrimidinesMESH: Stearoyl-CoA DesaturaseHepatocytesMESH : Mice KnockoutMESH : AnimalsStearoyl-CoA desaturase-1MESH : PeroxisomesBiochimie
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Agr system of Listeria monocytogenes EGD-e: role in adherence and differential expression pattern.

2007

ABSTRACT In this study, we investigated the agrBDCA operon in the pathogenic bacterium Listeria monocytogenes EGD-e. In-frame deletion of agrA and agrD resulted in an altered adherence and biofilm formation on abiotic surfaces, suggesting the involvement of the agr system of L. monocytogenes during the early stages of biofilm formation. Real-time PCR experiments indicated that the transcript levels of agrBDCA depended on the stage of biofilm development, since the levels were lower after the initial attachment period than during biofilm growth, whereas transcription during planktonic growth was not growth phase dependent. The mRNA quantification data also suggested that the agr system was a…

MESH : RNA MessengerTranscription GeneticOperon[ SDV.MP.BAC ] Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriologymedicine.disease_causeMESH: Listeria monocytogenesApplied Microbiology and BiotechnologyBacterial AdhesionRapid amplification of cDNA endsTranscription (biology)MESH : Bacterial ProteinsMESH : DNA BacterialMESH: Bacterial Proteins0303 health sciencesMESH : Trans-ActivatorsMESH: Gene Expression Regulation BacterialEcologycell-to-cell communicationMESH : BiofilmsBiotechnologyMESH : Gene Expression Regulation BacterialDNA BacterialMESH : Bacterial AdhesionMESH: Trans-ActivatorsGenetics and Molecular BiologyMESH: BiofilmsBiologyagr systemMicrobiology03 medical and health sciencesListeria monocytogenesBacterial ProteinsmedicineMESH: Bacterial AdhesionRNA MessengerGene030304 developmental biologyMESH: RNA MessengerMessenger RNA030306 microbiologyMESH: Transcription GeneticBiofilmMESH : Transcription GeneticGene Expression Regulation Bacterialbiochemical phenomena metabolism and nutritionbiology.organism_classificationMolecular biologyMESH: DNA Bacterial[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyListeria monocytogenesBiofilmsbiofilm formationTrans-ActivatorsMESH : Listeria monocytogenesBacteriaFood ScienceApplied and environmental microbiology
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Symplekin, a polyadenylation factor, prevents MOZ and MLL activity on HOXA9 in hematopoietic cells

2013

International audience; MOZ and MLL encoding a histone acetyltransferase and a histone methyltransferase, respectively, are targets for recurrent chromosomal translocations found in acute myeloblastic or lymphoblastic leukemia. We have previously shown that MOZ and MLL cooperate to activate HOXA9 gene expression in hematopoietic stem/progenitors cells. To dissect the mechanism of action of this complex, we decided to identify new proteins interacting with MOZ. We found that the scaffold protein Symplekin that supports the assembly of polyadenylation machinery was identified by mass spectrometry. Symplekin interacts and co-localizes with both MOZ and MLL in immature hematopoietic cells. Its …

MLLScaffold proteinPolyadenylationHematopoietic System[SDV]Life Sciences [q-bio]PolyadenylationCell Line03 medical and health scienceschemistry.chemical_compound0302 clinical medicinehemic and lymphatic diseasesGene expressionTranscriptional regulationHumansRNA MessengerPromoter Regions GeneticSymplekinHSF1neoplasmsMolecular BiologyHistone Acetyltransferases030304 developmental biologyHomeodomain ProteinsmRNA Cleavage and Polyadenylation Factors0303 health sciences[ SDV ] Life Sciences [q-bio]biologyNuclear ProteinsHistone-Lysine N-MethyltransferaseHOXA9Transcription regulationCell BiologyHistone acetyltransferaseMOZCell biology[SDV] Life Sciences [q-bio]Protein TransportRUNX1chemistry030220 oncology & carcinogenesisHistone methyltransferaseCancer researchbiology.proteinMyeloid-Lymphoid Leukemia ProteinProtein BindingBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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Colony-stimulating factor-1-induced oscillations in phosphatidylinositol-3 kinase/AKT are required for caspase activation in monocytes undergoing dif…

2009

Abstract The differentiation of human peripheral blood monocytes into resident macrophages is driven by colony-stimulating factor-1 (CSF-1), which upon interaction with CSF-1 receptor (CSF-1R) induces within minutes the phosphorylation of its cytoplasmic tyrosine residues and the activation of multiple signaling complexes. Caspase-8 and -3 are activated at day 2 to 3 and contribute to macrophage differentiation, for example, through cleavage of nucleophosmin. Here, we show that the phosphatidylinositol-3 kinase and the downstream serine/threonine kinase AKT connect CSF-1R activation to caspase-8 cleavage. Most importantly, we demonstrate that successive waves of AKT activation with increasi…

Macrophage colony-stimulating factorCellular differentiationImmunologyImmunoblottingApoptosisBiologyBiochemistryMonocytesImmunoenzyme TechniquesPhosphatidylinositol 3-KinasesHumansImmunoprecipitationRNA MessengerPhosphorylationProtein kinase BCells CulturedPhosphoinositide-3 Kinase InhibitorsMitogen-Activated Protein Kinase 1Caspase 8Mitogen-Activated Protein Kinase 3MAP kinase kinase kinaseKinaseAkt/PKB signaling pathwayReverse Transcriptase Polymerase Chain ReactionMacrophage Colony-Stimulating FactorMacrophagesCell DifferentiationCell BiologyHematologyFlow CytometryCell biologyEnzyme ActivationPhosphorylationSignal transductionProto-Oncogene Proteins c-aktSignal TransductionBlood
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Keratinocyte-Derived Granulocyte-Macrophage Colony Stimulating Factor Accelerates Wound Healing: Stimulation of Keratinocyte Proliferation, Granulati…

2001

Chronic, nonhealing wounds represent a major clinical challenge to practically all disciplines in modern medicine including dermatology, oncology, surgery, and hematology. In skin wounds, granulocyte-macrophage colony stimulating factor (GM-CSF) is secreted by keratinocytes shortly after injury and mediates epidermal cell proliferation in an autocrine manner. Many other cells involved in wound healing including macrophages, lymphocytes, fibroblasts, endothelial cells, and dendritic cells synthesize GM-CSF and/or are targets of this cytokine. Therefore, GM-CSF is a pleiotropic cytokine evoking complex processes during wound repair. Despite this complexity and the scarcity of mechanistic unde…

Macrophage colony-stimulating factorKeratinocytesMalemedicine.medical_treatmentGene ExpressionMitosisNeovascularization PhysiologicMice TransgenicDermatologytransgenic miceBiologyBiochemistryProinflammatory cytokineTransforming Growth Factor beta1MiceTransforming Growth Factor betamedicineAnimalsRNA MessengerAutocrine signallingMolecular BiologySkinWound Healingintegumentary systemGranulation tissueGranulocyte-Macrophage Colony-Stimulating FactorGM-CSFCell BiologyUp-RegulationCytokinemedicine.anatomical_structureGranulocyte macrophage colony-stimulating factorImmunologyModels AnimalCancer researchCarcinogensGranulation TissueCytokinesTetradecanoylphorbol AcetateFemaleKeratinocyteWound healingmedicine.drugJournal of Investigative Dermatology
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