Search results for "c-jun"

showing 10 items of 33 documents

Temporospatial expression of HSP72 and c-JUN, and DNA fragmentation in goat hippocampus after global cerebral ischemia

2001

The role of gene induction (expression of HSP72 and c-JUN proteins) and delayed ischemic cell death (in situ labeling of DNA fragmentation) have been investigated in the goat hippocampus after transient global cerebral ischemia. The animals were subjected to 20-min ischemia (bilateral occlusion of the external carotid arteries plus bilateral jugular vein compression) and allowed to reperfuse for 2 h, and then 1, 3, and 7 days. Histological signs of cell loss were not found in the hippocampus at 2 h, 1 day, or 3 days of reperfusion. However, such an ischemic insult produced extensive, selective, and delayed degeneration in the hippocampus, as 68% of the neurons in CA1 had died at 7 days, but…

Programmed cell deathCognitive NeuroscienceDentate gyrusc-junIschemiaSubiculumHippocampusBiologymedicine.diseasenervous systemApoptosismedicineDNA fragmentationNeuroscienceHippocampus
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Piclamilast inhibits the pro-apoptotic and anti-proliferative responses of A549 cells exposed to H(2)O(2) via mechanisms involving AP-1 activation.

2012

Reactive oxygen species (ROS) are involved in the pathogenesis of many inflammatory diseases such as chronic obstructive pulmonary disease (COPD). They can alter the expression of genes involved in cellular damage by activating transcription factors, including the NF-κB and the activator protein 1 (AP-1). Phosphodiesterase type 4 (PDE4) inhibitors have anti-inflammatory and antioxidant effects, as described in in vivo and in vitro COPD models. This study analysed the effects of piclamilast, a selective PDE4 inhibitor, on modulating the global gene expression profile in A549 cells exposed to H(2)O(2).Changes in gene expression were analysed using high-density Affymetrix microarrays and valid…

Proto-Oncogene Proteins c-junPyridinesActivating transcription factorApoptosisBiologymedicine.disease_causeBiochemistryAntioxidantschemistry.chemical_compoundPulmonary Disease Chronic ObstructiveIn vivoAnnexinCell Line TumorGene expressionmedicineHumansRNA MessengerPhosphorylationCell ProliferationOligonucleotide Array Sequence AnalysisA549 cellGene Expression ProfilingNF-kappa BGeneral MedicineCell Cycle CheckpointsHydrogen PeroxideMolecular biologyTranscription Factor AP-1chemistryGene Expression RegulationAlveolar Epithelial CellsBenzamidesPhosphodiesterase 4 InhibitorsSignal transductionReactive Oxygen SpeciesPiclamilastOxidative stressSignal TransductionFree radical research
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Theileria parasites secrete a prolyl isomerase to maintain host leukocyte transformation

2015

Infectious agents develop intricate mechanisms to interact with host cell pathways and hijack their genetic and epigenetic machinery to change host cell phenotypic states. Among the Apicomplexa phylum of obligate intracellular parasites, which cause veterinary and human diseases, Theileria is the only genus that transforms its mammalian host cells. Theileria infection of bovine leukocytes induces proliferative and invasive phenotypes associated with activated signalling pathways, notably JNK and AP-1 (ref. 2). The transformed phenotypes are reversed by treatment with the theilericidal drug buparvaquone. We used comparative genomics to identify a homologue of the peptidyl-prolyl isomerase PI…

Proto-Oncogene Proteins c-jun[SDV]Life Sciences [q-bio]Drug ResistanceparasitesBiologyArticleCell LineHost-Parasite InteractionsmiR-155TheileriaTheileriaLeukocytesProlyl isomeraseAnimalsHumanscancerSecretionNIMA-Interacting Peptidylprolyl IsomeraseZebrafishComputingMilieux_MISCELLANEOUSPeptidylprolyl isomeraseSKP Cullin F-Box Protein LigasesMultidisciplinaryProtein StabilityGeneral CommentaryIntracellular parasiteUbiquitinationPeptidylprolyl Isomerasebiology.organism_classificationXenograft Model Antitumor AssaysMolecular biology3. Good healthCell biologyUbiquitin ligaseNIMA-Interacting Peptidylprolyl IsomeraseTranscription Factor AP-1Cell Transformation NeoplasticSchistosoma haematobiumPIN1biology.proteinMedicineCattleNaphthoquinonesSignal Transduction
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Age-dependent regulation of antioxidant genes by p38α MAPK in the liver

2018

p38α is a redox sensitive MAPK activated by pro-inflammatory cytokines and environmental, genotoxic and endoplasmic reticulum stresses. The aim of this work was to assess whether p38α controls the antioxidant defense in the liver, and if so, to elucidate the mechanism(s) involved and the age-related changes. For this purpose, we used liver-specific p38α-deficient mice at two different ages: young-mice (4 months-old) and old-mice (24 months-old). The liver of young p38α knock-out mice exhibited a decrease in GSH levels and an increase in GSSG/GSH ratio and malondialdehyde levels. However, old mice deficient in p38α had higher hepatic GSH levels and lower GSSG/GSH ratio than young p38α knock-…

ROS Reactive oxygen species;RSK1 Ribosomal S6 kinase10301 basic medicineMAPK/ERK pathwayAgingHPLC High-performance liquid chromatographyAntioxidantmedicine.medical_treatmentTBP TATA-binding proteinClinical BiochemistryDEN Diethyl nitrosamine;MKP-1 MAPK phosphatase-1IκB kinaseGCLc Glutamate cysteine ligase catalytic subunitp38 Mitogen-Activated Protein KinasesG6PDH Glucose-6-phosphate dehydrogenaseBiochemistryAntioxidantsMicechemistry.chemical_compoundSuperoxide Dismutase-1Akt Protein kinase B0302 clinical medicineNrf2 Nuclear factor erythroid 2-related factor-2IL InterleukinSOD1 Cu/Zn-superoxide dismutaselcsh:QH301-705.5Mice KnockoutMK2 MAP-activated protein kinase 2;PGC-1α Peroxisome proliferator-activated receptor gamma coactivator 1-alphachemistry.chemical_classificationlcsh:R5-920Trx ThioredoxinGlutathione DisulfideTNF-α Tumor necrosis factor-alphabiologyLPS Lipopolysaccharide;GSSG Oxidized glutathione;MEF Mouse embryonic fibroblastsNF-kappa BGstm1 Glutathione S-transferase mu 1CatalaseEndoplasmic Reticulum StressGlutathioneLiverGSH Reduced glutathione;Catalase030220 oncology & carcinogenesisJNK c-Jun N-terminal kinaselcsh:Medicine (General)Research Papermedicine.medical_specialtyNF-E2-Related Factor 2Glutamate-Cysteine LigaseMKK MAPK kinaseAP-1 Activator protein-1IKK IƙB KinaseGene Expression Regulation EnzymologicSuperoxide dismutase03 medical and health sciencesInternal medicineGlutamate cysteine ligaseEGFR Epidermal growth factor receptormedicineAnimalsNuclear factor ƙBAnd catalaseChIP Chromatin immunoprecipitation;Protein kinase BNF-ƙB Nuclear factor kappa BSuperoxide DismutaseSuperoxide dismutase 1Superoxide dismutase 2Organic ChemistryGlutathioneASK1 Apoptosis signal-regulating kinase 1ATF2 activating transcription factor 2;030104 developmental biologyEndocrinologyEnzymeHsp Heat shock proteinlcsh:Biology (General)chemistrybiology.proteinSOD2 Mn-superoxide dismutaseMAPK mitogen activated protein kinaseNEM N-ethyl maleimide;Redox Biology
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Soluble interleukin 6 (IL-6) receptor influences the expression of the protooncogene junB and the production of fibrinogen in the HepG2 human hepatom…

1998

Abstract Interleukin 6 (IL-6) belongs to a family of cytokines using receptors sharing a common signal-transducing chain, gp130 and containing a specific ligand-binding chain (IL-6Rα). It was shown that both the membrane-bound and the soluble form (sIL-6R) of this ligand specific receptor chain occurs naturally. The soluble form of IL-6 receptor was found to be able to associate with the membrane-bound gp130 and to generate active IL-6 receptor complex capable of inducing signal transduction. This study on a human hepatoma cell line and primary rat hepatocytes examined how the effectiveness of IL-6 is modified by the presence of soluble IL-6 receptor and whether the sIL-6R in the absence of…

Receptor complexCarcinoma HepatocellularJUNBProto-Oncogene Proteins c-junImmunologyBiologyBiochemistryPolymerase Chain Reactionhemic and lymphatic diseasesGene expressionTumor Cells CulturedImmunology and AllergyAnimalsHumansRNA MessengerReceptorMolecular BiologyTranscription factorCells CulturedFibrinogenHematologyGlycoprotein 130Molecular biologyReceptors Interleukin-6RatsGene Expression RegulationLiverSolubilityInterleukin-6 receptorSignal transductionCytokine
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A homolog of the putative tumor suppressor QM in the sponge Suberites domuncula: downregulation during the transition from immortal to mortal (apopto…

1999

Abstract The activation of components of the transcription factors such as AP-1 or c-jun is essential for a physiological response of metazoan cells during aging. The activity of such proto-oncoproteins is under enzymatic control. The function of c-jun is additionally modulated by the QM protein. Here, we studied the expression of the gene, encoding the QM-like protein in the sponge Suberites domuncula . These animals contain high levels of telomerase in their somatic cells. To understand the switch from telomerase-positive immortal cells to telomerase-negative mortal cells which undergo apoptosis, the expression of the QM-like gene was measured in this system. The cDNA, termed QMSD , encod…

TelomeraseMolecular Sequence DataDown-RegulationGene ExpressionApoptosisDownregulation and upregulationComplementary DNAAnimalsHumansAmino Acid SequenceRNA MessengerCloning MolecularTranscription factorGenePhylogenyBase Sequencebiologyc-junProteinsRNA-Binding ProteinsCell BiologyGeneral Medicinebiology.organism_classificationMolecular biologyPoriferaSuberites domunculaOpen reading frameProtein BiosynthesisCarrier ProteinsDevelopmental BiologyTissue and Cell
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JNK phosphorylation relieves HDAC3-dependent suppression of the transcriptional activity of c-Jun

2003

The AP-1 transcription factor c-Jun is a prototypical nuclear effector of the JNK signal transduction pathway. The integrity of JNK phosphorylation sites at serines 63/73 and at threonines 91/93 in c-Jun is essential for signal-dependent target gene activation. We show that c-Jun phosphorylation mediates dissociation of an inhibitory complex, which is associated with histone deacetylase 3 (HDAC3). The subsequent events that ultimately cause increased mRNA synthesis are independent of c-Jun phosphorylation and its interaction with JNK. These findings provide an 'activation by de-repression' model as an explanation for the stimulatory function of JNK on c-Jun.

ThreonineTranscriptional ActivationTranscription GeneticMAP Kinase Kinase 4Proto-Oncogene Proteins c-junRecombinant Fusion ProteinsMitogen-activated protein kinase kinaseHistone DeacetylasesGeneral Biochemistry Genetics and Molecular BiologyCell LinePhosphorylation cascadeMiceSuppression GeneticGenes ReporterSerineAnimalsHumansRNA MessengerPhosphorylationMolecular BiologyTranscription factorSequence DeletionMitogen-Activated Protein Kinase KinasesGeneral Immunology and MicrobiologybiologyGeneral Neurosciencec-junJNK Mitogen-Activated Protein KinasesArticles3T3 CellsHDAC3Molecular biologyProtein Structure TertiaryMitogen-activated protein kinaseMutationMutagenesis Site-Directedbiology.proteinPhosphorylationSignal transductionProtein BindingThe EMBO Journal
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pRb suppresses camptothecin-induced apoptosis in human osteosarcoma Saos-2 cells by inhibiting c-Jun N-terminal kinase

2001

AbstractThis paper studies the cytotoxic effect induced by the topoisomerase I inhibitor camptothecin in human osteosarcoma Saos-2 cells, which lack p53 and contain a non-functional form of the product of the retinoblastoma gene, pRb. Cytotoxicity induced by camptothecin was dose- and time-dependent; the treatment with 100 nM camptothecin reduced cell viability by 50% at 32 h and by 75% at 72 h of exposure. The cytotoxic effect was caused by apoptosis, as ascertained by morphological evidence, acridine orange-ethidium bromide staining and flow cytometric analysis. Apoptosis was accompanied by both the activation of caspase-3 and the fragmentation of poly(ADP-ribose) polymerase. Treatment wi…

Time FactorsCell SurvivalProto-Oncogene Proteins c-junBlotting WesternBiophysicsApoptosisBiologyTransfectionRetinoblastoma ProteinBiochemistryStructural BiologyTumor Cells CulturedpRb JNK topoisomerase I inhibitors osteosarcomaGeneticsmedicineHumansCytotoxic T cellViability assayPhosphorylationFragmentation (cell biology)neoplasmsMolecular BiologySaos-2 cellsc-Jun N-terminal kinaseCell SizeDose-Response Relationship DrugCaspase 3Cell growthCell Cyclec-junJNK Mitogen-Activated Protein KinasesHydrogen PeroxideCell BiologyFlow CytometryGlutathioneMolecular biologyEnzyme ActivationOxidative StresspRbDNA Topoisomerases Type IApoptosisCaspasesCamptothecinMitogen-Activated Protein KinasesPoly(ADP-ribose) PolymerasesTopoisomerase I InhibitorsCamptothecinmedicine.drugFEBS Letters
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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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Transcriptional activation of apurinic/apyrimidinic endonuclease (Ape, Ref-1) by oxidative stress requires CREB.

1999

Abstract Apurinic/apyrimidinic endonuclease (APE alias Ref-1) is a multifunctional enzyme involved in DNA repair and redox regulation of transcription factors (e.g., AP-1). It also acts as a repressor of its own and other genes. Recently, it was shown that the level of APE mRNA and protein is enhanced upon treatment of cells with oxidative agents, such as hydrogen peroxide (H 2 O 2 ), which gives rise to an adaptive response of cells to oxidative stress. Induction of APE is due to APE promoter activation. To elucidate the mechanism of transcriptional activation of APE by oxidative agents, we introduced mutations into the cloned human APE promoter and checked its activity in transient transf…

Transcription GeneticDNA repairProto-Oncogene Proteins c-junvirusesCarbon-Oxygen LyasesBiophysicsRepressorContext (language use)CHO CellsCREBTransfectionBiochemistryPolymerase Chain ReactionEndonucleasestomatognathic systemCricetinaeDNA-(Apurinic or Apyrimidinic Site) LyaseAnimalsHumansAP siteBinding siteCyclic AMP Response Element-Binding ProteinPromoter Regions GeneticMolecular BiologyTranscription factorBinding SitesbiologyActivating Transcription Factor 2social sciencesCell BiologyHydrogen PeroxideOxidantsMolecular biologybody regionsOxidative Stressbiology.proteinMutagenesis Site-DirectedTranscription FactorsBiochemical and biophysical research communications
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