Search results for "Proto-Oncogene Proteins c-jun"

showing 10 items of 22 documents

Activation of c-Jun N-terminal kinase 1 by UV irradiation is inhibited by wortmannin without affecting c-iun expression.

1999

Activation of c-Jun N-terminal kinases (JNKs)/stress-activated protein kinases is an early response of cells upon exposure to DNA-damaging agents. JNK-mediated phosphorylation of c-Jun is currently understood to stimulate the transactivating potency of AP-1 (e.g., c-Jun/c-Fos; c-Jun/ATF-2), thereby increasing the expression of AP-1 target genes. Here we show that stimulation of JNK1 activity is not a general early response of cells exposed to genotoxic agents. Treatment of NIH 3T3 cells with UV light (UV-C) as well as with methyl methanesulfonate (MMS) caused activation of JNK1 and an increase in c-Jun protein and AP-1 binding activity, whereas antineoplastic drugs such as mafosfamide, mito…

Alkylating AgentsProto-Oncogene Proteins c-junUltraviolet RaysStimulationBiologyenvironment and public healthWortmanninTransactivationchemistry.chemical_compoundMiceAnimalsPhosphatidylinositolCollagenasesProtein kinase AMolecular BiologyCell Growth and DevelopmentMitogen-Activated Protein Kinase 1Kinasec-junJNK Mitogen-Activated Protein KinasesCell Biology3T3 CellsMethyl MethanesulfonateMolecular biologyAndrostadienesEnzyme ActivationGene Expression Regulation NeoplasticTranscription Factor AP-1chemistryCalcium-Calmodulin-Dependent Protein KinasesPhosphorylationMitogen-Activated Protein KinasesWortmanninMolecular and cellular biology
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TCDD deregulates contact inhibition in rat liver oval cells via Ah receptor, JunD and cyclin A.

2007

The aryl hydrocarbon receptor (AhR) is a transcription factor involved in physiological processes, but also mediates most, if not all, toxic responses to 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). Activation of the AhR by TCDD leads to its dimerization with aryl hydrocarbon nuclear translocator (ARNT) and transcriptional activation of several phase I and II metabolizing enzymes. However, this classical signalling pathway so far failed to explain the pleiotropic hazardous effects of TCDD, such as developmental toxicity and tumour promotion. Thus, there is an urgent need to define genetic programmes orchestrated by AhR to unravel its role in physiology and toxicology. Here we show that TCDD …

Cancer ResearchAryl hydrocarbon receptor nuclear translocatorPolychlorinated Dibenzodioxinscyclin AProto-Oncogene Proteins c-junCyclin DCyclin Acell cycle controlCyclin ATetrachlorodibenzodioxinModels BiologicalDownregulation and upregulationGeneticsAnimalsRNA Small InterferingMolecular BiologyTranscription factorAryl hydrocarbon receptorCells CulturedbiologyContact InhibitionContact inhibitionCell cycleAryl hydrocarbon receptorRatsAdult Stem CellsLiverReceptors Aryl Hydrocarbonliver oval cellsbiology.proteinCancer researchJunDOncogene
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Role of glutathione in the induction of apoptosis and c-fos and c-jun mRNAs by oxidative stress in tumor cells.

2003

We have used two tumor cell clones (B9 and G2), derived from the methylcholanthrene-induced murine fibrosarcoma GR9 and normal BALB/c3T3 fibroblasts, to study the ability of t-BOOH derived reactive oxygen radicals to induce oxidative stress, apoptosis and c-fos and c-jun mRNA transcription. These clones differ in terms of their major histocompatibility complex (MHC) (H-2) class I genes expression, their tumor induction and metastatic potential and their reduced glutathione (GSH) levels. Incubation of both cell clones in the presence of t-BOOH results in the increase of 8-oxo-2'-deoxyguanosine (8-oxo-dG) and malondialdehyde and the decrease of GSH. The xenobiotic also induces the transcripti…

Cancer ResearchBALB 3T3 CellsTranscription GeneticProto-Oncogene Proteins c-junFibrosarcomaCellApoptosisBiologymedicine.disease_causeAntioxidantsSuperoxide dismutasechemistry.chemical_compoundMicetert-ButylhydroperoxideCell CloneMalondialdehydemedicineTumor Cells CulturedAnimalsRNA MessengerDNA Primerschemistry.chemical_classificationReactive oxygen speciesReverse Transcriptase Polymerase Chain Reactionc-junHistocompatibility Antigens Class IDeoxyguanosineGlutathioneFibroblastsMolecular biologyGlutathioneOxidative Stressmedicine.anatomical_structureOncologychemistryGene Expression RegulationApoptosis8-Hydroxy-2'-Deoxyguanosinebiology.proteinReactive Oxygen SpeciesProto-Oncogene Proteins c-fosOxidative stressCancer letters
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Phosphorylation of the DNA repair protein APE/REF-1 by CKII affects redox regulation of AP-1

1999

The DNA repair protein apurinic endonuclease (APE/Ref-1) exerts several physiological functions such as cleavage of apurinic/apyrimidinic sites and redox regulation of the transcription factor AP-1, whose activation is part of the cellular response to DNA damaging treatments. Here we demonstrate that APE/Ref-1 is phosphorylated by casein kinase II (CKII). This was shown for both the recombinant APE/Ref-1 protein (Km=0.55 mM) and for APE/Ref-1 expressed in COS cells. Phosphorylation of APE/Ref-1 did not alter the repair activity of the enzyme, whereas it stimulated its redox capability towards AP-1, thus promoting DNA binding activity of AP-1. Inhibition of CKII mediated phosphorylation of A…

Cancer ResearchDNA RepairProto-Oncogene Proteins c-junDNA repairDNA damageCarbon-Oxygen LyasesCHO CellsProtein Serine-Threonine KinasesBiologyTransfectionSubstrate SpecificityCricetinaeDNA Repair ProteinDNA-(Apurinic or Apyrimidinic Site) LyaseGeneticsAnimalsHumansAP sitePhosphorylationCasein Kinase IIProtein kinase AMolecular BiologyMethyl MethanesulfonateCyclic AMP-Dependent Protein KinasesMolecular biologyDNA-(apurinic or apyrimidinic site) lyaseTranscription Factor AP-1COS CellsPhosphorylationCasein kinase 2Oxidation-ReductionDNA DamageHeLa CellsMutagensOncogene
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JNK and AP-1 mediate apoptosis induced by bortezomib in HepG2 cells via FasL/caspase-8 and mitochondria-dependent pathways

2006

The proteasome inhibitor bortezomib is an efficacious apoptotic agent in many tumor cells. This paper shows that bortezomib induced apoptosis in human hepatoma HepG2 cells associated with many modifications in the expression of survival or death factors. Although bortezomib increased the level of the protective factors HSP70 and HSP27, the effects of the drug that favour cell death were predominant. These events include accumulation of c-Jun, phospho-c-Jun and p53; increase in FasL level with activation of caspase-8; changes related to members of Bcl-2 family with increase in the level of pro-apoptotic members and decrease in that of anti-apoptotic ones; dissipation of mitochondrial potenti…

Cancer ResearchProgrammed cell deathFas Ligand ProteinProto-Oncogene Proteins c-junClinical BiochemistryPharmaceutical ScienceAntineoplastic AgentsApoptosisCaspase 8Cell LineBortezomibHsp27Cell Line TumormedicineHumansMitogen-Activated Protein Kinase 8Protease InhibitorsAP1Heat-Shock ProteinsPharmacologyCaspase 8Membrane GlycoproteinsbiologyJNK.Bortezomibc-JunLiver NeoplasmsBiochemistry (medical)c-junhepatomaCell BiologyapoptosiBoronic AcidsMitochondriaCell biologyTranscription Factor AP-1AP-1 transcription factorLiverProto-Oncogene Proteins c-bcl-2ApoptosisCaspasesPyrazinesTumor Necrosis Factorsbiology.proteinCancer researchProteasome inhibitorSignal Transductionmedicine.drugApoptosis
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In vivo studies of altered expression patterns of p53 and proliferative control genes in chronic vitamin A deficiency and hypervitaminosis

2003

Several clinical trials have revealed that individuals who were given beta-carotene and vitamin A did not have a reduced risk of cancer compared to those given placebo; rather, vitamin A could actually have caused an adverse effect in the lungs of smokers [Omenn, G.S., Goodman, G.E., Thornquist, M.D., Balmes, J., Cullen, M.R., Glass, A., Keogh, J.P., Meyskens, F.L., Valanis, B., Williams, J.H., Barnhart, S. & Hammar, S. N. Engl. J. Med (1996) 334, 1150-1155; Hennekens, C.H., Buring, J.E., Manson, J.E., Stampfer, M., Rosner, B., Cook, N.R., Belanger, C., LaMotte, F., Gaziano, J.M., Ridker, P.M., Willet, W. & Peto, R. (1996) N. Engl. J. Med. 334, 1145-1149]. Using differential display techniq…

Cyclin-Dependent Kinase Inhibitor p21VitaminRetinyl Estersmedicine.medical_specialtyMacromolecular SubstancesProto-Oncogene Proteins c-junReceptors Retinoic AcidBlotting WesternRetinoic acidBiologymedicine.disease_causeBiochemistrychemistry.chemical_compoundIn vivoCyclinsInternal medicinemedicineAnimalsHypervitaminosis ARNA MessengerRats WistarVitamin AReceptorLungDifferential displayReverse Transcriptase Polymerase Chain ReactionVitamin A DeficiencyGene Expression ProfilingDNAmedicine.diseaseHypervitaminosisPrecipitin TestsRatsVitamin A deficiencyEndocrinologyGene Expression RegulationLiverchemistryChronic DiseaseImmunologyDiterpenesTumor Suppressor Protein p53CarcinogenesisCell DivisionEuropean Journal of Biochemistry
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Selective uptake and degradation of c-Fos and v-Fos by rat liver lysosomes

1996

AbstractThe transcription factor c-Fos is a short-lived protein and calpains and ubiquitin-dependent systems have been proposed to be involved in its degradation. In this report, we consider a lysosomal degradation pathway for c-Fos. Using a cell-free assay, we have found that freshly isolated lysosomes can take up and degrade c-Fos with high efficiency. v-Fos, the oncogenic counterpart of c-Fos, can also be taken up by lysosomes, yet the amount of incorporated protein is much lower. c-Fos uptake is independent of its phosphorylation state but it appears to be regulated by dimerization with differentially phosphorylated forms of c-Jun, while v-Fos escapes this regulation. Moreover, we show …

LeupeptinsProto-Oncogene Proteins c-junBiophysicsProtein degradationProtein degradationTransfectionBiochemistryc-FosCell Linechemistry.chemical_compoundStructural BiologyLysosomeGeneticsmedicineAnimalsHumansProtease InhibitorsTrypsinPhosphorylationMolecular BiologyTranscription factorc-FosCell-Free Systembiologyc-junLeupeptinc-Junv-FosCalpainCell BiologyLysosomeRecombinant ProteinsRatsKineticsOncogene Proteins v-fosmedicine.anatomical_structureLiverchemistryBiochemistrybiology.proteinPhosphorylationElectrophoresis Polyacrylamide GelLysosomesProto-Oncogene Proteins c-fosHeLa CellsFEBS Letters
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Resveratrol decreases the levels of miR-155 by upregulating miR-663, a microRNA targeting JunB and JunD.

2010

An inflammatory component is present in the microenvironment of most neoplastic tissues, including those not causally related to an obvious inflammatory process. Several microRNAs, and especially miR-155, play an essential role in both the innate and adaptative immune response. Resveratrol (trans-3,4#,5-trihydroxystilbene) is a natural antioxidant with anti-inflammatory properties that is currently at the stage of preclinical studies for human cancer prevention. Here, we establish that, in human THP-1 monocytic cells as well as in human blood monocytes, resveratrol upregulates miR- 663, a microRNA potentially targeting multiple genes implicated in the immune response. In THP-1 cells, miR-66…

LipopolysaccharidesCancer ResearchJUNBProto-Oncogene Proteins c-junBlotting WesternResveratrolBiologyMonocytesmiR-15503 medical and health scienceschemistry.chemical_compound0302 clinical medicineImmune systemDownregulation and upregulationRNA interferencemicroRNAStilbenesBiomarkers TumorHumans[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyRNA MessengerLuciferases[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyCells Cultured030304 developmental biologyOligonucleotide Array Sequence AnalysisCancer Biology0303 health sciencesInnate immune systemmicroRNAReverse Transcriptase Polymerase Chain ReactionGene Expression ProfilingmicroRNA; ResveratrolGeneral MedicineAntineoplastic Agents Phytogenic3. Good healthUp-RegulationTranscription Factor AP-1MicroRNAschemistryGene Expression RegulationResveratrol030220 oncology & carcinogenesisCancer research
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TCDD induces c-jun expression via a novel Ah (dioxin) receptor-mediated p38–MAPK-dependent pathway

2005

The aryl hydrocarbon receptor (AhR) has a fundamental role during postnatal liver development and is essential for mediating dioxin toxicity. However, the genetic programs mediating, both, the toxic and physiological effects downstream of the transcription factor AhR are in major parts unknown. We have identified the proto-oncogene c-jun as a novel target gene of AhR. Induction of c-jun depends on activation of p38-mitogen-activated protein kinase (MAPK) by an AhR-dependent mechanism. None of the kinases that are known to phosphorylate p38-MAPK is activated by AhR. Neither the dephosphorylation rate of p38-MAPK is reduced. Furthermore, increased p38-MAPK phosphorylation in response to dioxi…

MAPK/ERK pathwayCancer ResearchPolychlorinated DibenzodioxinsProto-Oncogene Proteins c-junp38 mitogen-activated protein kinasesBiologyTransfectionProto-Oncogene Masp38 Mitogen-Activated Protein KinasesGenes ReporterCell Line TumorGeneticsHumansRNA NeoplasmRNA Small InterferingProtein kinase AMolecular BiologyTranscription factorDNA PrimersBase SequenceKinasec-junrespiratory systemAryl hydrocarbon receptorrespiratory tract diseasesGene Expression Regulation NeoplasticReceptors Aryl HydrocarbonMitogen-activated protein kinasebiology.proteinCancer researchOncogene
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Activation of Cardiac c-Jun NH 2 -Terminal Kinases and p38-Mitogen–Activated Protein Kinases With Abrupt Changes in Hemodynamic Load

2001

Abstract —The role of mitogen-activated protein kinase (MAPK) pathways as signal transduction intermediates of hemodynamic stress leading to cardiac hypertrophy in the adult heart is not fully established. In a rat model of pressure-overload hypertrophy, we examined whether activation of MAPK pathways, namely, the extracellular signal–regulated protein kinase (ERK), c-Jun NH 2 -terminal kinase (JNK), and the p38-MAPK pathways, occurs during rapid changes in hemodynamic load in vivo. A slight activation of ERK2 and marked increases in JNK1 and p38-MAPK activities were observed 30 minutes after aortic banding. The increase in p38-MAPK activity was accompanied by an increase in the phosphoryl…

MAPK/ERK pathwaymedicine.medical_specialtyProto-Oncogene Proteins c-junp38 mitogen-activated protein kinasesp38 Mitogen-Activated Protein KinasesVentricular Function LeftStress PhysiologicalInternal medicineInternal MedicinemedicineAnimalsASK1PhosphorylationRats WistarCyclic AMP Response Element-Binding ProteinProtein kinase AProtein kinase CMAPK14Activating Transcription Factor 2biologyKinaseMyocardiumJNK Mitogen-Activated Protein KinasesRatsCell biologyEnzyme ActivationTranscription Factor AP-1Disease Models AnimalEndocrinologyMitogen-activated protein kinasebiology.proteinFemaleMitogen-Activated Protein KinasesTranscription FactorsHypertension
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