Search results for "Oncogene"

showing 10 items of 1005 documents

C-myc mRNA Expression in Epithelial Ovarian Carcinomas in Relation to Estrogen Receptor Status, Metastatic Spread, Survival Time, FIGO Stage, and His…

1998

Recently, it has been suggested that c-myc expression might correlate with estrogen receptor (ER) status and metastatic spread in ovarian cancer. In this study, expression of c-myc mRNA in 90 epithelial ovarian carcinomas was determined using the S1 nuclease protection assay. Expression of c-myc mRNA was detectable in 27 of 90 tumors. There was no significant association between c-myc mRNA expression and metastatic spread, survival time, FIGO stage, or histologic grade and type. C-myc mRNA was expressed in 45% of ER-positive tumors but only 24% of ER-negative tumors (p = 0.094; Fisher's exact test). Similarly, 44% of progesterone receptor (PR)-positive and 23% of PR-negative tumors expresse…

Pathologymedicine.medical_specialtymedicine.drug_class10050 Institute of Pharmacology and ToxicologyEstrogen receptor610 Medicine & healthOvaryBiologyPathology and Forensic MedicineMetastasisProto-Oncogene Proteins c-mycProgesterone receptormedicineHumansRNA MessengerRNA NeoplasmSurvival rateEstrogen Receptor StatusOvarian NeoplasmsCarcinomaObstetrics and Gynecology2729 Obstetrics and Gynecologymedicine.diseaseSurvival Rate2734 Pathology and Forensic Medicinemedicine.anatomical_structureReceptors EstrogenEstrogen570 Life sciences; biologyFemaleReceptors ProgesteroneOvarian cancerInternational Journal of Gynecological Pathology
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Cytotoxic and protein kinase inhibiting nakijiquinones and nakijiquinols from the sponge Dactylospongia metachromia.

2014

Chemical investigation of the sponge Dactylospongia metachromia afforded five new sesquiterpene aminoquinones (1-5), two new sesquiterpene benzoxazoles (6 and 7), the known analogue 18-hydroxy-5-epi-hyrtiophenol (8), and a known glycerolipid. The structures of all compounds were unambiguously elucidated by one- and two-dimensional NMR and by MS analyses, as well as by comparison with the literature. Compounds 1-5 showed potent cytotoxicity against the mouse lymphoma cell line L5178Y with IC50 values ranging from 1.1 to 3.7 μM. When tested in vitro for their inhibitory potential against 16 different protein kinases, compounds 5, 6, and 8 exhibited the strongest inhibitory activity against AL…

Pharmaceutical ScienceAntineoplastic AgentsMarine BiologySesquiterpeneAnalytical Chemistrychemistry.chemical_compoundInhibitory Concentration 50MiceDrug DiscoveryAnimalsHumansProtein kinase ACytotoxicityIC50Nuclear Magnetic Resonance BiomolecularProtein Kinase InhibitorsPharmacologyBenzoxazolesMolecular StructureKinaseOrganic ChemistryQuinonesIn vitroPoriferaComplementary and alternative medicineBiochemistrychemistryCell cultureMolecular MedicineDrug Screening Assays AntitumorSesquiterpenesProto-oncogene tyrosine-protein kinase SrcJournal of natural products
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Apaf-1 deficient mouse fibroblasts are resistant to MNNG and MMS-induced apoptotic death without attenuation of Bcl-2 decline.

2005

Abstract Simple alkylating agents induce cell death by activating the apoptotic pathway. In rodent fibroblasts, apoptosis triggered by DNA methylation lesions is executed via the mitochondrial damage pathway. Here, we studied cell death induced by the methylating agents methyl methanesulfonate (MMS) and N-methyl-N′-nitro-N-nitrosoguanidine (MNNG) in mouse fibroblasts wild-type (wt) and deficient for Apaf-1 (apaf-1 knockout cells). Apaf-1 is an essential component of the apoptosome complex that becomes activated upon cytochrome c release from mitochondria. We show that apaf-1 knockout cells are more resistant to the cytotoxic effect (as measured by WST assay) of methylating agents. This is d…

PharmacologyProgrammed cell deathMethylnitronitrosoguanidineDNA damageCytochrome cApoptosisBiologyToxicologyMethyl MethanesulfonateMolecular biologyMethyl methanesulfonatechemistry.chemical_compoundMiceApoptotic Protease-Activating Factor 1chemistryProto-Oncogene Proteins c-bcl-2Cell cultureApoptosisbiology.proteinCytotoxic T cellAnimalsApoptosomeCell Line TransformedToxicology and applied pharmacology
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Integrin cytoplasmic domain and pITAM compete for spleen tyrosine kinase binding

2019

ABSTRACTIn hematopoietic tissues cell-cell communication involves immunoreceptors and specialized cell adhesion receptors that both mediate intracellular signals. Spleen tyrosine kinase (Syk) is a non-receptor tyrosine kinase involved in the downstream signaling of both immunoreceptors tyrosine activation motif (ITAM) receptors and integrin family cell adhesion receptors. Both phosphorylated ITAM (pITAM) and integrins bind to the regulatory domain of Syk composed of two Src homology 2 (SH2) domains. The interaction with pITAM is mediated by binding of a specific phosphotyrosine to each of the SH2 domains, leading to conformational changes and Syk kinase activation. Integrins bind to the int…

Phosphotyrosine binding0303 health sciencesbiologyChemistryIntegrinSykchemical and pharmacologic phenomenahemic and immune systemsSH2 domainCell biology03 medical and health sciences0302 clinical medicinebiology.proteinCell adhesionTyrosine kinase030217 neurology & neurosurgery030304 developmental biologyProto-oncogene tyrosine-protein kinase SrcIntegrin binding
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The PVT-1 oncogene is a Myc protein target that is overexpressed in transformed cells

2007

The human PVT-1 gene is located on chromosome 8 telomeric to the c-Myc gene and it is frequently involved in the translocations occurring in variant Burkitt's lymphomas and murine plasmacytomas. It has been proposed that PVT-1 regulates c-Myc gene transcription over a long distance. To get new insights into the functional relationships between the two genes, we have investigated PVT-1 and c-Myc expression in normal human tissues and in transformed cells. Our findings indicate that PVT-1 expression is restricted to a relative low number of normal tissues compared to the wide distribution of c-Myc mRNA, whereas the gene is highly expressed in many transformed cell types including neuroblastom…

PhysiologyClinical BiochemistryBiologyCell LineProto-Oncogene Proteins c-mycGenes ReporterNeoplasmsC-MYCAnimalsHumansTissue DistributionPromoter Regions GeneticGeneGENE-EXPRESSIONRegulation of gene expressionReporter geneOncogeneProteinsCell BiologyTransfectionMolecular biologyPVT1Cell Transformation NeoplasticGene Expression RegulationPVT-1Cell cultureRNA Long NoncodingChromatin immunoprecipitationJournal of Cellular Physiology
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Gata4 Blocks Somatic Cell Reprogramming By Directly Repressing Nanog

2012

Abstract Somatic cells can be reprogrammed to induced pluripotent stem (iPS) cells by ectopic expression of the four factors Oct4, Klf4, Sox2, and Myc. Here, we investigated the role of Gata4 in the reprogramming process and present evidence for a negative role of this family of transcription factors in the induction of pluripotency. Coexpression of Gata4 with Oct4, Klf4, and Sox2 with or without Myc in mouse embryonic fibroblasts greatly impaired reprogramming and endogenous Nanog expression. The lack of Nanog upregulation was associated with a blockade in the transition from the initiation phase of reprogramming to the full pluripotent state characteristic of iPS cells. Addition of Nanog …

Pluripotent Stem CellsTranscriptional ActivationHomeobox protein NANOGChromatin ImmunoprecipitationTranscription GeneticRex1Kruppel-Like Transcription FactorsDown-RegulationElectrophoretic Mobility Shift AssayBiologyCell LineProto-Oncogene Proteins c-mycKruppel-Like Factor 4MiceSOX2AnimalsRNA MessengerRNA Small InterferingInduced pluripotent stem cellEmbryonic Stem Cellsreproductive and urinary physiologyHomeodomain ProteinsSOXB1 Transcription FactorsNanog Homeobox ProteinCell DifferentiationNanog Homeobox ProteinCell BiologyCellular ReprogrammingEmbryonic stem cellGATA4 Transcription FactorKLF4embryonic structuresHepatocyte Nuclear Factor 3-betaCancer researchMolecular MedicineRNA Interferencebiological phenomena cell phenomena and immunityOctamer Transcription Factor-3ReprogrammingDevelopmental BiologyStem Cells
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Effect of flupirtine on Bcl-2 and glutathione level in neuronal cells treated in vitro with the prion protein fragment (PrP106-126).

1997

Flupirtine, trade name Katadolon, is a centrally acting nonopioid analgesic that has recently been found to display cytoprotective activity in vitro and in vivo on neurons induced to undergo apoptosis. This report shows that the PrP106-126 fragment of the prion protein, which is the likely etiological agent for a series of encephalopathies, is toxic to cortical neurons in vitro. Simultaneously, PrP106-126 influences the molecular GSH content and the bcl-2 expression in neurons. Significant toxicity (32% reduction in cell viability) was observed at a concentration of 50 microM of the peptide after 9 days of incubation, while at higher concentrations toxicity increased to 70%. Neurotoxicity w…

PrionsMolecular Sequence DataAminopyridinesApoptosisPharmacologyBiologychemistry.chemical_compoundDevelopmental NeurosciencemedicineAnimalsAmino Acid SequenceRats WistarCytotoxicityCells CulturedNeuronsNeurotoxicityGlutathioneAnalgesics Non-Narcoticmedicine.diseaseGlutathioneIn vitroPeptide FragmentsGenes bcl-2RatsOxidative StressNeuroprotective AgentsNeurologychemistryGene Expression RegulationProto-Oncogene Proteins c-bcl-2ApoptosisCell cultureImmunologyToxicityFlupirtineOxidation-Reductionmedicine.drugExperimental neurology
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Met inhibition revokes IFNγ-induction of PD-1 ligands in MET-amplified tumours

2019

BACKGROUND: Interferon-induced expression of programmed cell death ligands (PD-L1/PD-L2) may sustain tumour immuneevasion. Patients featuring MET amplification, a genetic lesion driving transformation, may benefit from anti-MET treatment. We explored if MET-targeted therapy interferes with Interferon-gamma modulation of PD-L1/PD-L2 in MET-amplified tumours.METHODS: PD-L1/PD-L2 expression and signalling pathways downstream of MET or Interferon-gamma were analysed in MET-amplified tumour cell lines and in patient-derived tumour organoids, in basal condition, upon Interferon-gamma stimulation, and after anti-MET therapy.RESULTS: PD-L1 and PD-L2 were upregulated in MET-amplified tumour cells up…

Programmed cell deathCancer ResearchCancer immunotherapyMET-amplified tumoursB7-H1 AntigenArticleInterferon-gammaTargeted therapiesDownregulation and upregulationInterferonCell Line TumorNeoplasmsHumansMedicineMet inhibitionMolecular Targeted TherapySTAT1Kinase activityReceptorProtein Kinase InhibitorsJanus KinasesReceptors InterferonOncogenebiologyPD-1 ligandsbusiness.industryLiver NeoplasmsOncogenesProto-Oncogene Proteins c-metProgrammed Cell Death 1 Ligand 2 ProteinOrganoidsSTAT1 Transcription FactorOncologybiology.proteinCancer researchOncology; Cancer Research; Met inhibition; IFNγ-induction;PD-1 ligands; MET-amplified tumoursTumor EscapeSignal transductionColorectal NeoplasmsbusinessIFNγ-inductionSignal Transductionmedicine.drug
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The abrogation of the HOXB7/PBX2 complex induces apoptosis in melanoma through the miR-221&222-c-FOS pathway.

2013

Cutaneous melanoma is the fastest increasing cancer worldwide. Although several molecular abnormalities have been associated with melanoma progression, the underlying mechanisms are still largely unknown and few targeted therapies are under evaluation. Here we show that the HOXB7/PBX2 dimer acts as a positive transcriptional regulator of the oncogenic microRNA-221 and -222. In addition, demonstrating c-FOS as a direct target of miR-221&222, we identify a HOXB7/PBX2→miR-221&222 →c-FOS regulatory link, whereby the abrogation of functional HOXB7/PBX2 dimers leads to reduced miR-221&222 transcription and elevated c-FOS expression with consequent cell death. Taking advantage of the treatment wit…

Programmed cell deathCancer ResearchSkin NeoplasmsTranscription GeneticApoptosisSmall Interferingc-FosPolymerase Chain ReactionCell LineGeneticCell Line TumorProto-Oncogene ProteinsHOXB7/PBX2 complexmicroRNATranscriptional regulationmedicinemelanomaHumansPBXRNA Small InterferingDNA PrimersHomeodomain Proteinsc-FOS pathwayTumorbiologymicroRNABase SequenceMelanomaHOXB7; HXR9 peptide; melanoma; microRNA; PBX; Apoptosis; Base Sequence; Cell Line Tumor; DNA Primers; Dimerization; Homeodomain Proteins; Humans; Melanoma; MicroRNAs; Polymerase Chain Reaction; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-fos; RNA Small Interfering; Skin Neoplasms; Transcription Genetic; Cancer Research; Oncologymedicine.diseaseMicroRNAsHXR9 peptideOncologyApoptosisCell cultureCutaneous melanomaHOXB7/PBX2 complex ;melanoma ;c-FOS pathwayCancer researchbiology.proteinHOXB7RNATranscriptionDimerizationProto-Oncogene Proteins c-fosCancer Cell Biology
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Chemically modified tetracyclines induce cytotoxic effects against J774 tumour cell line by activating the apoptotic pathway

2003

Here, we have studied the effects of chemically modified tetracyclines (CMTs) on apoptosis both at the level of the cytoplasmic proteolytic caspase cascade, and on Bcl-2 and c-myc mRNA expression in the J774 macrophage cell line. The results indicate that CMTs induce morphological changes consistent with apoptotic events, as clearly demonstrated both by the acridine orange and ethidium bromide staining, and by TUNEL and fragmentation ELISA assays. Furthermore, the analysis of the cell cycle by flow cytometry shows an evident apoptotic sub-G0G1 peak, without important modifications in the cell cycle distribution. CMTs induce programmed cell death (PCD) in a dose-dependent manner and CMT-8 is…

Programmed cell deathCell SurvivalImmunologyApoptosisProto-Oncogene Proteins c-mycMicechemistry.chemical_compoundTumor Cells CulturedAnimalsImmunology and AllergyRNA MessengerFragmentation (cell biology)CaspasePharmacologyTUNEL assayDose-Response Relationship DrugbiologyAcridine orangeTetracyclineCell cycleMolecular biologyGene Expression Regulation NeoplasticProto-Oncogene Proteins c-bcl-2chemistryTetracyclinesApoptosisCaspasesMacrophages Peritonealbiology.proteinFemaleSignal transductionInternational Immunopharmacology
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