Search results for "Proto-oncogene"

showing 10 items of 770 documents

Ovine Carotid Artery-Derived Cells as an Optimized Supportive Cell Layer in 2-D Capillary Network Assays

2014

PLoS one 9(3), e91664 (2014). doi:10.1371/journal.pone.0091664

Vascular Endothelial Growth Factor APathologyCellBecaplerminlcsh:MedicineCardiovascularUmbilical veinUmbilical CordDrug DiscoveryMolecular Cell BiologyBiological Systems EngineeringMyocyteCardiovascular Imaginglcsh:ScienceMultidisciplinaryProto-Oncogene Proteins c-sisAnimal ModelsFlow CytometryEndothelial stem cellBevacizumabmedicine.anatomical_structureCarotid ArteriesMonoclonalMedicineImmunohistochemical AnalysisResearch ArticleBiotechnologymedicine.medical_specialtyCell typeDrugs and DevicesDrug Research and DevelopmentMyocytes Smooth MuscleImmunologyBiomedical EngineeringBioengineeringBiologyAntibodies Monoclonal HumanizedCell LineModel OrganismsVascular Biologymedicine.arterymedicineAnimalsHumansBiologySheeplcsh:REndothelial CellsFeeder CellsUmbilical arteryMolecular biologyVascular Endothelial Growth Factor Receptor-2Coculture TechniquesCapillariesCell cultureImmunologic Techniqueslcsh:QCytometry
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High levels of HIF-2α highlight an immature neural crest-like neuroblastoma cell cohort located in a perivascular niche

2007

High HIF-2alpha protein levels in the sympathetic nervous system-derived childhood tumour neuroblastoma as well as immature phenotype correlate to unfavourable outcome. Here we show that a small subset of perivascularly located, strongly HIF-2alpha-positive tumour cells (MYCN amplified) lacks expression of differentiation markers, but expresses neural crest and early sympathetic progenitor marker genes such as Notch-1, HES-1, c-Kit, dHAND, and vimentin. HIF-2alpha- and CD68-positive tumour-associated macrophages were frequently found close to the immature and HIF-2alpha-positive neuroblastoma cells and as VEGF levels are high in the perivascular niche, we hypothesize that neuroblastoma neur…

Vascular Endothelial Growth Factor APathologymedicine.medical_specialtySympathetic Nervous SystemAngiogenesisVimentinPathology and Forensic MedicineNeuroblastomaNeuroblastomaBasic Helix-Loop-Helix Transcription FactorsTumor Cells CulturedmedicineHumansMacrophageProgenitorOncogene ProteinsN-Myc Proto-Oncogene ProteinNeovascularization PathologicbiologyMacrophagesNuclear ProteinsNeural crestmedicine.diseasePhenotypeCell HypoxiaNeoplasm ProteinsNeural CrestNeoplastic Stem Cellsbiology.proteinCancer researchStem cellThe Journal of Pathology
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Depletion ofL-arginine induces autophagy as a cytoprotective response to endoplasmic reticulum stress in human T lymphocytes

2012

PMCID: PMC3494587

X-Box Binding Protein 1Proteasome Endopeptidase ComplexProgrammed cell deathXBP1CD3 ComplexMAP Kinase Signaling SystemRNA SplicingT-LymphocytesT cellDown-RegulationApoptosisRegulatory Factor X Transcription FactorsUbiquitin-Activating EnzymesProtein Serine-Threonine KinasesBiologyArginineLymphocyte ActivationAutophagy-Related Protein 7Jurkat cellsJurkat CellsEndoribonucleasesAutophagymedicineHumansMolecular BiologyCell ProliferationTOR Serine-Threonine KinasesAutophagyMembrane ProteinsCell BiologyBECN1Endoplasmic Reticulum StressG1 Phase Cell Cycle CheckpointsBasic Research Paper3. Good healthCell biologyDNA-Binding Proteinsmedicine.anatomical_structureCytoprotectionApoptosisUnfolded protein responseBeclin-1MitogensApoptosis Regulatory ProteinsLysosomesProto-Oncogene Proteins c-aktTranscription FactorsAutophagy
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Distinct 5' SCL enhancers direct transcription to developing brain, spinal cord, and endothelium: neural expression is mediated by GATA factor bindin…

1999

The SCL gene encodes a basic helix-loop-helix transcription factor with a pivotal role in the development of endothelium and of all hematopoietic lineages. SCL is also expressed in the central nervous system, although its expression pattern has not been examined in detail and its function in neural development is unknown. In this article we present the first analysis of SCL transcriptional regulation in vivo. We have identified three spatially distinct regulatory modules, each of which was both necessary and sufficient to direct reporter gene expression in vivo to three different regions within the normal SCL expression domain, namely, developing endothelium, midbrain, and hindbrain/spinal …

animal structuresEmbryo NonmammalianTranscription GeneticHindbrainMice TransgenicChick EmbryoBiologybehavioral disciplines and activities03 medical and health sciencesMice0302 clinical medicineTranscription (biology)Genes Reporterhemic and lymphatic diseasesProto-Oncogene ProteinsBasic Helix-Loop-Helix Transcription FactorsAnimalsTissue DistributionEndotheliumEnhancerMolecular BiologyTranscription factorGeneIn Situ HybridizationT-Cell Acute Lymphocytic Leukemia Protein 1Zebrafish030304 developmental biologyRegulation of gene expressionGenetics0303 health sciencesReporter geneModels GeneticfungiBrainCell BiologyZebrafish ProteinsEmbryo MammalianCell biologyDNA-Binding ProteinsLac OperonSpinal CordNeural development030217 neurology & neurosurgeryDevelopmental BiologyTranscription FactorsDevelopmental biology
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Context-dependent Pax-5 repression of a PU.1/NF-κB regulated reporter gene in B lineage cells

2001

Enhancers located in the 3' end of the locus in part regulate immunoglobulin heavy chain (IgH) gene expression. One of these enhancers, HS 1,2, is developmentally regulated by DNA binding proteins like NF-kappaB, Pax-5 and the protein complex NF-alphaP in B lineage cells. Here we report that NF-alphaP is the ets protein PU.1. A glutathione-S-transferase (GST)-pulldown assay demonstrated that PU.1 can physically interact with NF-kappaB in solution. Experiments in COS cells showed that PU.1 and NF-kappaB (p50/c-Rel) can activate transcription of an enhancer linked reporter gene. The paired domain protein Pax-5 has previously been shown to repress enhancer-dependent transcription. Additional c…

animal structuresLymphomaTranscription GeneticEnhancer RNAsBiologyDNA-binding proteinMiceSOX4Genes ReporterTranscription (biology)CricetinaeProto-Oncogene ProteinsGene expressionGeneticsAnimalsCell LineageBinding siteEnhancerCells CulturedB-LymphocytesReporter geneNF-kappa BPAX5 Transcription FactorNuclear ProteinsGeneral MedicineMolecular biologyGlobinsDNA-Binding ProteinsEnhancer Elements GeneticGene Expression RegulationCOS Cellsembryonic structuresTrans-ActivatorsTranscription FactorsGene
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Plexin-B1 activates NF-κB and IL-8 to promote a pro-angiogenic response in endothelial cells.

2011

Background The semaphorins and their receptors, the plexins, are proteins related to c-Met and the scatter factors that have been implicated in an expanding signal transduction network involving co-receptors, RhoA and Ras activation and deactivation, and phosphorylation events. Our previous work has demonstrated that Semaphorin 4D (Sema4D) acts through its receptor, Plexin-B1, on endothelial cells to promote angiogenesis in a RhoA and Akt-dependent manner. Since NF-κB has been linked to promotion of angiogenesis and can be activated by Akt in some contexts, we wanted to examine NF-κB in Sema4D treated cells to determine if there was biological significance for the pro-angiogenic phenotype o…

animal structuresRHOAProto-Oncogene Proteins c-aktAngiogenesisSignaling in cellular processesG-protein signalingCancer TreatmentSEMA4Dlcsh:MedicineSignal transductionBiology03 medical and health sciencesMolecular cell biology0302 clinical medicineSemaphorinSettore BIO/10 - BiochimicaAkt Signaling CascadeMembrane Receptor SignalingInterleukin 8lcsh:ScienceBiologyProtein kinase BGTPase signalingRas signaling030304 developmental biology0303 health sciencesMultidisciplinaryMechanisms of Signal Transductionlcsh:RSignaling Cascades3. Good healthCell biologyPlexin B1RNA interferencepro-angiogenicendothelial cellsOncology030220 oncology & carcinogenesisembryonic structuresCancer researchbiology.proteinMedicinelcsh:QAntiangiogenesis TherapyAntiapoptotic signalingSignal transductionResearch ArticlePLoS ONE
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Activation of TRK Genes in Ewingʼs Sarcoma Trk A Receptor Expression Linked to Neural Differentiation

1997

Trk receptors have been identified by immunohistochemical methods in primitive neuroectodermal tumor (PNET)/Ewing's sarcoma (ES). However, the presence of different members of the Trk family of receptors in PNET/ES has not been specified. We have examined whether Trk A, B, and C receptors are specifically expressed in ES both with and without features of neural differentiation. Ten ES tumors (five primary tumors of bone and five extraosseous tumors transplanted into nude mice) were investigated for expression of Trk receptors by immunohistochemistry and reverse transcription-polymerase chain reaction. One primary ES and the five grafted ES tumors exhibited signs of neural differentiation; t…

animal structuresReceptor expressionReceptors Nerve Growth FactorSarcoma EwingBiologyPathology and Forensic MedicineMiceProto-Oncogene ProteinsmedicineAnimalsNeuroectodermal Tumors PrimitiveReceptor trkCReceptor trkAReceptorReceptor Ciliary Neurotrophic FactorMolecular BiologyNeuronsMembrane ProteinsReceptor Protein-Tyrosine KinasesEwing's sarcomaCell DifferentiationCell BiologyProtein-Tyrosine Kinasesmedicine.diseaseMolecular biologyGene Expression Regulation Neoplasticenzymes and coenzymes (carbohydrates)nervous systemTrk receptorPrimitive neuroectodermal tumorembryonic structuresImmunohistochemistrySarcomaImmunostainingDiagnostic Molecular Pathology
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Repression of Human Papillomavirus Oncogene Expression under Hypoxia Is Mediated by PI3K/mTORC2/AKT Signaling

2019

Oncogenic HPV types are major human carcinogens. Under hypoxia, HPV-positive cancer cells can repress the viral E6/E7 oncogenes and induce a reversible growth arrest. This response could contribute to therapy resistance, immune evasion, and tumor recurrence upon reoxygenation. Here, we uncover evidence that HPV oncogene repression is mediated by hypoxia-induced activation of canonical PI3K/mTORC2/AKT signaling. AKT-dependent downregulation of E6/E7 is only observed under hypoxia and occurs, at least in part, at the transcriptional level. Quantitative proteome analyses identify additional factors as candidates to be involved in AKT-dependent E6/E7 repression and/or hypoxic PI3K/mTORC2/AKT ac…

cervical cancerAKT1Down-RegulationAKT2Mechanistic Target of Rapamycin Complex 2mTORC2MicrobiologyHost-Microbe Biology03 medical and health sciences0302 clinical medicineVirologyCell Line TumorHumansHypoxiahuman papillomavirustumor virusPsychological repressionMechanistic target of rapamycinProtein kinase BPapillomaviridaePI3K/AKT/mTOR pathway030304 developmental biology0303 health sciencesOncogenebiologyAKTOncogene Proteins ViralQR1-502030220 oncology & carcinogenesisHost-Pathogen InteractionsCancer researchbiology.proteinddc:004Phosphatidylinositol 3-KinaseProto-Oncogene Proteins c-aktResearch ArticleSignal TransductionmBio
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Design, Synthesis and Biological Evaluation of Novel Pyrazolo[1,2,4]triazolopyrimidine Derivatives as Potential Anticancer Agents

2021

Three novel pyrazolo-[4,3-e][1,2,4]triazolopyrimidine derivatives (1, 2, and 3) were designed, synthesized, and evaluated for their in vitro biological activity. All three compounds exhibited different levels of cytotoxicity against cervical and breast cancer cell lines. However, compound 1 showed the best antiproliferative activity against all tested tumor cell lines, including HCC1937 and HeLa cells, which express high levels of wild-type epidermal growth factor receptor (EGFR). Western blot analyses demonstrated that compound 1 inhibited the activation of EGFR, protein kinase B (Akt), and extracellular signal-regulated kinase (Erk)1/2 in breast and cervical cancer cells at concentrations…

cervical cancercrystal X-ray analysisPharmaceutical ScienceAntineoplastic AgentsArticleAnalytical ChemistryHeLa03 medical and health sciencesbreast cancerQD241-4410302 clinical medicineDrug DiscoveryHumansEpidermal growth factor receptorPhysical and Theoretical Chemistrypyrazolo[124]triazolopyrimidineCytotoxicityProtein Kinase InhibitorsProtein kinase BCell Proliferation030304 developmental biologyMitogen-Activated Protein Kinase 1pyrazolo[124]triazolopyrimidine; EGF-receptor inhibitor; breast cancer; cervical cancer; molecular docking; crystal X-ray analysis0303 health sciencesBinding SitesMitogen-Activated Protein Kinase 3biologyChemistryKinaseOrganic ChemistryBiological activitymolecular dockingTriazolesbiology.organism_classificationMolecular biologyIn vitroErbB ReceptorsMolecular Docking SimulationPyrimidinesChemistry (miscellaneous)Docking (molecular)030220 oncology & carcinogenesisbiology.proteinMolecular MedicineProto-Oncogene Proteins c-aktEGF-receptor inhibitorHeLa CellsProtein BindingMolecules
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Phosphorylation of mismatch repair proteins MSH2 and MSH6 affecting MutSα mismatch-binding activity

2002

Mismatch repair (MMR) is involved in the removal of mispaired bases from DNA and thus plays an important role in the maintenance of genomic stability and the prevention of mutations and cancer. Moreover, MMR triggers genotoxicity and apoptosis upon processing of DNA lesions such as O6-methylguanine. Whereas the enzymology of MMR has been elucidated in great detail, only limited data are available concerning its regulation. Here we show that the major mismatch-binding proteins MSH2 and MSH6, forming the MutSalpha complex, are phosphorylated in vitro by protein kinase C and casein kinase II, but not by protein kinase A. Phosphorylation of MSH2 and MSH6 was also found within the cell, with MSH…

congenital hereditary and neonatal diseases and abnormalitiesDNA RepairDNA repairBase Pair MismatchMacromolecular SubstancesActive Transport Cell NucleusBiologyProtein Serine-Threonine KinasesArticleProto-Oncogene ProteinsGeneticsHumansProtein phosphorylationPhosphorylationProtein kinase ACasein Kinase IIneoplasmsProtein kinase CProtein Kinase CCell Nucleusnutritional and metabolic diseasesdigestive system diseasesDNA-Binding ProteinsMutS Homolog 2 ProteinBiochemistryMSH2PhosphorylationDNA mismatch repairCasein kinase 2HeLa Cells
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