Search results for "TRANSCRIPTION FACTORS"

showing 10 items of 848 documents

NFAT transcription factors control HIV-1 expression through a binding site downstream of TAR region.

2004

NFAT factors control HIV-1 transcription. We show here that, in addition to binding to two NF-kappaB/NFAT sites within the U3 HIV LTR, NFATc1 and NFATc2 bind to an NFAT site within the LTR's U5 region. Mutations in this site which abolish NFAT binding reduce the ability of NFATs to transactivate LTR-mediated transcription. Mutations in all three NFAT sites strongly interfered with LTR induction, but affected moderately the stimulatory effect of Tat.

Transcription GeneticvirusesImmunologyTransfectionJurkat cellsJurkat CellsTranscription (biology)Immunology and AllergyHumansNuclear proteinBinding siteTranscription factorHIV Long Terminal RepeatBinding SitesNFATC Transcription FactorsChemistryNuclear ProteinsNFATHematologyU937 CellsNFATC Transcription FactorsMolecular biologyDNA-Binding Proteinscardiovascular systemHIV-1HIV Long Terminal RepeatTranscription FactorsImmunobiology
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Recruitment of HIF-1α and HIF-2α to common target genes is differentially regulated in neuroblastoma: HIF-2α promotes an aggressive phenotype

2006

In neuroblastoma specimens, HIF-2alpha but not HIF-1alpha is strongly expressed in well-vascularized areas. In vitro, HIF-2alpha protein was stabilized at 5% O2 (resembling end capillary oxygen conditions) and, in contrast to the low HIF-1alpha activity at this oxygen level, actively transcribed genes like VEGF. Under hypoxia (1% O2), HIF-1alpha was transiently stabilized and primarily mediated acute responses, whereas HIF-2alpha protein gradually accumulated and governed prolonged hypoxic gene activation. Knockdown of HIF-2alpha reduced growth of neuroblastoma tumors in athymic mice. Furthermore, high HIF-2alpha protein levels were correlated with advanced clinical stage and high VEGF expr…

Transcriptional ActivationCancer ResearchProcollagen-Proline DioxygenaseAggressive phenotypeCELLCYCLEBiologyMiceNeuroblastomaNeuroblastomaBasic Helix-Loop-Helix Transcription FactorsTumor Cells CulturedmedicineAnimalsHumansRNA MessengerChildHypoxiaGeneOligonucleotide Array Sequence AnalysisRegulation of gene expressionGene knockdownGene Expression ProfilingCell BiologyCell cycleHypoxia (medical)Hypoxia-Inducible Factor 1 alpha Subunitmedicine.diseaseIn vitroGene Expression Regulation NeoplasticOxygenPhenotypeOncologyImmunologyCancer researchFemalemedicine.symptomNeoplasm TransplantationCancer Cell
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Role of SIRT1 and FOXO factors in eNOS transcriptional activation by resveratrol.

2013

Many of the cardiovascular protective effects of resveratrol are attributable to an enhanced production of nitric oxide (NO) by the endothelial NO synthase (eNOS). Resveratrol has been shown to enhance eNOS gene expression as well as eNOS enzymatic activity. The aim of the present study was to analyze the molecular mechanisms of eNOS transcriptional activation by resveratrol. Treatment of human EA.hy 926 endothelial cells with resveratrol led to a concentration-dependent upregulation of eNOS expression. In luciferase reporter gene assay, resveratrol enhanced the activity of human eNOS promoter fragments (3500, 1600, 633 and 263bp in length, respectively), indicating that the proximal promot…

Transcriptional ActivationCancer Researchendocrine system diseasesNitric Oxide Synthase Type IIIPhysiologyClinical BiochemistryFOXO1ResveratrolBiochemistryCell LineTransactivationchemistry.chemical_compoundSirtuin 1EnosStilbenesHumansRNA Small Interferingskin and connective tissue diseasesPromoter Regions GeneticTranscription factorGene knockdownAnalysis of VariancebiologySirtuin 1Chemistryorganic chemicalsfood and beveragesForkhead Transcription Factorsbiology.organism_classificationMolecular biologyUp-RegulationNitric oxide synthaseResveratrolGene Knockdown Techniquesbiology.proteinhormones hormone substitutes and hormone antagonistsNitric oxide : biology and chemistry
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Mechanism of leptin expression in breast cancer cells: role of hypoxia-inducible factor-1α

2007

We reported previously that the obesity hormone leptin is overexpressed in breast cancer biopsies. Here, we investigated molecular mechanisms involved in this process, focusing on conditions that are associated with obesity, that is, hyperinsulinemia and induction of hypoxia. By using quantitative real-time PCR, immunofluorescent detection of proteins and enzyme-linked immunosorbent assays, we found that treatment of MCF-7 breast cancer cells with high doses of insulin or the hypoxia-mimetic agent CoCl2, or culturing the cells under hypoxic conditions significantly increased the expression of leptin mRNA and protein. Notably, the greatest leptin mRNA and protein expression were observed und…

Transcriptional ActivationCancer Researchmedicine.medical_specialtyActive Transport Cell NucleusBreast NeoplasmsBiologymedicine.disease_causeleptinbreast cancerInternal medicineCoactivatorGene expressionTumor Cells CulturedGeneticsmedicineHumansInsulinHIFp300-CBP Transcription FactorsPromoter Regions GeneticMolecular BiologyCell NucleusRegulation of gene expressionBinding SitesLeptin receptorLeptinPromoterCobaltHypoxia-Inducible Factor 1 alpha SubunitCell HypoxiaGene Expression Regulation NeoplasticEndocrinologyhyperinsulinemiaCarcinogenesisChromatin immunoprecipitationhormones hormone substitutes and hormone antagonistsProtein BindingOncogene
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Melatonin induces transcriptional regulation of Bim by FoxO3a in HepG2 cells

2012

Background: Melatonin induces apoptosis in many different cancer cell lines, including hepatocellular carcinoma cells. However, the responsible pathways have not been clearly elucidated. A member of the forkhead transcription factors' family, FoxO3a, has been implicated in the expression of the proapoptotic protein Bim (a Bcl-2-interacting mediator of cell death). In this study, we used human HepG2 liver cancer cells as an in vitro model to investigate whether melatonin treatment induces Bim through regulation by the transcription factor FoxO3a. Methods: Cytotoxicity of melatonin was compared in HepG2 hepatoblastoma cells and primary human hepatocytes. Proapoptotic Bim expression was analys…

Transcriptional ActivationCancer Researchmedicine.medical_specialtyProgrammed cell deathSmall interfering RNACarcinoma HepatocellularTranscription GeneticApoptosisFoxO3amelatoninBiologyGenetics & GenomicsMelatoninDownregulation and upregulationCell Line TumorProto-Oncogene ProteinsInternal medicinemedicineTranscriptional regulationHumansGene silencingBimPhosphorylationRNA Small InterferingPromoter Regions GeneticTranscription factorBinding SitesBcl-2-Like Protein 11Forkhead Box Protein O3Membrane ProteinsForkhead Transcription FactorsHep G2 Cellshepatocellular carcinomaCell biologyEndocrinologyOncologyHepatocytesRNA Interferencebiological phenomena cell phenomena and immunityApoptosis Regulatory ProteinsChromatin immunoprecipitationProtein Bindingmedicine.drugBritish Journal of Cancer
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Transcription factors involved in the expression of SLC28 genes in human liver parenchymal cells.

2007

Human nucleoside transporters are encoded by SLC28 (hCNTs) and SLC29 (hENTs) genes. These proteins mediate the uptake of anticancer and some antiviral drugs and are also suitable candidates to facilitate nucleoside-derived drug uptake into hepatocytes for detoxification. Despite the putative relevance of these genes in liver physiology, the human SLC28 and SLC29 expression pattern is not known and suitable cell models are not available. These issues have been addressed by examining NT expression in human liver and primary cultures of human hepatocytes. Moreover, the effect of specific liver enriched transcription factors (LETFs) in hCNTs expression has been analyzed. Human hepatocytes expre…

Transcriptional ActivationCellBiophysicsGene ExpressionMembrane Transport ProteinsEquilibrative nucleoside transporterTransporterCell BiologyBiologyBiochemistryPhenotypeCell biologymedicine.anatomical_structureGene expressionmedicineHepatocytesHumansMolecular BiologyGeneNucleosideTranscription factorCells CulturedTranscription FactorsBiochemical and biophysical research communications
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Peroxisome-proliferator-activated receptors as physiological sensors of fatty acid metabolism: molecular regulation in peroxisomes

2001

The enzymes required for the beta-oxidation of fatty acyl-CoA are present in peroxisomes and mitochondria. Administration of hypolipidaemic compounds such as clofibrate to rodents leads to an increase in the volume and density of peroxisomes in liver cells. These proliferators also induce simultaneously the expression of genes encoding acyl-CoA oxidase, enoyl-CoA hydratase-hydroxyacyl-CoA dehydrogenase (multifunctional enzyme) and thiolase (3-ketoacyl-CoA thiolase). All these enzymes are responsible for long-chain and very-long-chain fatty acid beta-oxidation in peroxisomes. Similar results were observed when rat hepatocytes, or liver-derived cell lines, were cultured with a peroxisome prol…

Transcriptional ActivationGuinea PigsResponse elementReceptors Cytoplasmic and NuclearBiologyBiochemistryGene Expression Regulation EnzymologicMicechemistry.chemical_compoundPeroxisomesAnimalsAcetyl-CoA C-AcetyltransferasePhosphorylationTranscription factorProtein Kinase Cchemistry.chemical_classificationFatty acid metabolismThiolaseFatty AcidsFatty acidPeroxisomeRatsLiverchemistryBiochemistryAcetyl-CoA C-acetyltransferasePeroxisome proliferator-activated receptor alphaSignal TransductionTranscription FactorsBiochemical Society Transactions
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Transcriptional activation of the small GTPase gene rhoB by genotoxic stress is regulated via a CCAAT element

2001

The gene encoding the Ras-related GTPase RhoB-specific is immediate-early inducible by genotoxic treatments. Regulation of transcriptional activation of rhoB is still unclear. Here we show that cells lacking either p53 or c-Fos are not different from wild-type cells with respect to the level of rhoB induction upon UV irradiation, indicating that these transcription factors are not crucial for stimulation of rhoB mRNA expression. Extracts from UV-irradiated and non-irradiated cells revealed similar DNA-binding activities to a 0.17 kb rhoB promoter fragment harboring the functional element(s) necessary for stimulation of rhoB by UV light. By means of immunoprecipitation we found that an ATF-2…

Transcriptional ActivationImmunoprecipitationUltraviolet RaysRHOBMolecular Sequence DataCAAT boxOligonucleotidesBiologyResponse ElementsArticlechemistry.chemical_compoundMiceRhoB GTP-Binding ProteinGeneticsAnimalsSmall GTPaseRNA MessengerPromoter Regions GeneticrhoB GTP-Binding ProteinTranscription factorBinding SitesCcaat-enhancer-binding proteinsBase Sequence3T3 CellsDNAMolecular biologyMethyl methanesulfonatechemistryCCAAT-Binding FactorMutationCCAAT-Enhancer-Binding ProteinsProtein BindingTranscription Factors
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Peroxisome proliferators and peroxisome proliferator activated receptors (PPARs) as regulators of lipid metabolism.

1997

Peroxisome proliferation (PP) in mammalian cells, first described 30 years ago, represents a fascinating field of modern research. Major improvements made in its understanding were obtained through basic advances that have opened up new areas in cell biology, biochemistry and genetics. A decade after the first report on PP, a new metabolic pathway (peroxisomal beta-oxidation) and its inducibility by peroxisome proliferators were discovered. More recently, a new type of nuclear receptor, the peroxisome proliferator-activated receptor (PPAR), has been described. The first PPAR was discovered in 1990. Since then, many other PPARs have been characterized. This original class of nuclear receptor…

Transcriptional ActivationPeroxisome ProliferationPeroxisome proliferator-activated receptorReceptors Cytoplasmic and NuclearBiologyLigandsBiochemistryMicrobodiesGene Expression Regulation EnzymologicMicrosomesAnimalsHumansReceptorHypolipidemic Agentschemistry.chemical_classificationFatty AcidsLipid metabolismGeneral MedicinePeroxisomeLipid MetabolismCell biologyMitochondriaBiochemistrychemistryNuclear receptorLiverlipids (amino acids peptides and proteins)Peroxisome proliferator-activated receptor alphaAcyl-CoA OxidaseSignal transductionOxidoreductasesOxidation-ReductionSignal TransductionTranscription FactorsBiochimie
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Regulation of the peroxisomal β-oxidation-dependent pathway by peroxisome proliferator-activated receptor α and kinases

2000

The first PPAR (peroxisome proliferator-activated receptor) was cloned in 1990 by Issemann and Green (Nature 347:645-650). This nuclear receptor was so named since it is activated by peroxisome proliferators including several drugs of the fibrate family, plasticizers, and herbicides. This receptor belongs to the steroid receptor superfamily. After activation by a specific ligand, it binds to a DNA response element, PPRE (peroxisome proliferator response element), which is a DR-1 direct repeat of the consensus sequence TGACCT x TGACCT. This mechanism leads to the transcriptional activation of target genes (Motojima et al., J Biol Chem 273:16710-16714, 1998). After the first discovery, severa…

Transcriptional ActivationPeroxisome proliferator-activated receptor gammamedicine.drug_classReceptors Cytoplasmic and NuclearPeroxisome proliferator-activated receptorFibrateBiologyBiochemistryPhosphatidylinositol 3-KinasesmedicineAnimalsHumansPhosphorylationProtein kinase AProtein Kinase CPharmacologychemistry.chemical_classificationPeroxisomeNuclear receptorchemistryBiochemistryPeroxisome Proliferatorslipids (amino acids peptides and proteins)Peroxisome proliferator-activated receptor alphaSignal transductionSignal TransductionTranscription FactorsBiochemical Pharmacology
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