Search results for "Nuclear receptor coactivator 2"

showing 4 items of 4 documents

A role for the transcription intermediary factor 2 in zebrafish myelopoiesis.

2007

Objective TIF2 is fused with MOZ in the inv(8)(p11q13) acute myeloid leukemia. TIF2, member of the p160 family, is a histone acetyl transferase (HAT). Deletion of p160 genes were performed in mice. Some observations suggest that p160 family members may perform overlapping functions in mice. Therefore, we decided to choose the zebrafish model to study TIF2. The aim of this study was to characterize the role of this HAT during embryonic development. Material and Methods We use antisense, morpholino-modified oligomers to transiently knockdown tif2 gene, thus determining whether TIF2 plays a role in zebrafish early development. Results We show that tif2 is involved in embryogenesis and in primi…

Cancer ResearchMorpholinesEmbryonic DevelopmentIn situ hybridizationBiologyAngioblastSensitivity and SpecificityNuclear Receptor Coactivator 2Structure-Activity RelationshipNotochordGeneticsmedicineAnimalsRNA MessengerMolecular BiologyZebrafishZebrafishGeneticsMyelopoiesisGene knockdownMembrane GlycoproteinsEmbryogenesisMicrofilament ProteinsGene Expression Regulation DevelopmentalCell DifferentiationCell BiologyHematologyOligonucleotides Antisensebiology.organism_classificationCell biologymedicine.anatomical_structurePhenotypeFLI1Models AnimalRNAMyelopoiesisExperimental hematology
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Transcriptional activation of CYP2C9, CYP1A1, and CYP1A2 by hepatocyte nuclear factor 4alpha requires coactivators peroxisomal proliferator activated…

2006

Hepatocyte nuclear factor 4alpha (HNF4alpha) is a key transcription factor for the constitutive expression of cytochromes P450 (P450s) in the liver. However, human hepatoma HepG2 cells show a high level of HNF4alpha but express only marginal P450 levels. We found that the HNF4alpha-mediated P450 transcription in HepG2 is impaired by the low level of coactivators peroxisomal proliferator activated receptor-gamma coactivator 1alpha (PGC1alpha) and steroid receptor coactivator 1 (SRC1). Reporter assays with a chimeric CYP2C9-LUC construct demonstrated that the sole transfection of coactivators induced luciferase activity in HepG2 cells. In HeLa cells however, CYP2C9-LUC activity only significa…

MaleTranscriptional Activationendocrine systemBiologyResponse ElementsTransfectiondigestive systemAdenoviridaeNuclear Receptor Coactivator 1Cytochrome P-450 CYP1A2CoactivatorCytochrome P-450 CYP1A1HumansInsulinTranscription factorCells CulturedHeat-Shock ProteinsCytochrome P-450 CYP2C9Histone AcetyltransferasesPharmacologyTransfectionMiddle AgedMolecular biologyPeroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alphaNuclear receptor coactivator 1Hepatocyte nuclear factorsHepatocyte Nuclear Factor 4Nuclear receptor coactivator 3Nuclear receptor coactivator 2HepatocytesMolecular MedicineFemaleAryl Hydrocarbon HydroxylasesChromatin immunoprecipitationHeLa CellsProtein BindingTranscription FactorsMolecular pharmacology
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MOZ/TIF2-induced acute myeloid leukaemia in transgenic fish.

2008

The inv(8)(p11q13) chromosomal abnormality, described in acute myeloid leukaemias (AML), fuses the histone acetyl-transferase (HAT) MYST3 (MOZ) gene with another HAT gene, NCOA2 (TIF2). We generated a transgenic zebrafish in which the MYST3/NCOA2 fusion gene was expressed under control of the spi1 promoter. An AML developed in 2 of 180 MYST3/NCOA2-EGFP-expressing embryos, 14 and 26 months after injection of the fusion gene in a one-cell embryo, respectively. This leukaemia was characterised by an extensive invasion of kidneys by myeloid blast cells. This model, which is the first zebrafish model of AML, demonstrates the oncogenic potency of MYST3/NCOA2 fusion gene.

MyeloidMicroinjectionsOncogene Proteins FusionTransgeneBiologyKidneyMYST3Fusion geneAnimals Genetically ModifiedNuclear Receptor Coactivator 2hemic and lymphatic diseasesmedicineAnimalsZebrafishGeneZebrafishHistone AcetyltransferasesSPI1Reverse Transcriptase Polymerase Chain ReactionHematologymedicine.diseasebiology.organism_classificationMolecular biologyLeukemiaDisease Models AnimalLeukemia Myeloid Acutemedicine.anatomical_structureembryonic structuresCancer researchGene FusionBritish journal of haematology
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Co-regulator recruitment and the mechanism of retinoic acid receptor synergy.

2002

Crystal structure and co-regulator interaction studies have led to a general mechanistic view of the initial steps of nuclear receptor (NR) action. Agonist-induced transconformation of the ligand-binding domain (holo-LBD) leads to the formation of co-activator complexes, and destabilizes the co-repressor complexes bound to the ligand-free (apo) LBD. However, the molecular basis of retinoid-X receptor (RXR) 'subordination' in heterodimers, an essential mechanism to avoid signalling pathway promiscuity, has remained elusive. RXR, in contrast to its heterodimer partner, cannot autonomously induce transcription on binding of cognate agonists. Here we show that RXR can bind ligand and recruit co…

Protein ConformationReceptors Retinoic AcidPlasma protein bindingRetinoid X receptorLigandsNuclear Receptor Coactivator 2Structure-Activity RelationshipmedicineNuclear Receptor Co-Repressor 2Binding siteNuclear receptor co-repressor 2PhysicsMultidisciplinaryCell biologyDNA-Binding ProteinsRepressor ProteinsRetinoic acid receptorRetinoid X ReceptorsMechanism of actionBiochemistryNuclear receptorModels Chemicalembryonic structuresNuclear receptor coactivator 2medicine.symptomDimerizationProtein BindingTranscription FactorsNature
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