Search results for "ELAV Proteins"

showing 8 items of 8 documents

Intestinal epithelial HuR modulates distinct pathways of proliferation and apoptosis and attenuates small intestinal and colonic tumor development.

2014

Abstract HuR is a ubiquitous nucleocytoplasmic RNA-binding protein that exerts pleiotropic effects on cell growth and tumorigenesis. In this study, we explored the impact of conditional, tissue-specific genetic deletion of HuR on intestinal growth and tumorigenesis in mice. Mice lacking intestinal expression of HuR (Hur IKO mice) displayed reduced levels of cell proliferation in the small intestine and increased sensitivity to doxorubicin-induced acute intestinal injury, as evidenced by decreased villus height and a compensatory shift in proliferating cells. In the context of Apcmin/+ mice, a transgenic model of intestinal tumorigenesis, intestinal deletion of the HuR gene caused a three-fo…

Cancer ResearchPost-translational regulationRNA-binding proteinContext (language use)ApoptosisCell Growth ProcessesBiologymedicine.disease_causeArticleAU-rich RNAMiceGene expressionIntestinal NeoplasmsmedicineAnimalsmRNA stabilityIntestinal MucosaMice KnockoutCell growthMolecular biologyPhenotypeProtein-RNA interactionSmall intestineDisease Models Animalmedicine.anatomical_structureOncologyELAV ProteinsApoptosisColonic NeoplasmsCancer researchCarcinogenesis
researchProduct

The commonly used marker ELAV is transiently expressed in neuroblasts and glial cells in theDrosophilaembryonic CNS

2007

Glial cells in the Drosophila embryonic nervous system can be monitored with the marker Reversed-polarity (Repo), whereas neurons lack Repo and express the RNA-binding protein ELAV (Embryonic Lethal, Abnormal Vision). Since the first description of the ELAV protein distribution in 1991 (Robinow and White), it is believed that ELAV is an exclusive neuronal and postmitotic marker. Looking at ELAV expression, we unexpectedly observed that, in addition to neurons, ELAV is transiently expressed in embryonic glial cells. Furthermore, it is transiently present in the proliferating longitudinal glioblast, and it is transcribed in embryonic neuroblasts. Likewise, elav-Gal4 lines, which are generally…

Central Nervous SystemNervous systemGenes InsectBiologyAnimals Genetically ModifiedGlioblastNeuroblastGenes ReportermedicineAnimalsDrosophila ProteinsEmbryonic Stem CellsNeuronsRegulation of gene expressionGene Expression Regulation DevelopmentalEmbryoAnatomyEmbryonic stem cellPhenotypeNeural stem cellCell biologyPhenotypemedicine.anatomical_structureELAV Proteinsnervous systemMutationDrosophilaNeurogliaDevelopmental BiologyDevelopmental Dynamics
researchProduct

The RNA-binding protein ELAV regulates Hox RNA processing, expression and function within the Drosophila nervous system

2014

The regulated head-to-tail expression of Hox genes provides a coordinate system for the activation of specific programmes of cell differentiation according to axial level. Recent work indicates that Hox expression can be regulated via RNA processing but the underlying mechanisms and biological significance of this form of regulation remain poorly understood. Here we explore these issues within the developing Drosophila central nervous system (CNS). We show that the pan-neural RNA-binding protein (RBP) ELAV (Hu antigen) regulates the RNA processing patterns of the Hox gene Ultrabithorax (Ubx) within the embryonic CNS. Using a combination of biochemical, genetic and imaging approaches we demo…

Embryo Nonmammaliananimal structuresNeurogenesisRNA-binding proteinCellular differentiationMolecular Sequence DataRNA-binding proteinBiologyAntennapediaNervous SystemMorphogenesisAnimalsDrosophila ProteinsRNA Processing Post-TranscriptionalELAV/HuHox geneMolecular BiologyTranscription factorPhylogenyResearch ArticlesUltrabithoraxHomeodomain ProteinsAlternative polyadenylation (APA)GeneticsBase SequenceAlternative splicingGenes HomeoboxGene Expression Regulation DevelopmentalSegment-specific apoptosisHoxCell biologyDrosophila melanogasterELAV ProteinsRNA processingCentral nervous systemembryonic structuresDrosophilaDrosophila ProteinTranscription FactorsAlternative splicingDevelopmental BiologyDevelopment
researchProduct

Glucagon-like peptide-1 modulates neurally evoked mucosal chloride secretion in guinea pig small intestine in vitro

2011

Glucagon-like peptide-1 (GLP-1) acts at the G protein-coupled receptor, GLP-1R, to stimulate secretion of insulin and to inhibit secretion of glucagon and gastric acid. Involvement in mucosal secretory physiology has received negligible attention. We aimed to study involvement of GLP-1 in mucosal chloride secretion in the small intestine. Ussing chamber methods, in concert with transmural electrical field stimulation (EFS), were used to study actions on neurogenic chloride secretion. ELISA was used to study GLP-1R effects on neural release of acetylcholine (ACh). Intramural localization of GLP-1R was assessed with immunohistochemistry. Application of GLP-1 to serosal or mucosal sides of fla…

MaleCytoplasmendocrine systemmedicine.medical_specialtyReceptors Vasoactive Intestinal Polypeptide Type IPhysiologyGuinea PigsScopolamineVasoactive intestinal peptideHormones and SignalingIleumIn Vitro TechniquesHexamethoniumGlucagonGlucagon-Like Peptide-1 ReceptorCholine O-AcetyltransferaseGuinea pigChloridesGlucagon-Like Peptide 1IleumPhysiology (medical)Internal medicineIntestine SmallReceptors GlucagonmedicineAnimalsNeuropeptide YSecretionIntestinal MucosaNeuronsHepatologyChemistrydigestive oral and skin physiologyElectric ConductivityGastroenterologyAcetylcholineElectric StimulationPeptide FragmentsSmall intestineElectrophysiological PhenomenaEndocrinologymedicine.anatomical_structureSomatostatinELAV ProteinsGastric acidCarbacholSomatostatinhormones hormone substitutes and hormone antagonistsVasoactive Intestinal PeptideAmerican Journal of Physiology-Gastrointestinal and Liver Physiology
researchProduct

Proteome-Wide Characterization of the RNA-Binding Protein RALY-Interactome Using the in Vivo-Biotinylation-Pulldown-Quant (iBioPQ) Approach

2013

RALY is a member of the heterogeneous nuclear ribonucleoproteins, a family of RNA-binding proteins generally involved in many processes of mRNA metabolism. No quantitative proteomic analysis of RALY-containing ribonucleoparticles (RNPs) has been performed so far, and the biological role of RALY remains elusive. Here, we present a workflow for the characterization of RALY's interaction partners, termed iBioPQ, that involves in vivo biotinylation of biotin acceptor peptide (BAP)-fused protein in the presence of the prokaryotic biotin holoenzyme synthetase of BirA so that it can be purified using streptavidin-coated magnetic beads, circumventing the need for specific antibodies and providing e…

ProteomeRecombinant Fusion ProteinsMolecular Sequence DataBiotinRNA-binding proteinBiologyHeterogeneous ribonucleoprotein particleProteomicsPoly(A)-Binding Protein IBiochemistryInteractomeELAV-Like Protein 103 medical and health scienceschemistry.chemical_compound0302 clinical medicineNuclear Matrix-Associated ProteinsBiotinProtein Interaction MappingHumansCarbon-Nitrogen LigasesAmino Acid SequenceProtein Interaction MapsPeptide sequence030304 developmental biology0303 health sciencesEscherichia coli ProteinsHeterogeneous-Nuclear Ribonucleoprotein Group CRNA-Binding ProteinsGeneral ChemistryRepressor ProteinsHEK293 CellsELAV ProteinsGene Expression RegulationBiochemistrychemistryProtein Biosynthesis030220 oncology & carcinogenesisBiotinylationProteomeBiological AssayStreptavidinHeLa CellsProtein BindingJournal of Proteome Research
researchProduct

Nitric oxide increases the decay of matrix metalloproteinase 9 mRNA by inhibiting the expression of mRNA-stabilizing factor HuR.

2003

Dysregulation of extracellular matrix turnover is an important feature of many inflammatory processes. Rat renal mesangial cells express high levels of matrix metalloproteinase 9 (MMP-9) in response to inflammatory cytokines such as interleukin-1 beta. We demonstrate that NO does strongly destabilize MMP-9 mRNA, since different luciferase reporter gene constructs containing the MMP-9 3' untranslated region (UTR) displayed significant reduced luciferase activity in response to the presence of NO. Moreover, by use of an in vitro degradation assay we found that the cytoplasmic fractions of NO-treated cells contained a higher capacity to degrade MMP-9 transcripts than those obtained from contro…

Untranslated regionCytoplasmRNA StabilityMolecular Sequence DataGene ExpressionRNA-binding proteinBiologyKidneyNitric OxideELAV-Like Protein 1Gene expressionAnimalsElectrophoretic mobility shift assayNitric Oxide DonorsRNA MessengerEnzyme InhibitorsMolecular Biology3' Untranslated RegionsCyclic GMPCells CulturedRepetitive Sequences Nucleic AcidMessenger RNABase SequenceThree prime untranslated regionMolecular MimicryRNARNA-Binding ProteinsCell BiologyMolecular biologyRecombinant ProteinsRatsELAV ProteinsMatrix Metalloproteinase 9RibonucleoproteinsGuanylate CyclaseAntigens SurfaceAminoquinolinesDactinomycinSoluble guanylyl cyclaseInterleukin-1Nitroso CompoundsMolecular and cellular biology
researchProduct

Involvement of KSRP in the post-transcriptional regulation of human iNOS expression–complex interplay of KSRP with TTP and HuR

2005

We purified the KH-type splicing regulatory protein (KSRP) as a protein interacting with the 3'-untranslated region (3'-UTR) of the human inducible nitric oxide (iNOS) mRNA. Immunodepletion of KSRP enhanced iNOS 3'-UTR RNA stability in in vitro-degradation assays. In DLD-1 cells overexpressing KSRP cytokine-induced iNOS expression was markedly reduced. In accordance, downregulation of KSRP expression increases iNOS expression by stabilizing iNOS mRNA. Co-immunoprecipitations showed interaction of KSRP with the exosome and tristetraprolin (TTP). To analyze the role of KSRP binding to the 3'-UTR we studied iNOS expression in DLD-1 cells overexpressing a non-binding mutant of KSRP. In these ce…

Untranslated regionRNA StabilityTristetraprolinNitric Oxide Synthase Type II610 Medicine & healthRNA-binding proteinBiologyImmediate early proteinArticleGene Expression Regulation EnzymologicELAV-Like Protein 1Immediate-Early ProteinsTristetraprolinCell Line TumorGeneticsHumansRNA Messenger610 Medicine & healthPost-transcriptional regulation3' Untranslated RegionsRegulation of gene expressionMessenger RNAThree prime untranslated regionRNA-Binding ProteinsMolecular biologyDNA-Binding ProteinsELAV ProteinsAntigens SurfaceMutationTrans-ActivatorsCytokinesNitric Oxide SynthaseNucleic Acids Research
researchProduct

The 3'-UTR of the mRNA coding for the major protein kinase C substrate MARCKS contains a novel CU-rich element interacting with the mRNA stabilizing …

2003

The expression of the major protein kinase C substrate MARCKS (myristoylated alanine-rich C kinase substrate) is controlled by the stability of its mRNA. While the MARCKS mRNA is long living in quiescent fibroblasts (t1/2 = 14 h), its half-life time is drastically reduced (t1/2 = 2 h) in cells treated with phorbol esters to activate protein kinase C (PKC) or treated with growth factors. In a first step to study the underlying mechanism we identified both a cis-element on the MARCKS mRNA and the corresponding trans-acting factors. Fusing the complete 3'-UTR or specific regions of the 3'-UTR of the MARCKS gene to a luciferase reporter gene caused a drastic decrease in luciferase expression to…

Untranslated regionRecombinant Fusion ProteinsELAV-Like Protein 1Down-RegulationNerve Tissue ProteinsELAV-Like Protein 4BiologyBiochemistryELAV-Like Protein 1MiceGenes ReporterAnimalsRNA MessengerMARCKSLuciferasesMyristoylated Alanine-Rich C Kinase Substrate3' Untranslated RegionsProtein Kinase CProtein kinase CAU-rich elementMessenger RNAThree prime untranslated regionIntracellular Signaling Peptides and ProteinsMembrane ProteinsProteinsRNA-Binding Proteins3T3 CellsFibroblastsMolecular biologyELAV ProteinsAntigens SurfaceMARCKS GeneEuropean Journal of Biochemistry
researchProduct