Search results for "ELAV-Like Protein 1"

showing 7 items of 7 documents

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
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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
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MiR675-5p Acts on HIF-1α to Sustain Hypoxic Responses: A New Therapeutic Strategy for Glioma

2016

Hypoxia is a common feature in solid tumours. In glioma, it is considered the major driving force for tumour angiogenesis and correlates with enhanced resistance to conventional therapies, increased invasiveness and a poor prognosis for patients. Here we describe, for the first time, that miR675-5p, embedded in hypoxia-induced long non-coding RNA H19, plays a mandatory role in establishing a hypoxic response and in promoting hypoxia-mediated angiogenesis. We demonstrated, in vitro and in vivo, that miR675-5p over expression in normoxia is sufficient to induce a hypoxic moreover, miR675-5p depletion in low oxygen conditions, drastically abolishes hypoxic responses including angiogenesis. In …

0301 basic medicinemiRNA675AngiogenesisMedicine (miscellaneous)RNA-binding proteinAngiogenesis; Glioma; HuR; Hypoxia; miRNA675; Optical imaging; VHL; Medicine (miscellaneous); Pharmacology Toxicology and Pharmaceutics (miscellaneous)BiologyToxicology and Pharmaceutics (miscellaneous)Cell LineELAV-Like Protein 1Miceoptical imaging03 medical and health sciencesSettore BIO/13 - Biologia ApplicataStress PhysiologicalIn vivoVHLGliomamicroRNAmedicineAnimalsHumansPharmacology Toxicology and Pharmaceutics (miscellaneous)PharmacologyAngiogenesis; HuR; VHL.; glioma; hypoxia; miRNA675; optical imagingMessenger RNANeovascularization PathologichypoxiaVHL.RNAGliomaHypoxia (medical)Hypoxia-Inducible Factor 1 alpha Subunitmedicine.disease3. Good healthAngiogenesiMicroRNAs030104 developmental biologyImmunologyCancer researchHeterograftsHuRAngiogenesismedicine.symptomResearch PaperTheranostics
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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
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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
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Complex Contribution of the 3′-Untranslated Region to the Expressional Regulation of the Human Inducible Nitric-oxide Synthase Gene

2000

Cytokine stimulation of human DLD-1 cells resulted in a marked expression of nitric-oxide synthase (NOS) II mRNA and protein accompanied by only a moderate increase in transcriptional activity. Also, there was a basal transcription of the NOS II gene, which did not result in measurable NOS II expression. The 3′-untranslated region (3′-UTR) of the NOS II mRNA contains four AUUUA motifs and one AUUUUA motif, known to destabilize the mRNAs of proto-oncogenes, nuclear transcription factors, and cytokines. Luciferase reporter gene constructs containing the NOS II 3′-UTR showed a significantly reduced luciferase activity. The embryonic lethal abnormal vision (ELAV)-like protein HuR was found to b…

Regulation of gene expressionMessenger RNAGeneral transcription factorThree prime untranslated regionELAV-Like Protein 1LuciferaseRNA-binding proteinCell BiologyBiologyMolecular BiologyBiochemistryMolecular biologyTranscription factorJournal of Biological Chemistry
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Relief of microRNA-Mediated Translational Repression in Human Cells Subjected to Stress

2006

SummaryIn metazoans, most microRNAs imperfectly base-pair with the 3′ untranslated region (3′UTR) of target mRNAs and prevent protein accumulation by either repressing translation or inducing mRNA degradation. Examples of specific mRNAs undergoing microRNA-mediated repression are numerous, but whether the repression is a reversible process remains largely unknown. Here we show that cationic amino acid transporter 1 (CAT-1) mRNA and reporters bearing its 3′UTR can be relieved from the microRNA miR-122-induced inhibition in human hepatocarcinoma cells subjected to different stress conditions. The derepression of CAT-1 mRNA is accompanied by its release from cytoplasmic processing bodies and i…

AU-rich elementUntranslated regionBiochemistry Genetics and Molecular Biology(all)Three prime untranslated regionPolysomeP-bodiesELAV-Like Protein 1BiologyMolecular biologyPsychological repressionGeneral Biochemistry Genetics and Molecular BiologyDerepressionCell
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