Search results for "Electrophoretic mobility shift assay"

showing 10 items of 40 documents

Cationic polyaspartamide-based nanocomplexes mediate siRNA entry and down-regulation of the pro-inflammatory mediator high mobility group box 1 in ai…

2015

Abstract High-mobility group box 1 (HMGB1) is a nonhistone protein secreted by airway epithelial cells in hyperinflammatory diseases such as asthma. In order to down-regulate HMGB1 expression in airway epithelial cells, siRNA directed against HMGB1 was delivered through nanocomplexes based on a cationic copolymer of poly(N-2-hydroxyethyl)- d,l -aspartamide (PHEA) by using H441 cells. Two copolymers were used in these experiments bearing respectively spermine side chains (PHEA-Spm) and both spermine and PEG2000 chains (PHEA-PEG-Spm). PHEA-Spm and PHEA-PEG-Spm derivatives complexed dsDNA oligonucleotides with a w/w ratio of 1 and higher as shown by a gel retardation assay. PHEA-Spm and PHEA-P…

Polyaspartamide copolymerNucleic acid-based drugDown-RegulationPharmaceutical ScienceSpermineRespiratory MucosaBiologyTransfectionAirway epithelial cellsNucleic acid-based drugsFlow cytometrychemistry.chemical_compoundCell Line TumorMaterials TestingAirway epithelial cellmedicineHumansElectrophoretic mobility shift assayMTT assayDAPIRNA Small InterferingCytotoxicityPolyhydroxyethyl MethacrylateHMGB1Airway epithelial cells; HMGB1; Nucleic acid-based drugs; PHEA; Polyaspartamide copolymers; Sirnamedicine.diagnostic_testOligonucleotideMammaglobin AfungiGene Transfer TechniquesEpithelial CellsDNAPHEAMolecular biologyNanostructuresPolyaspartamide copolymerschemistrySirnaTrypan bluePeptides
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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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Evaluating ancient Egyptian prescriptions today: Anti-inflammatory activity of Ziziphus spina-christi.

2015

Abstract Background Ziziphus spina-christi (L.) Desf. (Christ's Thorn Jujube) is a wild tree today found in Jordan, Israel, Egypt, and some parts of Africa, which was already in use as a medicinal plant in Ancient Egypt. In ancient Egyptian prescriptions, it was used in remedies against swellings, pain, and heat, and thus should have anti-inflammatory effects. Nowadays, Z. spina-christi, is used in Egypt (by Bedouins, and Nubians), the Arabian Peninsula, Jordan, Iraq, and Morocco against a wide range of illnesses, most of them associated with inflammation. Pharmacological research undertaken to date suggests that it possesses anti-inflammatory, hypoglycemic, hypotensive and anti-microbial e…

0301 basic medicinemedicine.drug_classLeupeptinsIn silicoHerbal MedicineEgypt AncientAnti-Inflammatory AgentsPharmaceutical SciencePlant RootsAnti-inflammatory03 medical and health sciencesCell Line TumorDrug DiscoveryMedicineGallocatechinBioassayHumansElectrophoretic mobility shift assayHistory AncientPharmacologyZiziphus spina-christiInflammationPlants MedicinalbiologyTraditional medicinePlant Stemsbusiness.industryPlant ExtractsTranscription Factor RelAZiziphusZiziphusbiology.organism_classificationMolecular Docking Simulation030104 developmental biologyComplementary and alternative medicineDocking (molecular)SeedsMolecular MedicinebusinessPhytomedicine : international journal of phytotherapy and phytopharmacology
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The coat protein of prunus necrotic ringspot virus specifically binds to and regulates the conformation of its genomic RNA

2003

AbstractBinding of coat protein (CP) to the 3′ nontranslated region (3′-NTR) of viral RNAs is a crucial requirement to establish the infection of Alfamo- and Ilarviruses. In vitro binding properties of the Prunus necrotic ringspot ilarvirus (PNRSV) CP to the 3′-NTR of its genomic RNA using purified E. coli- expressed CP and different synthetic peptides corresponding to a 26-residue sequence near the N-terminus were investigated by electrophoretic mobility shift assays. PNRSV CP bound to, at least, three different sites existing on the 3′-NTR. Moreover, the N-terminal region between amino acid residues 25 to 50 of the protein could function as an independent RNA-binding domain. Single exchan…

Molecular Sequence DataElectrophoretic Mobility Shift AssayPlasma protein bindingBiologyIlarvirusProtein structureVirologyElectrophoretic mobility shift assayMagnesiumAmino Acid SequencePeptide sequence3' Untranslated RegionsIlarvirusBase SequenceCircular DichroismRNA ConformationRNAbiology.organism_classificationMolecular biologyProtein Structure TertiaryBiochemistryPrunus necrotic ringspot virusNucleic Acid ConformationRNA ViralCapsid ProteinsPrunusProtein BindingVirology
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A Functional Role of IκB-ε in Endothelial Cell Activation

2000

Abstract The NF-κB inhibitor IκB-ε is a new member of the IκB protein family, but its functional role in regulating NF-κB-mediated induction of adhesion molecule expression is unknown. In vascular endothelial cells, IκB-ε associates predominantly with the NF-κB subunit Rel A and to a lesser extent with c-Rel, whereas IκB-α and IκB-β associate with Rel A only. Following stimulation with TNF-α, pyrrolidine dithiocarbamate (PDTC), N-acetylcysteine, and dexamethasone prevented IκB kinase-induced IκB-α, but not IκB-β or IκB-ε phosphorylation and degradation. Since the activation of NF-κB is required for the induction of adhesion molecule expression, we examined the role of IκB-ε in the transacti…

Reporter geneProtein subunitImmunologyPromoterIκB kinaseBiologyMolecular biologychemistry.chemical_compoundTransactivationPyrrolidine dithiocarbamatechemistryImmunology and AllergyPhosphorylationElectrophoretic mobility shift assayThe Journal of Immunology
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Phenolic Acid-Mediated Regulation of the padC Gene, Encoding the Phenolic Acid Decarboxylase of Bacillus subtilis

2008

ABSTRACT In Bacillus subtilis , several phenolic acids specifically induce expression of padC , encoding a phenolic acid decarboxylase that converts these antimicrobial compounds into vinyl derivatives. padC forms an operon with a putative coding sequence of unknown function, yveFG , and this coding sequence does not appear to be involved in the phenolic acid stress response (PASR). To identify putative regulators involved in the PASR, random transposon mutagenesis, combined with two different screens, was performed. PadR, a negative transcriptional regulator of padC expression, was identified. padR is not located in the vicinity of padC , and the expression of padR is low and appears const…

Carboxy-lyasesCarboxy-LyasesOperonMolecular Sequence DataElectrophoretic Mobility Shift AssayBacillus subtilisBiologyMicrobiologyGene Expression Regulation Enzymologic03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsHydroxybenzoatesGene RegulationElectrophoretic mobility shift assay[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyAmino Acid SequenceMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesBase Sequence030306 microbiologyEffectorGene Expression Regulation BacterialPhenolic acidbiology.organism_classificationMolecular biologyRepressor ProteinsEnzymechemistryBiochemistryTransposon mutagenesisBacillus subtilis
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p53-Mediated downregulation of H ferritin promoter transcriptional efficiency via NF-Y.

2008

The tumor suppressor protein p53 triggers many of the cellular responses to DNA damage by regulating the transcription of a series of downstream target genes. p53 acts on the promoter of the target genes by interacting with the trimeric transcription factor NF-Y. H ferritin promoter activity is tightly dependent on a multiprotein complex called Bbf; on this complex NF-Y plays a major role. The aim of this work was to study the modulation of H ferritin expression levels by p53. CAT reporter assays indicate that: (i) p53 overexpression strongly downregulates the transcriptional efficiency driven by an H ferritin promoter construct containing only the NF-Y recognition sequence and that the phe…

Chromatin ImmunoprecipitationMultiprotein complexTranscription GeneticDown-RegulationBiologyBiochemistryTranscriptional regulationDownregulation and upregulationTranscription (biology)Transcriptional regulationFerritin geneHumansElectrophoretic mobility shift assayp300-CBP Transcription FactorsPromoter Regions GeneticTranscription factorGeneFerritin gene; Transcriptional regulation; Transcriptional factorCell BiologyHCT116 CellsMolecular biologyGene Expression Regulation NeoplasticCCAAT-Binding FactorDoxorubicinTranscriptional factorApoferritinsTumor Suppressor Protein p53Chromatin immunoprecipitationHeLa CellsProtein Binding
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Nuclear receptor NR5A2 and bone: gene expression and association with bone mineral density

2011

El pdf del artículo es el manuscrito de autor (PMCID: PMC3682472).-- et al.

endocrine systemmedicine.medical_specialtyBone densityEndocrinology Diabetes and MetabolismReceptors Cytoplasmic and NuclearElectrophoretic Mobility Shift AssaySingle-nucleotide polymorphismIn Vitro TechniquesArticleBone and BonesCell LineBone remodelingEndocrinologyOsteoprotegerinBone DensityInternal medicineBone cellmedicineHumansPromoter Regions GeneticAgedAged 80 and overRegulation of gene expressionBone mineralOsteoblastsBonesbiologyGeneral MedicineMiddle AgedGene regulationPostmenopauseEndocrinologyOsteocalcinbiology.proteinFemaleGene expression
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Oxidative stress induces the expression of the major histocompatibility complex in murine tumor cells.

2001

The effect of t-butyl hydroperoxide (t-BOOH) on the induction of the Major Histocompatibility Complex (MHC) class I genes has been studied in two cell clones (B9 and G2) of the methylcholanthrene-induced murine fibrosarcoma GR9. These two clones were selected based on their different biological and biochemical behavior specially related to their tumor induction capability when injected into a BALB/c mouse. t-BOOH (0.125 mM) induced the expression of H-2 molecules in both cell clones. In B9 cell clone, in which MHC basal expression is very low or absent, t-BOOH significantly induced H-2Kd, H-2Dd and H-2Ld molecules. In G2 cell clone the expression of MHC class I genes was also enhanced by th…

FibrosarcomaCellElectrophoretic Mobility Shift AssayBiologyMajor histocompatibility complexBiochemistryMajor Histocompatibility ComplexTransactivationMiceAntigentert-ButylhydroperoxideCell CloneMalondialdehydeMHC class ImedicineTumor Cells CulturedAnimalsGlutathione PeroxidaseMice Inbred BALB CSuperoxide DismutaseMHC Class I GeneHistocompatibility Antigens Class INF-kappa BDeoxyguanosineGeneral Medicine3T3 CellsCatalaseFlow CytometryMolecular biologyGlutathioneOxidative Stressmedicine.anatomical_structureGene Expression Regulation8-Hydroxy-2'-Deoxyguanosinebiology.proteinCD8MethylcholanthreneFree radical research
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Analysis of involvement of the 3?-untranslated regions in regulating mRNA stability for vitellogenin, cyanoprotein ?, and cyanoprotein ? from the bea…

2002

The degradation of the 3'-untranslated regions (UTRs) of vitellogenin, cyanoprotein alpha, and cyanoprotein beta from the bean bug, Riptortus clavatus, was analyzed in vitro. The degradation pattern was similar for all three RNAs, with a high degradation rate in non-diapausing adult insects and no degradation in the fifth instar nymphs and in diapausing adults, and was not correlated with the expression levels of these three proteins. Proteins binding to the 3'-UTRs were detected in polysomal and cytosolic extracts. These factors, however, were present in all developmental stages. The abundance of the polysomal factor showed little variation, but the cytosolic factor was enriched in adult i…

Untranslated regionPhysiologyMolecular Sequence DatahexamerinElectrophoretic Mobility Shift AssayRNA-binding proteinBinding CompetitiveBiochemistryHemipteraVitellogeninsVitellogeninBotanyAnimalsRNA Messenger3' Untranslated RegionsRegulation of gene expressionMessenger RNABase Sequencebiologyjuvenile hormoneThree prime untranslated regionRNA-Binding ProteinsRNAGeneral MedicineRNA binding proteincyanoproteindiapauseGene Expression RegulationBiochemistryInsect ScienceJuvenile hormonebiology.proteinInsect ProteinsSequence AlignmentArchives of Insect Biochemistry and Physiology
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