Search results for "Phosphopyruvate hydratase"

showing 10 items of 30 documents

ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: relationship with Myc promoter-binding protein 1 (MBP-1).

2000

The Myc promoter-binding protein-1 (MBP-1) is a 37-38 kDa protein that binds to the c-myc P2 promoter and negatively regulates transcription of the protooncogene. MBP-1 cDNA shares 97% similarity with the cDNA encoding the glycolytic enzyme alpha-enolase and both genes have been mapped to the same region of human chromosome 1, suggesting the hypothesis that the two proteins might be encoded by the same gene. We show here data indicating that a 37 kDa protein is alternatively translated from the full-length alpha-enolase mRNA. This shorter form of alpha-enolase is able to bind the MBP-1 consensus sequence and to downregulate expression of a luciferase reporter gene under the control of the c…

CytoplasmTranscriptional repressionRecombinant Fusion ProteinsBiophysicsEnolaseCodon InitiatorDown-RegulationBiologyAlternative translationResponse ElementsTransfectionBiochemistryCell LineGene productHSPA4Proto-Oncogene Proteins c-mycStructural BiologyHSPA2GeneticsBiomarkers TumorE2F1AnimalsHumansSOCS6Genes Tumor SuppressorDNA bindingPromoter Regions GeneticMolecular BiologyYY1Tumor Suppressor ProteinsNuclear ProteinsCell BiologyDNAMolecular biologyGPS2Neoplasm ProteinsDNA-Binding ProteinsMolecular WeightRepressor ProteinsAlternative SplicingGATAD2BChromosomes Human Pair 1Phosphopyruvate HydrataseProtein BiosynthesisPeptidesProtein BindingFEBS letters
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The gene encoding the transcriptional repressor BERF-1 maps to a region of conserved synteny on mouse chromosome 16 and human chromosome 3 and a rela…

1999

We have recently identified and characterized a Kruppel-like zinc finger protein (BERF-1), that functions as a repressor of β enolase gene transcription. By interspecific backcross analysis the gene encoding BERF-1 was localized 4.7 cM proximal to the <i>Mtv6</i> locus on mouse chromosome 16, and an isolated pseudogene was localized to mouse chromosome 8, about 5.3 cM distal to the D8Mit4 marker. Nucleotide sequence identity and chomosome location indicate that the gene encoding BERF-1 is the mouse homologue (<i>Zfp148</i>) of ZNF148 localized to human chromosome 3q21, a common translocation site in acute myeloid leukemia patients.

Genetic MarkersDNA ComplementaryTranscription GeneticKruppel-Like Transcription FactorsBiologyHybrid CellsPolymerase Chain ReactionGene Expression Regulation EnzymologicMiceChromosome 16GeneticsAnimalsHumansMolecular BiologyGenetics (clinical)Conserved SequenceSyntenyDNA PrimersGeneticsBase SequenceYY1Chromosome MappingTAF9Zinc FingersTCF4DNA-Binding ProteinsRepressor ProteinsChromosome 3GATAD2BPhosphopyruvate Hydratasecardiovascular systemChromosomes Human Pair 3Chromosome 22PseudogenesTranscription FactorsCytogenetics and cell genetics
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Assignment of enolase processed pseudogene (ENO1P) to human chromosome 1 bands 1q41→q42

1996

Geneticschemistry.chemical_classificationPhosphopyruvate hydratasePseudogeneEnolaseChromosome MappingChromosomeBiologyEnzymeGene mappingchemistryBiochemistryChromosomes Human Pair 1Phosphopyruvate HydrataseGeneticsHumansMolecular BiologyGeneIn Situ Hybridization FluorescencePseudogenesGenetics (clinical)Carbon-Oxygen LyasesCytogenetic and Genome Research
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Glycine receptors influence radial migration in the embryonic mouse neocortex.

2011

To investigate whether glycine receptors influence radial migration in the neocortex, we analyzed the effect of glycine and the glycinergic antagonist strychnine, on the distribution of 5-bromo-2'deoxyuridine-labeled neurons in organotypic slice cultures from embryonic mice cortices. Application of glycine impeded radial migration only in the presence of the glycine-transport blockers, ALX-5407 and ALX-1393. This effect was blocked by the specific glycine receptor antagonist strychnine, whereas application of strychnine in the absence of glycine was without effect. We conclude from these observations that an activation of glycine receptors can impede radial migration, but that the glycinerg…

GlycineCell CountNeocortexBiologychemistry.chemical_compoundMiceOrgan Culture TechniquesReceptors GlycineCell MovementGlial Fibrillary Acidic ProteinmedicineAnimalsDrug InteractionsReceptorGlycine receptorNeuronsNeocortexGeneral NeuroscienceAntagonistGlycine AgentsSarcosineGlycine receptor antagonistStrychnineStrychnineEmbryo MammalianCell biologymedicine.anatomical_structurechemistryBromodeoxyuridineCerebral cortexPhosphopyruvate HydrataseGlycineNeuroscienceNeuroreport
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Calretinin/PSA-NCAM immunoreactive granule cells after hippocampal damage produced by kainic acid and DEDTC treatment in mouse.

2003

There is a dramatic increase in the number of lightly immunoreactive calretinin cells in the granular layer of the dentate gyrus of the mouse hippocampus 1 day after excitotoxic injury using kainic acid combined with the zinc chelator diethyldithiocarbamate. At 7 days after treatment, these cells are strongly immunoreactive for calretinin and for the polysialated form of the glycoprotein neural cell adhesion molecule (PSA-NCAM). The reexpression of calretinin and PSA-NCAM after treatment corresponds well with the loss of input from the damaged hilar mossy cells. These cells could be considered immature granule cells since they are immunoreactive to markers for immature cells such as PSA-NCA…

Kainic acidTime FactorsNeural Cell Adhesion Molecule L1Granular layerHippocampal formationHippocampuschemistry.chemical_compoundMiceS100 Calcium Binding Protein GExcitatory Amino Acid AgonistsAnimalsMolecular BiologyChelating AgentsNeuronsKainic AcidbiologyGeneral NeuroscienceDentate gyrusNeurogenesisDrug SynergismMolecular biologyImmunohistochemistryMicroscopy Electronnervous systemchemistryCalbindin 2Phosphopyruvate HydrataseImmunologybiology.proteinSialic AcidsNeural cell adhesion moleculeNeurology (clinical)NeuNCalretininDitiocarbDevelopmental BiologyBrain research
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An integrated humoral and cellular response is elicited in pancreatic cancer by alpha-enolase, a novel pancreatic ductal adenocarcinoma-associated an…

2009

Pancreatic ductal adenocarcinoma (PDAC) is a fatal disease with a very poor 5-year survival rate. alpha-Enolase is a glycolytic enzyme that also acts as a surface plasminogen receptor. We find that it is overexpressed in PDAC and present on the cell surface of PDAC cell lines. The clinical correlation of its expression with tumor status has been reported for lung and hepatocellular carcinoma. We have previously demonstrated that sera from PDAC patients contain IgG autoantibodies to alpha-enolase. The present work was intended to assess the ability of alpha-enolase to induce antigen-specific T cell responses. We show that alpha-enolase-pulsed dendritic cells (DC) specifically stimulate healt…

KeratinocytesCancer ResearchPancreatic diseaseendocrine system diseasesalpha-enolaseAntibodies NeoplasmAlpha-enolaseT-LymphocytesMiceSkinImmunity Cellularhuman; pancreatic ductal adenocarcinoma; alpha enolase; tumor antigen; B cell response; T cell responsebiologyalpha enolasehuman; pancreatic ductal adenocarcinoma; alpha-enolase; tumor antigen; B cell response; T cell responseImmunohistochemistryTumor antigenUp-RegulationGene Expression Regulation Neoplasticmedicine.anatomical_structureOncologyAntibodyCarcinoma Pancreatic DuctalB cell responseT cellBlotting Westernpancreatic ductal adenocarcinomaGene Expression Regulation EnzymologicInterferon-gammaImmune systemAntigenAntigens NeoplasmCell Line TumorPancreatic cancermedicineAnimalsHumanshumanPancreasCell ProliferationDendritic Cellsmedicine.diseaseT cell responsepancreatic ductal adenocarcinoma; alpha-enolase; tumor antigen.digestive system diseasesPancreatic NeoplasmsImmunoglobulin GPhosphopyruvate HydrataseAntibody FormationImmunologybiology.proteintumor antigenT-Lymphocytes Cytotoxic
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Pro-invasive stimuli and the interacting protein Hsp70 favour the route of alpha-enolase to the cell surface

2017

AbstractCell surface expression of alpha-enolase, a glycolytic enzyme displaying moonlighting activities, has been shown to contribute to the motility and invasiveness of cancer cells through the protein non-enzymatic function of binding plasminogen and enhancing plasmin formation. Although a few recent records indicate the involvement of protein partners in the localization of alpha-enolase to the plasma membrane, the cellular mechanisms underlying surface exposure remain largely elusive. Searching for novel interactors and signalling pathways, we used low-metastatic breast cancer cells, a doxorubicin-resistant counterpart and a non-tumourigenic mammary epithelial cell line. Here, we demon…

Lipopolysaccharides0301 basic medicineAlpha-enolaseScienceCellPlasma protein bindingArticle03 medical and health sciencesCell MovementEpidermal growth factorCell Line TumormedicineHumansHSP70 Heat-Shock ProteinsRegulation of gene expressionMultidisciplinarybiologyQCell MembraneR3. Good healthCell biologyGene Expression Regulation NeoplasticSettore BIO/18 - Genetica030104 developmental biologymedicine.anatomical_structurePhosphopyruvate HydrataseChaperone (protein)Cancer cellbiology.proteinMedicineEnolase Hsp70 protein cell surface cancer biologyIntracellularProtein Binding
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Cellular expression of connexins in the rat brain: neuronal localization, effects of kainate-induced seizures and expression in apoptotic neuronal ce…

2003

The identification of connexins (Cxs) expressed in neuronal cells represents a crucial step for understanding the direct communication between neurons and between neuron and glia. In the present work, using a double-labelling method combining in situ hybridization for Cx mRNAs with immunohistochemical detection for neuronal markers, we provide evidence that, among cerebral connexins (Cx26, Cx32, Cx36, Cx37, Cx40, Cx43, Cx45 and Cx47), only Cx45 and Cx36 mRNAs are localized in neuronal cells in both developing and adult rat brain. In order to establish whether connexin expression is influenced in vivo by abnormal neuronal activity, we examined the short-term effects of kainate-induced seizur…

MaleAgingTime FactorsgliaHippocampusConnexinbrain developmentKainate receptorApoptosisIn situ hybridizationBiologyConnexinsgap junctionbrain development; gap junction; gliaSeizuresTubulinmedicineExcitatory Amino Acid AgonistsIn Situ Nick-End LabelingPremovement neuronal activityAnimalsRNA MessengerOrganic ChemicalsRats WistarIn Situ HybridizationFluorescent DyesNeuronsMessenger RNAKainic AcidReverse Transcriptase Polymerase Chain ReactionGeneral NeuroscienceGap junctionBrainGene Expression Regulation DevelopmentalFluoresceinsImmunohistochemistryCell biologyRatsmedicine.anatomical_structurenervous systemAnimals NewbornPhosphopyruvate HydrataseAutoradiographysense organsNeuronNeuroscienceDensitometryThe European journal of neuroscience
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Echinostoma caproni: identification of enolase in excretory/secretory products, molecular cloning, and functional expression.

2007

In order to investigate molecules that could be involved in host-trematode relationships, we have analysed the excretory/secretory products (ESP) of Echinostoma caproni following a proteomic approach. Actin, Gluthathione S-transferase (GST) and enolase have been identified in the ESP. Enolase, observed to be one of the most abundant proteins, was further characterized. The molecular cloning and in vitro expression in Escherichia coli of E. caproni enolase allowed us to determine that the protein contains 431 amino acids and a theoretical MW of 46272 Da. E. caproni enolase shows high homology to other trematode enolases. The recombinant protein binds specifically to human plasminogen in vitr…

MaleImmunologyEnolaseBlotting WesternMolecular Sequence DataMolecular cloningBiologymedicine.disease_causeGene Expression Regulation Enzymologiclaw.inventionlawCricetinaeEchinostomamedicineAnimalsHumansElectrophoresis Gel Two-DimensionalAmino Acid SequenceCloning MolecularRats WistarEscherichia coliActinchemistry.chemical_classificationMesocricetusSequence Homology Amino AcidReverse Transcriptase Polymerase Chain ReactionPlasminogenGeneral MedicineMolecular biologyIn vitroRecombinant ProteinsAmino acidRatsInfectious DiseaseschemistryBiochemistryExcretory systemPhosphopyruvate HydrataseSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationRecombinant DNAParasitologyElectrophoresis Polyacrylamide GelSequence AlignmentExperimental parasitology
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Identification of antigenic proteins from Echinostoma caproni (Trematoda) recognized by mouse immunoglobulins M, A and G using an immunoproteomic app…

2008

Antigenic proteins of Echinostoma caproni (Trematoda) against mouse IgM, IgA, IgG, IgG1 and IgG2a were investigated by immunoproteomics. Excretory/secretory products (ESP) of E. caproni separated by two-dimensional (2D) gel electrophoresis were transferred to nitrocellulose membranes and probed with the different mouse immunoglobulin classes. A total of four proteins (enolase, 70 kDa heat-shock protein (HSP-70), actin and aldolase) were accurately identified. Enolase was recognized in eight different spots of which seven of them were detected in the expected molecular weight and were recognized by IgA, IgG or IgG and IgG1. Another spot identified as enolase at 72 kDa was only recognized by …

MaleProteomicsImmunologyEnolaseBlotting WesternImmunoglobulinsEchinostoma caproniImmunoproteomicsaldolaseMiceexcretory/secretory productsAntigenHeat shock proteinEchinostomaFructose-Bisphosphate AldolaseAnimalsSecretionElectrophoresis Gel Two-DimensionalHSP70 Heat-Shock ProteinsGel electrophoresisEchinostomiasisMice Inbred ICRbiologyAldolase Aheat-shock proteinMolecular biologyActinsenolaseBiochemistryAntigens HelminthPhosphopyruvate HydrataseSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationImmunologybiology.proteinParasitologyAntibodyactinParasite immunology
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