Search results for "Cebus"

showing 10 items of 124 documents

Cloning and characterization of the promoter of Hugl-2, the human homologue of Drosophila lethal giant larvae (lgl) polarity gene.

2007

The human lgl gene, Hugl-2 (llgl2, Lgl2), codes for a cytoskeletal protein involved in regulating cell polarity. Here, we report the identification and functional characterization of the promoter region ( approximately 1.2kb) of the Hugl-2 gene. Luciferase expression assays show a high basal Hugl-2 promoter activity in different cell lines and primary human hepatocytes. Truncations of the promoter identified a GC-rich region important for this activity. Alignment of human and mouse genomic sequences demonstrate that this is an evolutionary conserved region fcontaining putative binding sites for several transcription factors including Elk-1 and Sp-1. Mithramycin A reduces Hugl-2 expression i…

Sp1 Transcription FactorMolecular Sequence DataBiophysicsDown-RegulationGenes InsectBiologyBiochemistryCell LineDownregulation and upregulationEpidermal growth factorCell polarityChlorocebus aethiopsAnimalsDrosophila ProteinsHumansLuciferaseCloning MolecularPromoter Regions GeneticMolecular BiologyGeneTranscription factorBase PairingBase SequenceEpidermal Growth FactorSequence Homology Amino AcidTumor Suppressor ProteinsCell PolarityPromoterCell BiologyMolecular biologyCytoskeletal ProteinsDrosophila melanogasterCell cultureCOS CellsSequence AlignmentBiochemical and biophysical research communications
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Elimination of a bacterial pore-forming toxin by sequential endocytosis and exocytosis

2008

Staphylococcus aureus alpha-toxin is the archetype of bacterial pore forming toxins and a key virulence factor secreted by the majority of clinical isolates of S. aureus. Toxin monomers bind to target cells and oligomerize to form small beta-barrel pores in the plasma membrane. Many nucleated cells are able to repair a limited number of lesions by unknown, calcium-independent mechanisms. Here we show that cells can internalize alpha-toxin, that uptake is essential for cellular survival, and that pore-complexes are not proteolytically degraded, but returned to the extracellular milieu in the context of exosome-like structures, which we term toxosomes.

Staphylococcus aureusEndosomeBacterial ToxinsBiophysicsEndosomesBiologyEndocytosisHemolysin ProteinsBiochemistryα-ToxinExocytosisVirulence factorExocytosisCell LineHemolysin ProteinsStructural BiologyNucleated cellChlorocebus aethiopsGeneticsExtracellularAnimalsHumansMolecular BiologyCell NucleusBacterial pore forming toxinPore-forming toxinInnate defence mechanismCell BiologyEndocytosisCell biologyExosomeBiochemistryCOS CellsMutationMacrolidesFEBS Letters
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Novel pathogenic mechanism of microbial metalloproteinases: liberation of membrane-anchored molecules in biologically active form exemplified by stud…

1996

Certain membrane-anchored proteins, including several cytokines and cytokine receptors, can be released into cell supernatants through the action of endogenous membrane-bound metalloproteinases. The shed molecules are then able to fulfill various biological functions; for example, soluble interleukin-6 receptor (sIL-6R) can bind to bystander cells, rendering these cells sensitive to the action of IL-6. Using IL-6R as a model substrate, we report that the metalloproteinase from Serratia marcescens mimics the action of the endogenous shedding proteinase. Treatment of human monocytes with the bacterial protease led to a rapid release of sIL-6R into the supernatant. This effect was inhibitable …

Staphylococcus aureusProteasesmedicine.medical_treatmentImmunologyBiologyMatrix metalloproteinaseMicrobiologyMonocytesSubstrate SpecificityAntigens CDChlorocebus aethiopsmedicineAnimalsHumansReceptorSerratia marcescensMetalloproteinaseProteaseMembrane ProteinsMetalloendopeptidasesBiological activityBacterial InfectionsReceptors InterleukinListeria monocytogenesReceptors Interleukin-6Recombinant ProteinsBlotInfectious DiseasesSolubilityBiochemistryPseudomonas aeruginosaParasitologySignal transductionResearch ArticleSignal TransductionInfection and Immunity
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Synthesis and antiviral activity of scopadulane-rearranged diterpenes.

2009

A new bioactive diterpene skeleton resulting from a backbone rearrangement is described. Activity of the rearranged product and several derivatives against Herpes Virus Simplex type 2 is reported.

StereochemistryvirusesHerpesvirus 2 HumanViral Plaque AssayBiologymedicine.disease_causeVirus ReplicationAntiviral AgentsViruschemistry.chemical_compoundInhibitory Concentration 50Pharmaceutical technologyVirologyChlorocebus aethiopsmedicineInhibitory concentration 50AnimalsVero CellsPharmacologyMolecular StructureTerpenoidHerpes simplex viruschemistryBiochemistryDiterpeneDiterpenesHerpes virus simplexAntiviral research
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Surface-exposed Amino Acid Residues of HPV16 L1 Protein Mediating Interaction with Cell Surface Heparan Sulfate

2007

Efficient infection of cells by human papillomaviruses (HPVs) and pseudovirions requires primary interaction with cell surface proteoglycans with apparent preference for species carrying heparan sulfate (HS) side chains. To identify residues contributing to virus/cell interaction, we performed point mutational analysis of the HPV16 major capsid protein, L1, targeting surface-exposed amino acid residues. Replacement of lysine residues 278, 356, or 361 for alanine reduced cell binding and infectivity of pseudovirions. Various combinations of these amino acid exchanges further decreased cell attachment and infectivity with residual infectivity of less than 5% for the triple mutant, suggesting …

Surface PropertiesLysinePlasma protein bindingBiochemistryAntibodieschemistry.chemical_compoundCapsidChlorocebus aethiopsAnimalsHumansComputer SimulationMolecular Biologychemistry.chemical_classificationAlanineInfectivityHeparinLysineCell MembraneCapsomereOncogene Proteins ViralCell BiologyHeparan sulfateAmino acidchemistryBiochemistryCapsidMutagenesisCOS CellsCapsid ProteinsHeparitin SulfateProtein BindingJournal of Biological Chemistry
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Evidence for a multistep mechanism for cell-cell fusion by herpes simplex virus with mutations in the syn 3 locus using heparin derivatives during fu…

1994

Addition of heparin-Na+ as well as related substances of high and intermediate MW (Arteparon and polyanion SP54) 3 h after infection inhibit fusion from within (FFWI) induced by HSV strains with mutations in the syn 3 locus only. The concentration of heparin-Na+ required to inhibit FFWI is 10-fold higher (1 mg/ml) than that needed to inhibit adsorption. Instead of fusion, cell rounding is observed. The effect is readily reversible. A low MW heparin disaccharide is ineffective. Neomycin, at a concentration of 8 mM, inhibits FFWI induced by all HSV-1 but not HSV-2 strains, whereas adsorption is inhibited at 3 mM. We conclude from our observations that cell-cell fusion (FFWI) induced by syn 3 …

SyncytiumCell fusionHeparinCellMutantGeneral MedicineBiologyGiant CellsVirologyCell membranemedicine.anatomical_structureMutagenesisCell cultureCell surface receptorVirologyChlorocebus aethiopsmedicineVero cellAnimalsSimplexvirusVero CellsCells CulturedArchives of Virology
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Pigment epithelium-derived factor is a niche signal for neural stem cell renewal.

2006

Adult stem cells are characterized by self-renewal and multilineage differentiation, and these properties seem to be regulated by signals from adjacent differentiated cell types and by extracellular matrix molecules, which collectively define the stem cell "niche." Self-renewal is essential for the lifelong persistence of stem cells, but its regulation is poorly understood. In the mammalian brain, neurogenesis persists in two germinal areas, the subventricular zone (SVZ) and the hippocampus, where continuous postnatal neuronal production seems to be supported by neural stem cells (NSCs). Here we show that pigment epithelium-derived factor (PEDF) is secreted by components of the murine SVZ a…

TelencephalonCellular differentiationSubventricular zoneBiologyHippocampusMicePEDFEpendymaLateral VentriclesChlorocebus aethiopsmedicineAnimalsHumansNerve Growth FactorsEye ProteinsCells CulturedSerpinsCell ProliferationInjections IntraventricularNeuronsNeuronal PlasticityGeneral NeuroscienceStem CellsNeurogenesisCell CycleCell DifferentiationNeural stem cellmedicine.anatomical_structurenervous systemCOS CellsEndothelium VascularStem cellNeuroscienceCell DivisionAstrocyteAdult stem cellSignal TransductionNature neuroscience
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Differential vesicular targeting and time course of synaptic secretion of the mammalian neurotrophins.

2005

Neurotrophins are a family of secreted neuronal survival and plasticity factors comprising NGF, BDNF, neurotrophin-3 (NT-3), and NT-4. Whereas synaptic secretion of BDNF has been described, the routes of intracellular targeting and secretion of NGF, NT-3, and NT-4 in neurons are poorly understood.To allow for a direct comparison of intracellular targeting and release properties, all four mammalian neurotrophins were expressed as green fluorescent protein fusion proteins in cultured rat hippocampal neurons. We show that BDNF and NT-3 are targeted more efficiently to dendritic secretory granules of the regulated pathway of secretion (BDNF, in 98% of cells; NT-3, 85%) than NGF (46%) and NT-4 (…

Time FactorsDevelopment/Plasticity/RepairBiologyHippocampal formationHippocampusPC12 CellsPostsynaptic potentialChlorocebus aethiopsAnimalsHumansSecretionNerve Growth FactorsCells CulturedGeneral NeuroscienceConstitutive secretory pathwaySynapsinFusion proteinCell biologyRatsnervous systemCOS CellsSynapsesbiology.proteinSynaptic VesiclesIntracellularNeurotrophinThe Journal of neuroscience : the official journal of the Society for Neuroscience
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Asymptomatic vaginal herpes simplex virus infections in mice: virology and pathohistology

1996

One of the causes of genital tract infections in humans are herpes simplex virus types 1 and 2 (HSV-1, HSV-2). Although primary and recurrent infections can be clinically apparent and in part very serious, many infections are asymptomatic and result only in temporary genital shedding of virus (recurrences). During our investigations of vaginitis, strain IES of HSV-1 produced an asymptomatic infection. Replication in the murine vaginal (vag.) epithelium as well as antibody formation after vag. infection was comparable to those of survivors after infection with highly virulent strains. Titration of liver, spleen, ovaries, adrenal glands spinal cord, or brain after vag. IES infection revealed …

Time FactorsvirusesVirulenceEnzyme-Linked Immunosorbent AssayBiologyAntibodies ViralVirus Replicationmedicine.disease_causeAsymptomaticEpitheliumVirusHerpesviridaeImmunoenzyme TechniquesMiceSpecies SpecificityVirologyAlphaherpesvirinaeChlorocebus aethiopsmedicineAnimalsSimplexvirusVaginitisAntigens ViralVero CellsIn Situ HybridizationVaginitisMice Inbred BALB CHerpes GenitalisVirulenceGeneral Medicinebiology.organism_classificationmedicine.diseaseVirologymedicine.anatomical_structureHerpes simplex virusOrgan SpecificityDNA ViralVaginaVaginaFemalemedicine.symptomArchives of Virology
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The Kelch protein NS1-BP interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control

2007

Alpha-enolase is a key glycolytic enzyme that plays a functional role in several physiological processes depending on the cellular localization. The enzyme is mainly localized in the cytoplasm whereas an alternative translated form, named MBP-1, is predominantly nuclear. The MBP-1 protein has been characterized as a c-Myc promoter binding protein that negatively controls transcription. In the present study, we identified the kelch protein NS1-BP as one of the alpha-enolase/MBP-1 partners by using a yeast two-hybrid screening. Although NS1-BP has been originally described as a protein mainly localized in the nucleus, we provide evidence that NS1-BP also interacts with actin in human cells, a…

Transcription GeneticTranscription FactorGlycolysiAlpha-enolaseKelch proteinsRNA-Binding ProteinHeLa CellChlorocebus aethiopsTranscriptional regulationPromoter Regions GeneticCellular localizationNuclear ProteinbiologyNuclear ProteinsRNA-Binding ProteinsCell biologyDNA-Binding ProteinsProtein TransportCOS CellsYeast two-hybrid assayGlycolysisHumanProtein BindingSubcellular FractionsImmunoprecipitationDNA-Binding ProteinTwo-hybrid screeningEnolaseChlorocebus aethiopProto-Oncogene Proteins c-mycCOS CellBiomarkers TumorAnimalsHumansKelch proteinMolecular BiologyActinTumor Suppressor ProteinAnimalTumor Suppressor ProteinsBinding proteinc-Myc transcriptionCell BiologyMolecular biologyActinsKelch proteinSubcellular FractionSettore BIO/18 - GeneticaGene Expression RegulationCytoplasmPhosphopyruvate Hydratasebiology.proteinHeLa CellsTranscription FactorsBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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