Search results for "Cell Surface"

showing 10 items of 201 documents

A Synthetic MUC1 Anticancer Vaccine Containing Mannose Ligands for Targeting Macrophages and Dendritic Cells

2017

A MUC1 anticancer vaccine equipped with covalently linked divalent mannose ligands was found to improve the antigen uptake and presentation by targeting mannose-receptor-positive macrophages and dendritic cells. It induced much stronger specific IgG immune responses in mice than the non-mannosylated reference vaccine. Mannose coupling also led to increased numbers of macrophages, dendritic cells, and CD4+ T cells in the local lymph organs. Comparison of di- and tetravalent mannose ligands revealed an increased binding of the tetravalent version, suggesting that higher valency improves binding to the mannose receptor. The mannose-coupled vaccine and the non-mannosylated reference vaccine ind…

CD4-Positive T-Lymphocytes0301 basic medicinemedicine.medical_treatmentMannoseEnzyme-Linked Immunosorbent AssayReceptors Cell SurfaceLigands010402 general chemistryCancer Vaccines01 natural sciencesBiochemistryDivalentMice03 medical and health scienceschemistry.chemical_compoundImmune systemCancer immunotherapyDrug DiscoverymedicineAnimalsHumansLectins C-TypeGeneral Pharmacology Toxicology and PharmaceuticsMUC1Pharmacologychemistry.chemical_classificationMice Inbred BALB CbiologyChemistryMacrophagesMucin-1Organic ChemistryDendritic CellsMolecular biology0104 chemical sciencesMannose-Binding Lectins030104 developmental biologyLymphatic systemImmunoglobulin GImmunologyMCF-7 Cellsbiology.proteinMolecular MedicineLymph NodesAntibodyMannoseMannose ReceptorMannose receptorProtein BindingChemMedChem
researchProduct

Glycoprotein 96-activated dendritic cells induce a CD8-biased T cell response.

2005

Heat shock proteins (Hsps) are able to induce protective immune responses against pathogens and tumors after injection into immunocompetent hosts. The activation of components of the adaptive immune system, including cytotoxic T lymphocytes specific for pathogen- or tumor-derived peptides, is crucial for the establishment of immuno- protection. Hsps acquire these peptides during intracellular protein degradation and when released during necrotic cell death, facilitate their uptake and Minor Histocompatibility Complex (MHC)-restricted representation by professional antigen-presenting cells (APCs). In addition, the interaction of Hsps with APCs, including the Endoplasmatic Reticulum (ER)-resi…

CD4-Positive T-LymphocytesLipopolysaccharidesAntigen-Presenting CellsBone Marrow CellsMice TransgenicReceptors Cell SurfaceBiologyCD8-Positive T-LymphocytesMajor histocompatibility complexLymphocyte ActivationBiochemistryMiceImmune systemHeat shock proteinCytotoxic T cellAnimalsHumansAntigen-presenting cellCells CulturedMembrane GlycoproteinsToll-Like ReceptorsCell DifferentiationCell BiologyDendritic cellDendritic CellsOriginal ArticlesAcquired immune systemLymphocyte SubsetsCell biologyMice Inbred C57BLToll-Like Receptor 4biology.proteinInflammation MediatorsCD8Signal TransductionCell stresschaperones
researchProduct

A trifunctional dextran-based nanovaccine targets and activates murine dendritic cells, and induces potent cellular and humoral immune responses in v…

2013

Dendritic cells (DCs) constitute an attractive target for specific delivery of nanovaccines for immunotherapeutic applications. Here we tested nano-sized dextran (DEX) particles to serve as a DC-addressing nanocarrier platform. Non-functionalized DEX particles had no immunomodulatory effect on bone marrow (BM)-derived murine DCs in vitro. However, when adsorbed with ovalbumine (OVA), DEX particles were efficiently engulfed by BM-DCs in a mannose receptor-dependent manner. A DEX-based nanovaccine containing OVA and lipopolysaccharide (LPS) as a DC stimulus induced strong OVA peptide-specific CD4(+) and CD8(+) T cell proliferation both in vitro and upon systemic application in mice, as well a…

CD4-Positive T-LymphocytesLipopolysaccharidesOvalbumin610 Medizinlcsh:MedicineBone Marrow CellsReceptors Cell SurfaceCD8-Positive T-LymphocytesMiceTh2 Cells610 Medical sciencesAnimalsLectins C-Typelcsh:ScienceCell ProliferationImmunity CellularVaccineslcsh:RDextransDendritic CellsImmunity HumoralMannose-Binding LectinsNanoparticleslcsh:QAdsorptionMannose ReceptorResearch ArticlePLoS ONE
researchProduct

Protein kinase CK2 enables regulatory T cells to suppress excessive TH2 responses in vivo

2014

The quality of the adaptive immune response depends on the differentiation of distinct CD4(+) helper T cell subsets, and the magnitude of an immune response is controlled by CD4(+)Foxp3(+) regulatory T cells (Treg cells). However, how a tissue- and cell type-specific suppressor program of Treg cells is mechanistically orchestrated has remained largely unexplored. Through the use of Treg cell-specific gene targeting, we found that the suppression of allergic immune responses in the lungs mediated by T helper type 2 (TH2) cells was dependent on the activity of the protein kinase CK2. Genetic ablation of the β-subunit of CK2 specifically in Treg cells resulted in the proliferation of a hithert…

CD4-Positive T-LymphocytesMaleT cellImmunologyMice TransgenicReceptors Cell Surfacechemical and pharmacologic phenomenaCell Growth ProcessesT-Lymphocytes RegulatoryCell LineMiceTh2 CellsImmune systemHypersensitivitymedicineAnimalsHumansImmunology and AllergyIL-2 receptorCasein Kinase IIMice Inbred BALB CChemistryPeripheral toleranceFOXP3Cell DifferentiationForkhead Transcription FactorsDendritic CellsAcquired immune systemCell biologyMice Inbred C57BLmedicine.anatomical_structureCell cultureInterferon Regulatory FactorsImmunologyLeukocytes MononuclearIRF4Nature Immunology
researchProduct

β-Catenin Signaling Drives Differentiation and Proinflammatory Function of IRF8-Dependent Dendritic Cells

2014

Abstract β-Catenin signaling has recently been tied to the emergence of tolerogenic dendritic cells (DCs). In this article, we demonstrate a novel role for β-catenin in directing DC subset development through IFN regulatory factor 8 (IRF8) activation. We found that splenic DC precursors express β-catenin, and DCs from mice with CD11c-specific constitutive β-catenin activation upregulated IRF8 through targeting of the Irf8 promoter, leading to in vivo expansion of IRF8-dependent CD8α+, plasmacytoid, and CD103+CD11b− DCs. β-Catenin–stabilized CD8α+ DCs secreted elevated IL-12 upon in vitro microbial stimulation, and pharmacological β-catenin inhibition blocked this response in wild-type cells…

CD8 AntigensCellular differentiationImmunologyReceptors Cell SurfaceVaccinia virusPyrimidinonesCD8-Positive T-LymphocytesBiologyParasite LoadArticleProinflammatory cytokineMiceAntigens CDVacciniaAnimalsImmunology and AllergyPromoter Regions Geneticbeta CateninInflammationMice KnockoutCell DifferentiationDendritic CellsT lymphocyteTh1 CellsBridged Bicyclo Compounds HeterocyclicInterleukin-12CD11c AntigenCell biologyEnzyme ActivationMice Inbred C57BLInterferon Regulatory FactorsInterleukin 12FemaleIRF8Signal transductionIntegrin alpha ChainsToxoplasmaSpleenToxoplasmosisCD8Signal TransductionInterferon regulatory factorsThe Journal of Immunology
researchProduct

Efficient Targeting of Protein Antigen to the Dendritic Cell Receptor DEC-205 in the Steady State Leads to Antigen Presentation on Major Histocompati…

2002

To identify endocytic receptors that allow dendritic cells (DCs) to capture and present antigens on major histocompatibility complex (MHC) class I products in vivo, we evaluated DEC-205, which is abundant on DCs in lymphoid tissues. Ovalbumin (OVA) protein, when chemically coupled to monoclonal alphaDEC-205 antibody, was presented by CD11c+ lymph node DCs, but not by CD11c- cells, to OVA-specific, CD4+ and CD8+ T cells. Receptor-mediated presentation was at least 400 times more efficient than unconjugated OVA and, for MHC class I, the DCs had to express transporter of antigenic peptides (TAP) transporters. When alphaDEC-205:OVA was injected subcutaneously, OVA protein was identified over a …

CD8-Positive T-LymphocytesMice0302 clinical medicineImmunology and AllergyCytotoxic T cellMice KnockoutAntigen Presentation0303 health sciencesMembrane GlycoproteinstoleranceAntibodies MonoclonalDEC-205 receptorrespiratory systemFlow CytometryEndocytosismedicine.anatomical_structureMHC class IFemaleOvalbuminT cellImmunologyAntigen presentationReceptors Cell Surfacechemical and pharmacologic phenomenaBiologyMajor histocompatibility complexArticleMinor Histocompatibility Antigens03 medical and health sciencesAntigenAntigens CDMHC class IImmune TolerancemedicineAnimalsLectins C-Typedendritic cellsAntigensCD40 Antigens030304 developmental biologyHistocompatibility Antigens Class IDendritic cellMolecular biologyCD11c AntigenMice Inbred C57BLCD8 T cellbiology.proteinLymph NodesCarrier ProteinsCD8030215 immunologyJournal of Experimental Medicine
researchProduct

Dual regulation of SPI1/PU.1 transcription factor by heat shock factor 1 (HSF1) during macrophage differentiation of monocytes

2014

International audience; : In addition to their cytoprotective role in stressful conditions, heat shock proteins (HSPs) are involved in specific differentiation pathways, e.g. we have identified a role for HSP90 in macrophage differentiation of human peripheral blood monocytes exposed to Macrophage Colony-Stimulating Factor (M-CSF). Here, we show that deletion of the main transcription factor involved in heat shock gene regulation, heat shock factor 1 (HSF1), affects M-CSF-driven differentiation of mouse bone marrow cells. HSF1 transiently accumulates in the nucleus of human monocytes undergoing macrophage differentiation, including M-CSF-treated peripheral blood monocytes and phorbol ester-…

Cancer ResearchCellular differentiation[SDV]Life Sciences [q-bio][SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Mice0302 clinical medicineHeat Shock Transcription FactorsHSF1[SDV.BDD]Life Sciences [q-bio]/Development BiologyCells CulturedComputingMilieux_MISCELLANEOUSRegulation of gene expression0303 health sciencesMice Inbred BALB C[SDV.MHEP.HEM]Life Sciences [q-bio]/Human health and pathology/HematologyHematology[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biomolecules [q-bio.BM]3. Good healthDNA-Binding ProteinsOncology030220 oncology & carcinogenesismonocytesProteasome Endopeptidase ComplexAntigens Differentiation MyelomonocyticReceptors Cell Surface[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiology03 medical and health sciencesAntigens CDHeat shock proteinProto-Oncogene Proteinstranscription factorsAnimalsHumans[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology[ SDV.BDD ] Life Sciences [q-bio]/Development BiologyTranscription factor030304 developmental biologySPI1Macrophagesheat-shock proteinsfungi[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular biologyMolecular biologyHsp70Heat shock factorMice Inbred C57BLcell differentiationGene Expression RegulationTrans-Activators[SDV.MHEP]Life Sciences [q-bio]/Human health and pathology
researchProduct

Detection of the DCC gene product in normal and malignant colorectal tissues and its relation to a codon 201 mutation.

1998

Protein expression of the putative tumour-suppressor gene DCC on chromosome 18q was evaluated in a panel of 16 matched colorectal cancer and normal colonic tissue samples together with DCC mRNA expression and allelic deletions (loss of heterozygosity, LOH). Determined by a polymerase chain reaction (PCR)-LOH assay, 12 of the 16 (75%) cases were informative with LOH occurring in 2 of the 12 cases. For DCC mRNA, transcripts could be detected in all analysed normal tissues (eight out of eight) by RT-PCR, whereas 6 of the 15 tumours were negative. DCC protein expression, investigated by immunohistochemistry using the monoclonal antibody 15041 A directed against the intracellular domain, was hom…

Cancer ResearchDeleted in Colorectal CancerDNA Mutational AnalysisLoss of HeterozygosityReceptors Cell SurfaceBiologymedicine.disease_causePolymerase Chain ReactionLoss of heterozygosityGene productmedicineHumansGenes Tumor SuppressorRNA MessengerRNA NeoplasmCodonGeneMessenger RNAMutationTumor Suppressor ProteinsfungiDCC ReceptorImmunohistochemistryNeoplasm ProteinsBlotting SouthernOncologyCancer researchImmunohistochemistryColorectal NeoplasmsCell Adhesion MoleculesImmunostainingResearch ArticleBritish Journal of Cancer
researchProduct

Late steps of parvoviral infection induce changes in cell morphology.

2008

Previously, virus-induced non-filopodial extensions have not been encountered in connection with viral infections. Here, we report emergence of long extensions protruding from Norden laboratory feline kidney (NLFK) and A72 (canine fibroma) cells infected with canine parvovirus for 72 h. These extensions significantly differ in length and number from those appearing in control cells. The most striking feature in the extensions is the length, reaching up to 130 microm, almost twice the average length of a healthy NLFK cell. In A72 cells, the extensions were even longer, up to 200 microm. The results presented here also suggest that the events leading to the growth of these extensions start ea…

Cancer ResearchMorphology (linguistics)biologyParvovirus CanineCellCanine parvovirusmedicine.diseasebiology.organism_classificationVirologyVirusCell LineParvoviridae InfectionsInfectious Diseasesmedicine.anatomical_structureDogsVirologymedicineCatsAnimalsAbnormal extensionCell Surface ExtensionsDog DiseasesFibromaCell ShapeVirus research
researchProduct

The protease complex consisting of dipeptidyl peptidase IV and seprase plays a role in the migration and invasion of human endothelial cells in colla…

2006

Abstract Dipeptidyl peptidase IV (DPP4/CD26) and seprase/fibroblast activation protein α are homologous type II transmembrane, homodimeric glycoproteins that exhibit unique prolyl peptidase activities. Human DPP4 is ubiquitously expressed in epithelial and endothelial cells and serves multiple functions in cleaving the penultimate positioned prolyl bonds at the NH2 terminus of a variety of physiologically important peptides in the circulation. Recent studies showed a linkage between DPP4 and down-regulation of certain chemokines and mitogenic growth factors, and degradation of denatured collagens (gelatin), suggesting a role of DPP4 in the cell invasive phenotype. Here, we found the existen…

Cancer ResearchProteasesDipeptidyl Peptidase 4medicine.medical_treatmentBiologyArticleDipeptidyl peptidaseExtracellular matrixFibroblast activation protein alphaCell MovementmedicineHumansSerine proteaseProteaseSerine EndopeptidasesAntibodies MonoclonalEndothelial CellsCell migrationdipeptidyl peptidase IV CD26 seprase fibroblast activation protein α endothelial cell migration angiogenesisExtracellular MatrixUp-RegulationEndothelial stem cellOncologyBiochemistrybiology.proteinGelatinCell Surface ExtensionsCollagenPeptide Hydrolases
researchProduct