Search results for "Mannose"

showing 10 items of 96 documents

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
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Inhibition of human immunodeficiency virus-1 infection by human conglutinin-like protein: in vitro studies.

1992

The lectin-like protein analogous to bovine conglutinin was purified from human serum. The carbohydrate-binding ability of conglutinin-like protein was inhibited by D-mannose, N-acetylglucosamine and L-fucose as well as by mannan-containing oligosaccharides. By applying a lectin-based ELISA system it was demonstrated that conglutinin-like protein binds to human immunodeficiency virus-1 (HIV-1) glycoprotein 120 (gp120) via its carbohydrate binding site. In vitro experiments with T-lymphoblastoid CEM cells revealed that conglutinin-like protein abolishes infection by HIV-1; a 50% cytoprotective concentration of 23.9 micrograms/ml was measured. These findings demonstrate that human conglutinin…

Cancer ResearchMolecular Sequence DataCarbohydratesImmunoglobulinsEnzyme-Linked Immunosorbent AssayHIV Envelope Protein gp120Mannose-Binding LectinVirusChromatography AffinityArticleViral ProteinsConglutininProtein A/GHumansImmunoconglutininsBinding siteKey wordsConglutinin‐like proteinchemistry.chemical_classificationAcquired Immunodeficiency SyndromebiologyHIV‐1Immunization PassiveLectinMolecular biologyMannanIn vitrogp120OncologychemistryCarbohydrate Sequencebiology.proteinHIV-1Protein GGlycoproteinCarrier ProteinsLectinJapanese journal of cancer research : Gann
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Evidence for a selective and electroneutral K+/H+-exchange in Saccharomyces cerevisiae using plasma membrane vesicles

1996

The existence of a K+/H+ transport system in plasma membrane vesicles from Saccharomyces cerevisiae is demonstrated using fluorimetric monitoring of proton fluxes across vesicles (ACMA fluorescence quenching). Plasma membrane vesicles used for this study were obtained by a purification/reconstitution protocol based on differential and discontinuous sucrose gradient centrifugations followed by an octylglucoside dilution/gel filtration procedure. This method produces a high percentage of tightly-sealed inside-out plasma membrane vesicles. In these vesicles, the K+/H+ transport system, which is able to catalyse both K+ influx and efflux, is mainly driven by the K+ transmembrane gradient and ca…

Cell Membrane Permeability[SDV]Life Sciences [q-bio]Coated VesiclesCoated vesicleBiological Transport ActiveBioengineeringSaccharomyces cerevisiaeBiologyH(+)-K(+)-Exchanging ATPaseApplied Microbiology and BiotechnologyBiochemistryMembrane PotentialsCell membraneElectron Transport Complex IVH(+)-K(+)-Exchanging ATPasealpha-MannosidaseMannosidasesGeneticsmedicineCentrifugation Density GradientNa+/K+-ATPaseComputingMilieux_MISCELLANEOUSMembrane potentialVesicleCell MembraneDithiazanineElectron Transport Complex IVIsoxazolesHydrogen-Ion ConcentrationMembranemedicine.anatomical_structureSpectrometry Fluorescence[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyBiochemistryBiophysicsChromatography GelPotassiumProtonsMannoseBiotechnology
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Uridine enhances the cytotoxic effect of D-glucosamine in rat C6 glioma cells.

1986

This paper studies the influence of uridine on the effects exerted by D-glucosamine in rat C6 glioma cells. 2 mM uridine increased markedly both the cytotoxic effect of the aminosugar and the inhibition of thymidine incorporation into acid-insoluble fraction. Furthermore the complete resumption of the capacity to incorporate either 3H-thymidine or 3H-mannose which was observed after the removal of the aminosugar, was impeded when the cells were treated contemporaneously with D-glucosamine and uridine. An exposure for 4 hr to 20 mM glucosamine alone enhanced about 15-fold the cellular pool of UDP-N-acetylhexosamines; the addition of 2 mM uridine intensified the expansion of this pool, which …

Cell SurvivalBiologyC6 gliomaGeneral Biochemistry Genetics and Molecular BiologyCell Linechemistry.chemical_compoundGlucosamineGliomamedicineCytotoxic T cellAnimalsGeneral Pharmacology Toxicology and PharmaceuticsCytotoxicityUridineGlucosamineUridine Diphosphate N-AcetylglucosamineDrug SynergismGeneral MedicineGliomamedicine.diseaseMolecular biologyUridineIn vitroRatsBiochemistrychemistryAminosugarcytotoxic effectMannoseThymidineLife sciences
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Binding and activation of human and mouse complement by Cryptosporidium parvum (Apicomplexa) and susceptibility of C1q- and MBL-deficient mice to inf…

2008

Cryptosporidium parvum is a protozoan parasite (Apicomplexa) that causes gastrointestinal disease in animals and humans. Whereas immunocompetent hosts can limit the infection within 1 or 2 weeks, immunocompromised individuals develop a chronic, life-threatening disease. The importance of the adaptive cellular immune response, with CD4+ T-lymphocytes being the major players, has been clearly demonstrated. Several non-adaptive immune mechanisms have been suggested to contribute to the host defence, such as interferon-gamma (IFN-gamma) from NK cells, certain chemokines, beta-defensins and pro-inflammatory cytokines, but the influence of the complement systems has been less well studied. We ana…

ChemokineImmunologyProtozoan ProteinsCryptosporidiosisComplement factor ISodium ChlorideMannose-Binding LectinMicrobiologyMiceImmune systemmedicineAnimalsHumansRNA MessengerMolecular BiologyComplement ActivationImmunodeficiencyMannan-binding lectinCryptosporidium parvumbiologyReverse Transcriptase Polymerase Chain ReactionComplement C1qOocystsTemperaturemedicine.diseasebiology.organism_classificationVirologyComplement systemMice Inbred C57BLCryptosporidium parvumGene Expression RegulationLectin pathwayComplement C3bbiology.proteinCattleDisease SusceptibilityMolecular immunology
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The human gene for mannan-binding lectin-associated serine protease-2 (MASP-2), the effector component of the lectin route of complement activation, …

2001

The proteases of the lectin pathway of complement activation, MASP-1 and MASP-2, are encoded by two separate genes. The MASP1 gene is located on chromosome 3q27, the MASP2 gene on chromosome 1p36.23-31. The genes for the classical complement activation pathway proteases, C1r and C1s, are linked on chromosome 12p13. We have shown that the MASP2 gene encodes two gene products, the 76 kDa MASP-2 serine protease and a plasma protein of 19 kDa, termed MAp19 or sMAP. Both gene products are components of the lectin pathway activation complex. We present the complete primary structure of the human MASP2 gene and the tight cluster that this locus forms with non-complement genes. A comparison of the …

Chromosomes Artificial BacterialTranscription GeneticGenetic LinkageRNA SplicingImmunologyMolecular Sequence DataBiologyGeneticsHumansPromoter Regions GeneticComplement ActivationGenetics (clinical)Mannan-binding lectinGeneticsComplement component 2Base SequenceCD69Serine EndopeptidasesC4AChromosome MappingCollectinsKLRB1Chromosomes Human Pair 1Lectin pathwayMannose-Binding Protein-Associated Serine ProteasesMultigene Familybiology.proteinCarrier ProteinsMASP2MASP1
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Inhalable Formulation Based on Lipid–Polymer Hybrid Nanoparticles for the Macrophage Targeted Delivery of Roflumilast

2022

Here, novel lipid-polymer hybrid nanoparticles (LPHNPs), targeted to lung macrophages, were realized as potential carriers for Roflumilast administration in the management of chronic obstructive pulmonary disease (COPD). To achieve this, Roflumilast-loaded fluorescent polymeric nanoparticles, based on a polyaspartamide-polycaprolactone graft copolymer, and lipid vesicles, made from 1,2-dipalmitoyl-sn-glycero-3-phosphocholine and 1,2-distearoyl-sn-glycero-phosphoethanolamine-N-(polyethylene glycol)-mannose, were properly combined using a two-step method, successfully obtaining Roflumilast-loaded hybrid fluorescent nanoparticles (Man-LPHFNPs@Roflumilast). These exhibit colloidal size and a ne…

CyclopropanesPolymers and PlasticsPolymersMacrophagesPhosphatidylethanolaminesAminopyridinesBioengineeringPolyethylene GlycolsBiomaterialsSettore CHIM/09 - Farmaceutico Tecnologico ApplicativoBenzamidesMaterials ChemistryHumansNanoparticlesParticle SizeMannoseBiomacromolecules
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Selective targeting of avidin/mannose 6-phosphate receptor chimeras to early or late endosomes

2000

Summary In this study we have used the Semliki forest virus expression system to transiently express chimeric proteins that contain transmembrane and cytoplasmic domains of the cation-independent mannose 6-phosphate receptor (CI-MPR) fused to chicken avidin. Immunofluorescence and electron microscopy studies showed that the chimeric protein with the entire cytoplasmic domain of CI-MPR was transported to late endosomes, where it accumulated. We made use of the biotin-binding capacity of lumenal avidin, and found that, in agreement with this distribution, the chimeric protein could be labelled with biotinylated HRP endocytosed for a long, but not a brief, period of time. However, truncation o…

CytoplasmTime FactorsHistologyEndosomeRecombinant Fusion ProteinsAmino Acid MotifsGreen Fluorescent ProteinsEndosomesEndocytosisReceptor IGF Type 2Pathology and Forensic Medicine03 medical and health sciencesCationsCricetinaeAnimalsBiotinylation030304 developmental biologyProtein Synthesis Inhibitors0303 health sciencesBrefeldin AMannose 6-phosphate receptorbiologyCell Membrane030302 biochemistry & molecular biologyPovidoneBiological TransportCell BiologyGeneral MedicineAvidinSilicon DioxideSemliki forest virusFusion proteinMolecular biologyEndocytosisTransmembrane proteinProtein Structure TertiaryLuminescent ProteinsMicroscopy ElectronTransmembrane domainCross-Linking ReagentsMicroscopy FluorescenceBiotinylationbiology.proteinCattleChickensDimerizationAvidinEuropean Journal of Cell Biology
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A D-mannose-specific lectin from Gerardia savaglia that inhibits nucleocytoplasmic transport of mRNA.

1987

A new lectin has been isolated from the coral Gerardia savaglia by affinity chromatography, using locust gum as an absorbent, and D-mannose as eluant. Final purification was achieved by Bio-Gel P300 gel filtration. The agglutinin is a protein composed of two polypeptide chains with a Mr of 14800; the two subunits are not linked by disulfide bond(s). The isoelectric point is 4.8, the amino acid composition is rich in the acidic amino acids aspartic acid and glutamic acid. The absorption maximum for the protein was at 276 nm; with a molar absorption coefficient of 1.27 X 10(5) M-1 cm-1. The lectin precipitated erythrocytes from humans (A, B and O), sheep, rabbit and carp with a titer between …

ElectrophoresisPore complexCytoplasmChemical PhenomenaMacromolecular SubstancesMannoseMitosisBiochemistryChromatography Affinity03 medical and health scienceschemistry.chemical_compoundCnidariaMiceAgglutininAffinity chromatographyLectinsAnimalsLymphocytesRNA MessengerAmino Acids030304 developmental biologyGlycoproteinsCell Nucleus0303 health sciencesbiologyChemistry Physical030302 biochemistry & molecular biologyLectinNuclear ProteinsHemagglutination Inhibition TestsNuclear matrixMolecular biologyMolecular WeightIsoelectric pointBiochemistrychemistryConcanavalin Abiology.proteinMannoseEuropean journal of biochemistry
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N-Glycosylation modification of proteins is an early marker of the enterocytic differentiation process of HT-29 cells

1990

International audience; The human colon cancer cell line HT-29 remains totally undifferentiated when glucose is present in the culture medium (HT-29 Glc+), while the same cells may undergo typical enterocytic differentiation after reaching confluence when grown in glucose-deprived medium (HT-29 Glc-). Recently, we demonstrated a deficiency in the overall N-glycan processing in confluent undifferentiated cells, whereas differentiated cells follow a classical pattern of N-glycosylation. The main changes in N-glycosylation observed in confluent undifferentiated cells may be summarised as follows: 1) the conversion of high mannose into complex glycopeptides is greatly decreased; 2) this decreas…

EmbryologyGlycosylationGrowth phaseCellular differentiationMedicine (miscellaneous)macromolecular substancesBiology03 medical and health sciences0302 clinical medicineN-linked glycosylationPolysaccharides[ CHIM.ORGA ] Chemical Sciences/Organic chemistry[SDV.BDD] Life Sciences [q-bio]/Development BiologyTumor Cells CulturedHumansProcess (anatomy)[SDV.BDLR] Life Sciences [q-bio]/Reproductive Biology030304 developmental biologychemistry.chemical_classification0303 health sciences[CHIM.ORGA]Chemical Sciences/Organic chemistryProteinsCell Differentiation[CHIM.ORGA] Chemical Sciences/Organic chemistryGlycopeptideIntestinescarbohydrates (lipids)Human colon cancer[SDV.AEN] Life Sciences [q-bio]/Food and NutritionGlucoseReproductive MedicineBiochemistrychemistryCell culture030220 oncology & carcinogenesisColonic Neoplasmslipids (amino acids peptides and proteins)Animal Science and ZoologyGlycoproteinMannoseCell DivisionDevelopmental BiologyFood Science
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