Search results for "LECTINS"

showing 10 items of 181 documents

TLR2 and Dectin-1 Signaling in Mouse Hematopoietic Stem and Progenitor Cells Impacts the Ability of the Antigen Presenting Cells They Produce to Acti…

2020

Microbial recognition by pattern recognition receptors (PRRs) expressed on hematopoietic stem and progenitor cells (HSPCs) not only activates myelopoiesis but also programs the function of the monocytes and macrophages they produce. For instance, changes in HSPC programming modify the ability of macrophages derived from them to produce inflammatory cytokines. While HSPCs exposed to a TLR2 agonist give rise to tolerized macrophages (lower proinflammatory cytokine production), HSPCs treated with Dectin-1 ligands produce trained macrophages (higher proinflammatory cytokine production). However, nothing is known about the impact of HSPC exposure to microbes on the function of antigen presenting…

CD4-Positive T-LymphocytesOvalbuminhematopoietic stem and progenitor cellsCD4 T cellsAntigen-Presenting CellsMice Transgenicantigen presenting cellsLymphocyte Activationinnate immune memoryProinflammatory cytokineLipopeptidesCandida albicansAnimalsTLR2Lectins C-TypeProgenitor cellAntigen-presenting celllcsh:QH301-705.5CD86CD40biologyChemistryCommunicationHistocompatibility Antigens Class IIZymosanGeneral MedicineTh1 CellsHematopoietic Stem CellsAcquired immune systemToll-Like Receptor 2Cell biologyMice Inbred C57BLlcsh:Biology (General)biology.proteinCytokinesTh17 CellsMyelopoiesisCD80Dectin-1Signal TransductionCells
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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
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Study of surface carbohydrates on isolated Golgi subfractions by fluorescent-lectin binding and flow cytometry

1995

The Golgi complex is a functionally heterogeneous subcellular structure that plays a key role in the synthesis, maturation, and sorting of newly synthesized glycoproteins. Fluorescent lectins have been used extensively to analyze surface glycoproteins by flow cytometry in whole cells and more recently in isolated subcellular organelles, such as mitochondria and chloroplasts. We report here the use of several fluorescein-isothiocyanate-conjugated lectins to detect and quantify specific surface sugars by flow cytometry on isolated elements from purified cis and trans-Golgi fractions from rat liver. Our results show that this approach may be useful to study Golgi composition and function, sinc…

CarbohydratesBiophysicsGolgi ApparatusPathology and Forensic MedicineFlow cytometrysymbols.namesakeEndocrinologyIsothiocyanatesLectinsOrganellemedicineAnimalsRats WistarFluorescent Dyeschemistry.chemical_classificationMembrane Glycoproteinsbiologymedicine.diagnostic_testIntracellular MembranesCell BiologyHematologyGolgi apparatusFlow CytometryWheat germ agglutininRatsChloroplastLiverBiochemistrychemistryConcanavalin Asymbolsbiology.proteinGlycoproteinFunction (biology)Protein BindingCytometry
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Expression patterns of complex glycoconjugates and endogenous lectins during fetal development of the viscerocranium

1999

Summary Experimental evidence suggests that carbohydrates and their corresponding receptors (endogenous lectins) decode biological information. Therefore, the expression of complex oligosaccharides — the potential ligand part of this recognition system — during chondrogenesis and osteogenesis was determined in the viscerocranium of fetal rats by mapping the staining patterns of exogenous lectins. Results were compared with the expression of bone- and/or cartilage-specific core proteins and the binding profiles of neoglycoconjugates. These synthetic tools make possible the localization of sugar-ligand-binding sites. The spatial and temporal distribution patterns of glycoconjugates were highl…

Cartilage ArticularGlycoconjugateOligosaccharidesGestational AgeMesodermRats Sprague-DawleyEmbryonic and Fetal DevelopmentOsteogenesisPregnancyLectinsAnimalsReceptorchemistry.chemical_classificationbiologyMacrophagesGriffonia simplicifoliaSkullLectinGeneral MedicineOligosaccharidebiology.organism_classificationChondrogenesisLigand (biochemistry)RatsBiochemistrychemistryViscerocraniumbiology.proteinFemalePlant LectinsAnatomyGlycoconjugatesDevelopmental BiologyAnnals of Anatomy - Anatomischer Anzeiger
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Characterization of fusion from without induced by herpes simplex virus

1991

The process of fusion from without (FFWO) induced by herpes simplex virus (HSV) was analyzed by using various inhibitors and compared to fusion from within (FFWI). The fate of certain elements of the cytoskeleton after FFWO was also investigated. Our experiments demonstrate FFWO as a very suitable system for study of early virus-cell interactions. Zn++ ions proved inhibitory for penetration whilst pretreatment of cells with Ca++ ions before infection enhanced FFWO activity. Dissociation of penetration from the fusion process itself was possible by use of Zn++ ions, low pH-treatment and antiserum on the one hand and N-ethylmaleimide and cytochalasin D on the other. Penetration itself needs o…

Cations DivalentCycloheximideBiologyVirusCell FusionCell membranechemistry.chemical_compoundSpecies SpecificityLectinsVirologymedicineAnimalsSimplexvirusProtease InhibitorsVero CellsCytoskeletonPolysaccharide-LyasesCytochalasin DCell fusionCell MembraneLipid bilayer fusionGeneral MedicineTunicamycinLipidsVirologymedicine.anatomical_structurechemistryEthylmaleimideVero cellReceptors VirusGlycoconjugatesArchives of Virology
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Multiple sclerosis patient-derived CSF induces transcriptional changes in proliferating oligodendrocyte progenitors.

2014

Background: Cerebrospinal fluid (CSF) is in contact with brain parenchyma and ventricles, and its composition might influence the cellular physiology of oligodendrocyte progenitor cells (OPCs) thereby contributing to multiple sclerosis (MS) disease pathogenesis. Objective: To identify the transcriptional changes that distinguish the transcriptional response induced in proliferating rat OPCs upon exposure to CSF from primary progressive multiple sclerosis (PPMS) or relapsing remitting multiple sclerosis (RRMS) patients and other neurological controls. Methods: We performed gene microarray analysis of OPCs exposed to CSF from neurological controls, or definitive RRMS or PPMS disease course. R…

Cell physiologyAdultPathologymedicine.medical_specialtyTranscription GeneticGalectin 3GalectinsImmunocytochemistryBiologyArticleCerebrospinal fluidMultiple Sclerosis Relapsing-RemittingNeural Stem CellsmedicineAnimalsHumansProgenitor cellCells CulturedCell ProliferationCerebrospinal FluidMultiple sclerosisBrainHuman brainBlood ProteinsMultiple Sclerosis Chronic Progressivemedicine.diseaseMicroarray AnalysisNeural stem cellOligodendrocyteRatsUp-RegulationOligodendrogliamedicine.anatomical_structureNeurologyNeurology (clinical)Multiple sclerosis (Houndmills, Basingstoke, England)
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Characterization of the trimeric, self-recognizing Geodia cydonium lectin I.

1983

A D-galactose-specific lectin I was extracted from the sponge Geodia cydonium and purified by affinity chromatography. The molecular weight of lectin I as determined by high-pressure liquid gel chromatography, was found to be 36500 +/- 1300. Disc gel electrophoresis in the presence and in the absence of sodium dodecyl sulfate showed that lectin I is a trimer composed of three different subunits (Mr: 13800, 13000 and 12200); two of the three subunits are linked by one disulfide bond. Isoelectric focusing gave a pI of 5.6 for the native molecule and a pI of 4.4 and of 7.4 for the subunits. The three subunits carry carbohydrate side chains, composed of D-galactose (94%) and of arabinose (5%). …

Chemical PhenomenaCarbohydratesBiochemistryChromatography AffinityGel permeation chromatographychemistry.chemical_compoundAffinity chromatographyLectinsAnimalsGeodiaSodium dodecyl sulfateAmino AcidsChromatography High Pressure Liquidchemistry.chemical_classificationbiologyChemistryIsoelectric focusingLectinGlycosidic bondbiology.organism_classificationPoriferaMolecular WeightChemistryBiochemistryConcanavalin Abiology.proteinEuropean journal of biochemistry
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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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IDENTIFICATION OF LECTINS IN THE KINETIDS OFTETRAHYMENA PYRIFORMIS

1997

Previously we described lectin-like molecules in the ciliate Tetrahymena pyriformis; by application of synthetic neoglycoconjugates it is now shown that T. pyriformis contains considerable amounts of both a beta-D-glucose- and a lactose-specific lectin. No evidence for the presence of alpha-D-mannose-, alpha-D-galactose- or of alpha-L-fucose-specific lectins could be obtained. The two lectins, identified in T. pyriformis, are associated with the kinetids. During cell division the lectins disappear or become masked in the fission furrow. Therefore, we assume that these lectins are involved in the organization of the distribution pattern of the kinetids during cell division perhaps due to lec…

CiliateCell divisionbiologyTetrahymena pyriformisLectinCell BiologyGeneral Medicinebiology.organism_classificationCell biologyMicroscopy FluorescenceAlbuminsLectinsDistribution patternTetrahymena pyriformisbiology.proteinAnimalsIdentification (biology)GlycoconjugatesCell DivisionFluorescein-5-isothiocyanateCell Biology International
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Different adhesins for type IV collagen on Candida albicans: identification of a lectin-like adhesin recognizing the 7S(IV) domain

2001

Adherence of the opportunistic pathogen Candida albicans to basement membrane (BM) proteins is considered a crucial step in the development of candidiasis. In this study the interactions of C. albicans yeast cells with the three main domains of type IV collagen, a major BM glycoprotein, were analysed. C. albicans adhered to the three immobilized domains by different mechanisms. Adhesion to the N-terminal cross-linking domain (7S) required the presence of divalent cations, whereas interaction with the central collagenous domain (CC) was cation-independent. Recognition of the C-terminal non-collagenous domain (NC1) was partially cation-dependent. Binding inhibition assays with the correspondi…

Collagen Type IVGlycosylationImmunoblottingOligosaccharidesBiologyMicrobiologyBasement MembraneType IV collagenOligosaccharide bindingCationsLectinsCandida albicansCell AdhesionAnimalsCandida albicanschemistry.chemical_classificationExtracellular Matrix ProteinsLectinOligosaccharidebiology.organism_classificationCorpus albicansBacterial adhesinchemistryBiochemistrybiology.proteinCattleGlycoproteinMicrobiology
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