Search results for "LECTINS"

showing 10 items of 181 documents

EVOLUTION, ADAPTATION AND IMMUNE FUNCTIONS OF FISH LECTINS

2019

Fish are equipped with a complex lectin repertoire that, like mammals, are involved almost all the immune reactions. Carbohydrate recognition and interactions mediated by lectins have been recognized involved in vertebrate innate immunity, not only for recognition of potential pathogens, but also acting in the agglutination, immobilization and other functional steps. In fish, C, F types galectins, Rhamnose-bind- ing lectin (RBL) and pentraxin have been identified in both car- tilaginous and bony fish. In addition, selectins and other genes have been found in the currently available fish genomes. On the basis of our results about F-type and RBL lectins we showed that: lectin repertoires in f…

fish lectins RBL FBL
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F-type lectin from the sea bass (Dicentrarchus labrax): purification, cDNA cloning, tissue expression and localization, and opsonic activity.

2009

Recently described biochemical and structural aspects of fucose-binding lectins from the European eel (Anguilla anguilla) and striped bass (Morone saxatilis) led to the identification of a novel lectin family ("F-type" lectins) characterized by a unique sequence motif and a characteristic structural fold. The F-type fold is shared not only with other members of this lectin family, but also with apparently unrelated proteins ranging from prokaryotes to vertebrates. Here we describe the purification, biochemical and molecular properties, and the opsonic activity of an F-type lectin (DlFBL) isolated from sea bass (Dicentrarchus labrax) serum. DlFBL exhibits two tandemly arranged carbohydrate-r…

food.ingredientDNA ComplementaryImmunoblottingAquatic ScienceChromatography AffinityBass (fish)F-type lectin; Dicentrarchus labrax;teleost;emaggluthinins opsoninfoodPhagocytosisOpsonin ProteinsComplementary DNALectinsEnvironmental ChemistryAnimalsDicentrarchus labraxRNA MessengerSea bassCloning MolecularOpsoninemaggluthinins opsoninPhylogenyteleostbiologyBase SequenceLectinGeneral MedicineOpsonin Proteinsbiology.organism_classificationMolecular biologyGene Expression RegulationImmunologybiology.proteinMacrophages PeritonealF lectin sea bass inflammationDicentrarchusBassElectrophoresis Polyacrylamide GelSequence motifF-type lectinFishshellfish immunology
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F-Type Lectins: A highly diversified family of fucose-binding proteins with a unique sequence motif and structural fold, involved in self/non-self-re…

2017

The F-type lectin (FTL) family is one of the most recent to be identified and structurally characterized. Members of the FTL family are characterized by a fucose recognition domain [F-type lectin domain (FTLD)] that displays a novel jellyroll fold (“F-type” fold) and unique carbohydrate- and calcium-binding sequence motifs. This novel lectin family comprises widely distributed proteins exhibiting single, double, or greater multiples of the FTLD, either tandemly arrayed or combined with other structurally and functionally distinct domains, yielding lectin subunits of pleiotropic properties even within a single species. Furthermore, the extraordinary variability of FTL sequences (isoforms) th…

lcsh:Immunologic diseases. Allergy0301 basic medicineGene isoformImmunologySettore BIO/05 - ZoologiaFucose bindingReviewFucoseF-type lectinsSelf/non-self-recognitionKelch motif03 medical and health scienceschemistry.chemical_compoundGene duplicationImmunology and AllergyStructural modelingGeneticsInnate immunitybiologyPhylogenetic treefucolectinsLectinGlycan recognition030104 developmental biologychemistrybiology.proteinFucose-bindingFucolectinlcsh:RC581-607Sequence motifF-type lectinF-type lectins; Fucolectins; Fucose-binding; Glycan recognition; Innate immunity; Self/non-self-recognition; Structural modeling; Immunology and Allergy; Immunology
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Immunological Markers for PML Prediction in MS Patients Treated with Natalizumab

2015

International audience; Natalizumab (NTZ), a monoclonal antibody recognizing the alpha4 integrin chain, has been approved for the treatment of active multiple sclerosis, but expose to the onset of a rare side effect, progressive multifocal leukoencephalopathy (PML). Estimating the individual risk of PML in NTZ-treated patients is a major challenge, and therapeutic strategies are mainly guided by the overall PML risk assessed by identified risk factors: JC virus (JCV) seropositivity, treatment duration (with peak incidence after 24 months), and the previous use of immunosuppressive therapies. Given that this stratification does not yet allow a precise individual prediction of PML, other pred…

lcsh:Immunologic diseases. Allergy[SDV.IMM] Life Sciences [q-bio]/ImmunologySide effectmedicine.drug_classvirusesImmunologyJC virusReview Articlerisk stratificationCD11aJC virusmultiple sclerosismedicine.disease_causeMonoclonal antibodyCD49dprogressive multifocal leukoencephalopathyNatalizumabeffector memory T-cellst effector memory cellsImmunology and AllergyMedicineselectinPMLbusiness.industryMultiple sclerosisProgressive multifocal leukoencephalopathyvirus diseasesmedicine.disease3. Good healthJCVImmunologySelectins[SDV.IMM]Life Sciences [q-bio]/Immunologylcsh:RC581-607businessmedicine.drugFrontiers in Immunology
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Monoclonal antibody TeM 106 reacts with a tonoplast intrinsic protein of 106 kDa from Brassica oleracea L

1995

A monoclonal antibody, designated TeM 106, that recognizes an intrinsic protein from the vacuole membrane (tonoplast) of cauliflower (Brassica oleracea L. var. botrytis) is described. Mice were immunized with a tonoplast fraction that had been purified from differentiating meristematic cells from the cauliflower head. Hybridomas were generated and screened by means of Enzyme Linked Immuno Sorbent Assays for differential reactivity to tonoplast over non-related proteins (bovine serum albumin). One out of 14 reactive murine clones was selected on the basis of its stability, secretory efficiency, and high affinity of the secreted antibodies. TeM 106 is an IgM which was shown by indirect immuno…

medicine.drug_classBlotting WesternFluorescent Antibody TechniqueMannoseEnzyme-Linked Immunosorbent AssayBrassicaVacuoleMonoclonal antibodyEpitopeMicechemistry.chemical_compoundAntigenAntibody SpecificityConcanavalin AmedicineAnimalsElectrophoresis Gel Two-DimensionalBovine serum albuminPlant ProteinsGel electrophoresisbiologyAntibodies MonoclonalMembrane ProteinsSerum Albumin BovineIntracellular MembranesCell BiologyMolecular biologyMolecular WeightKineticsBiochemistrychemistryVacuolesbiology.proteinElectrophoresis Polyacrylamide GelPlant LectinsAntibodyJournal of Cell Science
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Screening for inhibitors of HIV gp120-CD4 binding using an enzyme-linked immunoabsorbent assay.

1993

Binding of the HIV-1 major viral surface glycoprotein, gp120, to the major cell receptor, CD4, is essential for HIV infection of the target cell and syncytium formation. An enzyme-linked immunoassay using solid phase CD4 was used to quantitate the binding of HIV-1 gp120 to CD4, and to assess the activity and mechanism of action of putative inhibitors of that reaction. Monoclonal antibodies to the gp120 binding site on CD4 (e.g., Leu3a) blocked gp120 binding, while monoclonal antibodies to other portions of CD4 (e.g. OKT4) did not. Both aurintricarboxylic acid and sulfonated polysaccharides (e.g., dextran sulfate) blocked CD4-gp120 interactions by binding to the CD4 component. Human polyclon…

medicine.drug_classvirusesEnzyme-Linked Immunosorbent AssayHIV Envelope Protein gp120Monoclonal antibodyAntiviral Agentschemistry.chemical_compoundPolysaccharidesVirologyLectinsAurintricarboxylic acidmedicineGlycoproteinschemistry.chemical_classificationbiologyLigand binding assayvirus diseasesLectinReproducibility of ResultsMolecular biologyRecombinant ProteinsEnzymechemistryMechanism of actionPolyclonal antibodiesCD4 Antigensbiology.proteinHIV-1medicine.symptomAntibodyJournal of virological methods
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YKL-40 as a predictor of mortality after acute coronary syndrome

2020

medicine.medical_specialtyAcute coronary syndromebusiness.industryMEDLINEAdipokinemedicine.diseaseGastroenterologyAdipokinesLectinsInternal medicineInternal MedicinemedicineHumansChitinase-3-Like Protein 1Acute Coronary SyndromeChitinase-3-Like Protein 1businessPolish Archives of Internal Medicine
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CD1a+ and CD207+ cells are reduced in oral submucous fibrosis and oral squamous cell carcinoma

2019

Background The objective of this study investigated the distribution of immature dendritic cells (DCs), Langerhans cells and plasmacytoid DCs in oral submucous fibrosis (OSMF), OSMF associated with oral squamous cell carcinoma (OSMF-OSCC), oral leukoplakia (OL), and oral squamous cell carcinoma (OSCC). Material and Methods Fourteen cases of OSMF, 9 of OSMF-OSCC, 8 of OL¸ 45 of OSCC and 8 of normal epithelium were retrospectively retrieved and their diagnoses confirmed. Immunoreactions against CD1a, CD207 e CD303 were performed and the number of positive cells quantified. Results A significant decrease of CD1a+ was found in OSMF (p≤0.05), OSMF-OSCC (p ≤ 0.01), and OSCC (p ≤ 0.001) when compa…

medicine.medical_specialtyOral Submucous FibrosisGastroenterologyMalignant transformation03 medical and health sciences0302 clinical medicineImmune systemAntigenAntigens CDInternal medicinemedicineCarcinomaHumansLectins C-TypeGeneral DentistryLeukoplakiaRetrospective StudiesMouth neoplasmOral Medicine and Pathologybusiness.industryResearch030206 dentistry:CIENCIAS MÉDICAS [UNESCO]medicine.diseaseEpitheliumstomatognathic diseasesmedicine.anatomical_structureMannose-Binding LectinsOtorhinolaryngologyOral submucous fibrosisUNESCO::CIENCIAS MÉDICASCarcinoma Squamous CellSurgeryMouth NeoplasmsLeukoplakia OralbusinessMedicina Oral, Patología Oral y Cirugía Bucal
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Evaluation of waterborne exposure to heavy metals in innate immune defences present on skin mucus of gilthead seabream (Sparus aurata)

2015

Aquatic animals are continuously exposed to chemical pollutants but the effects evoked in skin surfaces, which receive the most direct contact with them, are poorly investigated. Terminal carbohydrate composition and immunological components present in skin mucus of gilthead seabream (Sparus aurata L.) specimens exposed to waterborne sublethal dosages of heavy metals [arsenic (As2O3), cadmium (CdCl2) and mercury (CH3HgCl) at 5, 5 and 0.04 μM, respectively for 2, 10 and 30 days were analysed. Moreover, the presence of a fucose binding lectin (FBL) was evaluated by western blot and the protein profiles were by SDS-PAGE and HPLC. Results showed little effects of heavy metals in the presence of…

mucosal immunity heavy metals lectins gilthead seabream (Sparus aurata).chemistry.chemical_elementAquatic ScienceBiologyMicrobiologySkin mucus Mucosal immunity Heavy metals Lectins Gilthead seabream (Sparus aurata)chemistry.chemical_compoundRandom AllocationImmune systemWestern blotMetals HeavymedicineEnvironmental ChemistryAnimalsMethylmercuryImmunity MucosalSkinchemistry.chemical_classificationCadmiumInnate immune systemmedicine.diagnostic_testAquatic animalGeneral MedicineMucusImmunity InnatePerciformesEnzymechemistryImmunologyWater Pollutants Chemical
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Aberrant glycosylation of alpha-dystroglycan causes defective binding of laminin in the muscle of chicken muscular dystrophy.

2005

Dystroglycan is a central component of dystrophin-glycoprotein complex that links extracellular matrix and cytoskeleton in skeletal muscle. Although dystrophic chicken is well established as an animal model of human muscular dystrophy, the pathomechanism leading to muscular degeneration remains unknown. We show here that glycosylation and laminin-binding activity of alpha-dystroglycan (alpha-DG) are defective in dystrophic chicken. Extensive glycan structural analysis reveals that Galbeta1-3GalNAc and GalNAc residues are increased while Siaalpha2-3Gal structure is reduced in alpha-DG of dystrophic chicken. These results implicate aberrant glycosylation of alpha-DG in the pathogenesis of mus…

musculoskeletal diseasesanimal structuresGlycosylationGlycosylationBiophysicsBiochemistryChromatography AffinityExtracellular matrixchemistry.chemical_compoundStructural BiologyLamininGeneticsDystroglycanmedicineAnimalsDystroglycanMuscular dystrophyDystrophic chickenDystroglycansMuscle SkeletalMolecular BiologybiologySkeletal muscleCell BiologyMuscular Dystrophy AnimalMuscular dystrophymedicine.diseaseMolecular biologycarbohydrates (lipids)Disease Models Animalmedicine.anatomical_structurechemistrybiology.proteinPikachurinLamininPlant LectinsITGA7ChickensProtein BindingFEBS letters
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