Search results for " lectins"

showing 8 items of 48 documents

Transgenic overexpression of corticotropin releasing hormone provides partial protection against neurodegeneration in an in vivo model of acute excit…

2008

Abstract Corticotropin releasing hormone (CRH) is the central modulator of the mammalian hypothalamic–pituitary–adrenal (HPA) axis. In addition, CRH affects other processes in the brain including learning, memory, and synaptic plasticity. Moreover, CRH has been shown to play a role in nerve cell survival under apoptotic conditions and to serve as an endogenous neuroprotectant in vitro . Employing mice overexpressing murine CRH in the CNS, we observed a differential response of CRH-overexpressing mice (CRH-COE hom -Nes) to acute excitotoxic stress induced by kainate compared with controls (CRH-COE con -Nes). Interestingly, CRH-overexpression reduced the duration of epileptic seizures and pre…

endocrine systemmedicine.medical_specialtyIndolesRNA UntranslatedCorticotropin-Releasing HormoneExcitotoxicityMice TransgenicNerve Tissue ProteinsBiologymedicine.disease_causeNeuroprotectionHippocampusNestinCorticotropin-releasing hormoneMiceIntermediate Filament ProteinsNeurotrophic factorsNeurofilament ProteinsSeizuresInternal medicineGlial Fibrillary Acidic Proteinpolycyclic compoundsmedicineExcitatory Amino Acid AgonistsReaction TimeAnimalsNeuroinflammationBrain-derived neurotrophic factorAnalysis of VarianceKainic AcidCell DeathGeneral NeuroscienceBrain-Derived Neurotrophic FactorNeurodegenerationProteinsLong-term potentiationmedicine.diseaseDisease Models AnimalEndocrinologynervous systemGene Expression RegulationNerve DegenerationNeurotoxicity SyndromesPlant Lectinshormones hormone substitutes and hormone antagonistsNeuroscience
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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 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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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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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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Separated hemocyte populations from the ascidian Ciona intestinalis contain and release in vitro opsonizingCa++-independent and β-galactoside specifi…

2007

opsonizationhemocytehemocyte lectinhemagglutinins: β-galactosidetunicatephagocytosiβ-galactosides; phagocytosis; opsonization; hemocytes; tunicates; Ciona intestinalis [hemocyte lectins; hemagglutinins]Ciona intestinalis
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