Search results for "Plant Lectins"

showing 10 items of 15 documents

Glycoprotein and ganglioside changes in human trophoblasts after exposure to pulsed doppler ultrasound

1995

Changes in glycoprotein and ganglioside composition in human trophoblasts (eighth week of gestation) after in vitro exposure to pulsed Doppler ultrasound (pulse duration 1.22 microseconds; repetition frequency 11.1 kHz; center frequency 4 MHz; ISPPA = 175.5 W/cm2; ISPTA = 0.59 W/cm2) were investigated. Evacuated trophoblasts were divided in two halves and insonated for 10 min on top of a 6-cm layer of 5% gelatin in 50-mL tubes (Falcon) at 37 degrees C. One half of each trophoblast was sham insonated and served as an internal control. After insonation trophoblasts were maintained at 37 degrees C for 24 h. Glycoproteins were detected using alpha-D-mannose specific lectins from Galanthus nival…

Acoustics and UltrasonicsImmunoblottingBiophysicsMannoseG(M2) Gangliosidechemistry.chemical_compoundGangliosidesLectinsmedicineG(M3) GangliosideHumansRadiology Nuclear Medicine and imagingGlycoproteinschemistry.chemical_classificationMembrane GlycoproteinsGangliosideGalanthusRadiological and Ultrasound TechnologybiologyChemistryTrophoblastLectinMolecular biologyN-Acetylneuraminic AcidTrophoblastsMolecular WeightMembrane glycoproteinsglycoproteins; gangliosides; lectins; pulsed doppler ultrasoundmedicine.anatomical_structureUltrasonography Doppler PulsedG(M2) GangliosideImmunologySialic Acidsbiology.proteinElectrophoresis Polyacrylamide GelChromatography Thin LayerPlant LectinsGlycoproteinMannoseN-Acetylneuraminic acid
researchProduct

Isolated hevein-like domains, but not 31-kd endochitinases, are responsible for IgE-mediated in vitro and in vivo reactions in latex-fruit syndrome.

2005

Background Individuals with natural rubber latex allergy often have immediate reactions to plant-derived foods and fresh fruits, such as avocado and banana. IgE of these patients has been shown to bind endochitinases containing an N-terminal hevein-like domain (HLD). However, evidence on 31-kd endochitinase-induced reactions in vivo is lacking. Objective We sought to assess the clinical significance of 31-kd endochitinases and isolated HLDs in latex-fruit syndrome. Methods The 31-kd endochitinases and corresponding HLDs were purified or produced from avocado, banana, latex, and wheat germ. Skin prick test reactivities against purified proteins were examined in 15 patients with natural rubbe…

AdultMaleLatexImmunologyMolecular Sequence DataEnzyme-Linked Immunosorbent Assaymedicine.disease_causeImmunoglobulin ECross-reactivityMicrobiology03 medical and health sciences0302 clinical medicineFood allergyChitin bindingLatex HypersensitivitymedicineImmunology and AllergyHumansAmino Acid Sequence030304 developmental biologyDNA PrimersSkin Tests0303 health sciencesbiologySequence Homology Amino AcidChemistryPerseaChitinasesfood and beveragesMusaAllergensImmunoglobulin EMiddle Agedmedicine.diseaseIn vitroWheat germ agglutinin3. Good healthProtein Structure Tertiary030228 respiratory systemSpectrometry Mass Matrix-Assisted Laser Desorption-IonizationImmunologybiology.proteinFemaleAntibodyPlant LectinsAnaphylaxisFood HypersensitivityAntimicrobial Cationic PeptidesThe Journal of allergy and clinical immunology
researchProduct

Sulphoevernan, a polyanionic polysaccharide, and the narcissus lectin potently inhibit human immunodeficiency virus infection by binding to viral env…

1990

Sulphoevernan is a sulphated alpha-1----3, 1----4 polyglucan (Mr 20,000) with a helical structure. This compound effectively inhibits both human immunodeficiency virus type 1 (HIV-1) and type 2 infection of cells in vitro at concentrations around 0.5 micrograms/ml. Moreover, the compound completely inhibits HIV-1-induced syncytium formation at a concentration of 1 microgram/ml. Competition experiments with 35S-labelled sulphoevernan revealed that the mannose-specific lectin from Narcissus pseudonarcissus prevented binding of sulphoevernan to HIV-1, whereas the antibody OKT4A did not reduce the amount of sulphoevernan bound to MT-2 cells. These data indicate that the non-cytotoxic polymer su…

Antiviral AgentsVirusCell LineViral envelopeViral Envelope ProteinsIn vivoPolysaccharidesVirologyLectinsMurine leukemia virusHumansGlucansSyncytiumbiologyLectinbiology.organism_classificationVirologyIn vitroHIV-2biology.proteinHIV-1AntibodyPlant LectinsZidovudineCell DivisionProtein BindingThe Journal of general virology
researchProduct

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
researchProduct

Expression of the transcription factor Pax6 in the adult rat dentate gyrus

2005

The transcription factor Pax 6 is expressed in precursor cells during embryonic CNS development, and it plays an important role in the regulation of cell proliferation and neuronal fate determination. Pax 6-expressing cells are also present in the adult hippocampal dentate gyrus and subventricular zone/rostral migratory stream, regions in which neuronal precursors exist during adult life. In the adult dentate gyrus, precursor cells are located in the innermost portion of the granule cell layer, and Pax 6-expressing nuclei are most abundant in this region. To examine the putative role of Pax 6 in adult hippocampal neurogenesis, we have studied the proliferative activity, distribution, and ph…

Doublecortin Domain ProteinsMalePAX6 Transcription FactorAntimetabolitesGreen Fluorescent ProteinsSubventricular zoneNerve Tissue ProteinsHippocampal formationBiologyNestinRats Sprague-DawleyCellular and Molecular NeuroscienceIntermediate Filament ProteinsGlial Fibrillary Acidic ProteinBasic Helix-Loop-Helix Transcription FactorsmedicineAnimalsPaired Box Transcription FactorsEye ProteinsCell ProliferationHomeodomain ProteinsNeuronsStem CellsDentate gyrusNeuropeptidesNeurogenesisGranule cellImmunohistochemistryRatsRepressor ProteinsNeuroepithelial cellNeuropoiesismedicine.anatomical_structureBromodeoxyuridinenervous systemDentate GyrusPAX6Plant LectinsMicrotubule-Associated ProteinsNeuroscienceJournal of Neuroscience Research
researchProduct

Avidin Is a Promising Tag for Fusion Proteins Produced in Baculovirus-Infected Insect Cells

1999

The baculovirus expression vector system (BEVS) has become one of the most versatile and powerful eukaryotic systems for recombinant protein expression. We have constructed a novel baculovirus transfer vector (pbacAVs+C) which allows for the efficient production, detection, and single-step purification of the desired molecule as a secretion-compatible avidin fusion protein in insect cells. It also enables fast construction of the baculoviruses by site-specific transposition in Escherichia coli. To demonstrate the power of this vector, we report here on the production of immunologically intact hevein, a major cysteine-rich latex allergen, as avidin fusion protein. Our results indicate that a…

EnteropeptidaseStreptavidinRecombinant Fusion ProteinsGenetic VectorsMolecular Sequence DataGene ExpressionSpodopteramedicine.disease_causeCell Linelaw.invention03 medical and health scienceschemistry.chemical_compoundlawLectinsmedicineAnimalsAmino Acid SequenceEscherichia coliPeptide sequenceDNA PrimersPlant Proteins030304 developmental biology0303 health sciencesBinding SitesBase Sequencebiology030302 biochemistry & molecular biologyAvidinFusion proteinMolecular biologyEnteropeptidasechemistryBiochemistryCell culturebiology.proteinRecombinant DNAPlant LectinsBaculoviridaeAntimicrobial Cationic PeptidesPlasmidsBiotechnologyAvidinProtein Expression and Purification
researchProduct

Effects of neuron-specific ADAM10 modulation in an in vivo model of acute excitotoxic stress.

2008

A disintegrin and metalloprotease (ADAM) 10 is the main candidate enzyme for the alpha-secretase processing of the amyloid precursor protein (APP). Neuron-specific ADAM10 overexpression proved beneficial in the APP[V717I] mutant Alzheimer mouse model [Postina R, Schroeder A, Dewachter I, Bohl J, Schmitt U, Kojro E, Prinzen C, Endres K, Hiemke C, Blessing M, Flamez P, Dequenne A, Godaux E, van Leuven F, Fahrenholz F (2004) A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model. J Clin Invest 113:1456-1464]. Since Alzheimer patients have a high prevalence for epileptic seizures, we investigated the effects of ADAM10 modula…

Genetically modified mousemedicine.medical_specialtyIndolesADAM10TransgeneExcitotoxicityMice Transgenicmedicine.disease_causeNeuroprotectionHippocampusADAM10 ProteinAmyloid beta-Protein PrecursorMiceLeucineSeizuresStress PhysiologicalInternal medicineGlial Fibrillary Acidic ProteinmedicineAmyloid precursor proteinAnimalsNeuroinflammationNeuronsAnalysis of VarianceKainic AcidbiologyCell DeathDose-Response Relationship DrugChemistryGeneral NeuroscienceNeurodegenerationMembrane ProteinsValinemedicine.diseaseADAM ProteinsDisease Models AnimalEndocrinologyGene Expression RegulationMutationbiology.proteinAmyloid Precursor Protein SecretasesPlant LectinsNeuroscienceNeuroscience
researchProduct

The Major Conformational IgE-binding Epitopes of Hevein (Hev b6.02) Are Identified by a Novel Chimera-based Allergen Epitope Mapping Strategy

2002

A novel approach to localize and reconstruct conformational IgE-binding epitope regions of hevein (Hev b6.02), a major natural rubber latex allergen, is described. An antimicrobial protein (AMP) from the amaranth Amaranthus caudatus was used as an immunologically non-IgE-binding adaptor molecule to which terminal or central parts of hevein were fused. Hevein and AMP share a structurally identical core region but have different N-terminal and C-terminal regions. Only 1 of 16 hevein-allergic patients showed weak IgE binding to purified native or recombinant AMP. Chimeric AMP with the hevein N terminus was recognized by IgE from 14 (88%) patients, and chimeric AMP with the hevein C terminus wa…

MaleModels MolecularProtein ConformationImmunoglobulin Emedicine.disease_causeBiochemistryEpitopelaw.inventionEpitopes0302 clinical medicineAllergenlawLectinsPlant Proteins0303 health sciencesbiologyMiddle Aged3. Good healthDatabases as TopicBiochemistryRecombinant DNAFemalePlant LectinsProtein BindingAdultPeptide BiosynthesisAdolescentRecombinant Fusion ProteinsEnzyme-Linked Immunosorbent Assay03 medical and health sciencesChimera (genetics)medicineAnimalsHumansMolecular BiologyAged030304 developmental biologyDose-Response Relationship DrugC-terminusCell BiologyAllergensImmunoglobulin EMolecular biologyAdenosine MonophosphateProtein Structure TertiaryN-terminusEpitope mappingSpectrometry Mass Matrix-Assisted Laser Desorption-Ionizationbiology.proteinChickensEpitope MappingAntimicrobial Cationic Peptides030215 immunologyJournal of Biological Chemistry
researchProduct

Construction of hevein (Hev b 6.02) with reduced allergenicity for immunotherapy of latex allergy by comutation of six amino acid residues on the con…

2004

Abstract Recently we have established that IgE Abs bind to conformational epitopes in the N- and C-terminal regions of the major natural rubber latex allergen, hevein (Hev b 6.02). To identify the critical amino acid residues that interact with IgE, the hevein sequence was scanned by using site-specific mutations. Twenty-nine hevein mutants were designed and produced by a baculovirus expression system in insect cells and tested by IgE inhibition-ELISA using sera from 26 latex allergic patients. Six potential IgE-interacting residues of hevein (Arg5, Lys10, Glu29, Tyr30, His35, and Gln38) were identified and characterized further in detail. Based on these six residues, two triple mutants (HΔ…

MaleModels MolecularProtein ConformationMutantImmunoglobulin Emedicine.disease_causeEpitopelaw.inventionEpitopes0302 clinical medicineProtein structureAllergenlawImmunology and AllergyCombinatorial Chemistry TechniquesChild0303 health sciencesbiologyChemistryMiddle AgedRecombinant Proteins3. Good healthBiochemistryLatex allergyRecombinant DNAFemalePlant LectinsProtein BindingAdultAdolescentImmunologyMutagenesis (molecular biology technique)Binding Competitive03 medical and health sciencesLatex HypersensitivitymedicineHumansPoint Mutation030304 developmental biologyAgedAllergensImmunoglobulin Emedicine.disease030228 respiratory systemAmino Acid SubstitutionDesensitization Immunologicbiology.proteinMutagenesis Site-DirectedBinding Sites AntibodyAntimicrobial Cationic PeptidesJournal of immunology (Baltimore, Md. : 1950)
researchProduct

Study of nuclear and acrosomal sperm morphometry in ram using a computer-assisted sperm morphometry analysis fluorescence (CASMA-F) method.

2014

The aim of this study was to develop a new method that allows morphometric assessment of the sperm nucleus and acrosome in the ram using fluorescence microscopy and free software. The study was divided into three experiments. In the first experiment, semen smears from 20 ejaculates were fixed and labeled with a propidium iodide-pisum sativum agglutinin (PI/PSA) combination. Digital images of the sperm nucleus, acrosome, and whole sperm head were captured and analyzed using the ImageJ program. The computer-assisted sperm morphometry analysis fluorescence (CASMA-F) method used allowed the differentiation, capture, and morphometric analysis of most sperm nuclei, acrosomes, and whole heads with…

Maleendocrine systemSperm HeadSemenBiologyAndrologyFood AnimalsFluorescence microscopeImage Processing Computer-AssistedAnimalsSmall AnimalsAcrosomeFluorescent DyesSheepStaining and Labelingurogenital systemEquineOptical ImagingPeasSpermFluorescenceSpermatozoaStainingMorphometric analysisAnimal Science and ZoologyPlant LectinsPropidiumTheriogenology
researchProduct