Search results for "Antibody opsonization"

showing 8 items of 8 documents

The Clinical Enzymology of the Complement System

1989

The complement (C) system is one of the most important humoral systems mediating many activities that contribute to inflammation and host defense, e.g. various anaphylatoxin activities, Chemotaxis and opsonization for phagocytosis. The C system is similar to other humoral systems, such as coagulation, fibrinolysis and the kinin system, a multifactoral system whose activation represents sequentially occurring multi-step activation cascades of the “classical” as well as the “alternative” pathway.

Antibody opsonizationClassical complement pathwayChemistrymedicineAnaphylatoxinChemotaxisInflammationKininComplement deficiencymedicine.symptommedicine.diseaseCell biologyComplement system
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Quantitative analysis of opsonophagocytosis and of killing of Candida albicans by human peripheral blood leukocytes by using flow cytometry

1991

We describe a simple, rapid, automated procedure for measuring opsonophagocytosis and killing of Candida albicans by human peripheral blood leukocytes. Yeast cells are labelled by allowing uptake and cleavage of membrane-permeable bis-carboxyethyl-carboxyfluorescein pentaacetoxymethylester to its membrane-impermeable fluorescent derivative bis-carboxyethyl-carboxyfluorescein. The yeast cells are added to cell-rich plasma obtained after dextran sedimentation of erythrocytes. Opsonophagocytosis and killing are quantified by using automated fluorescent cell analysis, and the following parameters can be obtained: (i) relative percentage of phagocytes that participate in opsonophagocytosis, (ii)…

Cytotoxicity ImmunologicMicrobiology (medical)Phagocytemedicine.drug_classPhagocytosisIn Vitro TechniquesMonoclonal antibodyMicrobiologyFlow cytometryPhagocytosisCandida albicansLeukocytesmedicineHumansCandida albicansPhagocytesbiologymedicine.diagnostic_testOpsonin ProteinsFlow Cytometrybiology.organism_classificationMolecular biologyYeastCorpus albicansAntibody opsonizationmedicine.anatomical_structureEvaluation Studies as TopicResearch ArticleJournal of Clinical Microbiology
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Digestive vacuole of Plasmodium falciparum released during erythrocyte rupture dually activates complement and coagulation.

2012

Abstract Severe Plasmodium falciparum malaria evolves through the interplay among capillary sequestration of parasitized erythrocytes, deregulated inflammatory responses, and hemostasis dysfunction. After rupture, each parasitized erythrocyte releases not only infective merozoites, but also the digestive vacuole (DV), a membrane-bounded organelle containing the malaria pigment hemozoin. In the present study, we report that the intact organelle, but not isolated hemozoin, dually activates the alternative complement and the intrinsic clotting pathway. Procoagulant activity is destroyed by phospholipase C treatment, indicating a critical role of phospholipid head groups exposed at the DV surfa…

HemeproteinsMalePain ThresholdErythrocytesImmunologyComplement Pathway AlternativePlasmodium falciparumVacuoleBiochemistryHemolysisMonocytesMicrobiologyHypesthesiaRats Sprague-DawleyPhagocytosisparasitic diseasesAnimalsHumansMalaria FalciparumBlood CoagulationLungbiologyPhospholipase CHemozoinDextran SulfatePlasmodium falciparumCell BiologyHematologyIntracellular Membranesbiology.organism_classificationComplement systemRatsAntibody opsonizationImmunologyVacuolesAlternative complement pathwaySpleenWaste disposalBlood
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Secreted proteophosphoglycan of Leishmania mexicana amastigotes activates complement by triggering the mannan binding lectin pathway.

1997

Cutaneous lesions induced by infection of mice with the protozoan parasite, Leishmania mexicana, contain abundant amounts of a high molecular mass proteophosphoglycan (PPG), which is secreted by the amastigote stage residing in phagolysosomes of macrophages and can then be released into the tissue upon rupture of the infected cells. Amastigote PPG forms sausage-shaped but soluble particles and belongs to a novel class of serine-rich proteins that are extensively O-glycosylated by phosphooligosaccharides capped by mannooligosaccharides. The purified molecule is shown here to efficiently activate complement (C) and deplete hemolytic activity of normal serum and may prevent the opsonization of…

ImmunologyLeishmania mexicanaProtozoan ProteinsCollectinLeishmaniasis CutaneousLeishmania mexicanaMiceImmunology and AllergyAnimalsAmastigoteComplement ActivationMannan-binding lectinSerine proteaseMice KnockoutbiologyMacrophagesComplement C4Complement C3biology.organism_classificationCollectinsComplement systemAntibody opsonizationBiochemistryLectin pathwaybiology.proteinMice Inbred CBACalciumProteoglycansCarrier ProteinsEuropean journal of immunology
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Flow cytometric assay for quantifying opsonophagocytosis and killing of Staphylococcus aureus by peripheral blood leukocytes.

1992

We describe a novel flow cytometric method for quantifying opsonophagocytosis and killing of Staphylococcus aureus in cell-rich plasma obtained after dextran sedimentation of erythrocytes. To analyze opsonophagocytosis, phagocytes were labeled with a phycoerythrin-conjugated monoclonal antibody and were incubated with viable staphylococci containing carboxyfluorescein as a vital fluorescent dye. Phagocytosing cells assumed a dual, orange-green fluorescence. The relative numbers of bacteria associating with phagocytes could be determined by quantifying the decrease of free green fluorescent particles. A parallel incubation of fluorescent bacteria with unlabeled cell-rich plasma was performed…

Microbiology (medical)PhagocytePhagocytosisStaphylococcusmedicine.disease_causeMicrobiologyFlow cytometrychemistry.chemical_compoundPhagocytosismedicineLeukocytesHumansFluoresceinbiologymedicine.diagnostic_testAntibodies MonoclonalPhycoerythrinOpsonin ProteinsFlow CytometryFluoresceinsAntibody opsonizationKineticsmedicine.anatomical_structureSpectrometry FluorescencechemistryStaphylococcus aureusbiology.proteinAntibodyStaphylococcusResearch ArticleJournal of clinical microbiology
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Primary structure and opsonic activity of an F-lectin from serum of the gilt head breamSparus aurata(Pisces, Sparidae)

2012

Abstract The recently described fucose-binding agglutinin from the European eel revealed a novel lectin fold (the ‘F-type’ fold) that is shared with other carbohydrate-binding proteins and proteins from prokaryotes to vertebrates clustered under the newly established F-type lectin (FTL) family. We previously reported the purification and biochemical characterization of a fucose-binding protein (FBP) isolated from serum of the gilt head bream (Sparus aurata, SauFBP). In the present article, the complete coding sequence of SauFBP revealed that it is a member of the FTL family, consisting of two tandem carbohydrate recognition domains (CRD) that display the F-type sequence motif. In vitro opso…

Protein primary structureLectinBiologymedicine.disease_causeMolecular biologyFucoseAntibody opsonizationchemistry.chemical_compoundAgglutininchemistryImmunologymedicinebiology.proteinAnimal Science and ZoologySequence motifOpsoninEscherichia coliItalian Journal of Zoology
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Immune Thrombocytopenia: Recent Advances in Pathogenesis and Treatments

2021

Immune thrombocytopenia (ITP) is a rare autoimmune disease due to both a peripheral destruction of platelets and an inappropriate bone marrow production. Although the primary triggering factors of ITP remain unknown, a loss of immune tolerance—mostly represented by a regulatory T-cell defect—allows T follicular helper cells to stimulate autoreactive splenic B cells that differentiate into antiplatelet antibody-producing plasma cells. Glycoprotein IIb/IIIa is the main target of antiplatelet antibodies leading to platelet phagocytosis by splenic macrophages, through interactions with Fc gamma receptors (FcγRs) and complement receptors. This allows macrophages to activate autoreactive T cells …

biologybusiness.industryReviewHematologyComplement receptorAntibody opsonizationClassical complement pathwayImmune systemhemic and lymphatic diseasesImmunologybiology.proteinCytotoxic T cellMedicineDiseases of the blood and blood-forming organsPlateletRC633-647.5AntibodybusinessThrombopoietinHemaSphere
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The Inflammatory Feed-Forward Loop Triggered by the Complement Component C3 as a Potential Target in Endometriosis

2021

Copyright © 2021 Agostinis, Zorzet, Balduit, Zito, Mangogna, Macor, Romano, Toffoli, Belmonte, Morello, Martorana, Borelli, Ricci, Kishore and Bulla. The complement system is a major component of humoral innate immunity, acting as a first line of defense against microbes via opsonization and lysis of pathogens. However, novel roles of the complement system in inflammatory and immunological processes, including in cancer, are emerging. Endometriosis (EM), a benign disease characterized by ectopic endometrial implants, shows certain unique features of cancer, such as the capacity to invade surrounding tissues, and in severe cases, metastatic properties. A defective immune surveillance against…

endometriosisTHP-1 CellsTNF-amast cellsPeritoneal DiseasesCell DegranulationEndometriumImmunology and AllergyOriginal ResearchMice Knockoutmedicine.diagnostic_testendometriosiComplement C3Hep G2 CellsAntibody opsonizationmedicine.anatomical_structureComplement C3aTumor necrosis factor alphaFemaleInflammation MediatorsSignal TransductionImmunologyBiologySettore MED/08 - Anatomia PatologicaImmunofluorescencePeritoneal cavityPeritoneummedicineAnimalsHumansSettore MED/05 - Patologia ClinicaC3complement system...Innate immune systemTumor Necrosis Factor-alphaPeritoneal fluidC3; endometriosis; mast cells; complement system; TNF-aRC581-607Coculture TechniquesImmunity InnateComplement systemImmunity HumoralMice Inbred C57BLDisease Models AnimalCase-Control StudiesTNF-αCancer researchPeritoneal DiseaseImmunologic diseases. Allergymast cell
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