title: Receptor expression and functional status of cultured human eosinophils derived from umbilical cord blood mononuclear cells.
abstract: Selective use of recombinant human cytokines has enabled the culture of large numbers of eosinophils from human cord blood mononuclear cells, raising the possibility of their use as a model of eosinophil function. Cultured eosinophils (CE) were compared with normal-density peripheral blood eosinophils (PBE) in terms of their membrane receptor expression and function. Fc gamma R and CR1 expression of CE and PBE was similar. In contrast, the specific mean fluorescence for LFA-1 alpha, p150,95 alpha, ICAM-1, and HLA-DR was significantly elevated for CE compared with PBE. CE responded in PAF-induced chemotaxis in a similar fashion to PBE. CE gave higher numbers of both resting and platelet activating factor (PAF)-stimulated immunoglobulin G (IgG)- and C3b-dependent rosettes than PBE. CE and PBE had comparable capacity to kill IgG- and C-opsonized schistosomula in terms of both baseline values and PAF-induced enhancement of cytotoxicity. Baseline adherence by CE and PBE to plasma-coated glass was essentially the same, but stimulated adhesion (PAF) of CE was lower. Compared with PBE, CE generated less than half the amounts of extracellular and cell-associated PAF induced by calcium ionophore A23187 stimulation. Unlike PBE, CE did not generate PAF after exposure to IgG-coated Sepharose particles. CE stimulated with IgG-coated beads generated small quantities of LTC4, while A23187 stimulation resulted in approximately half the LTC4 levels observed with PBE. The total cell content of eosinophil peroxidase (EPO) was similar for CE and PBE. These data suggest that although CE and PBE have many phenotypic and functional properties in common there are quantitative differences that may be a consequence of their immaturity and/or the influence of the cytokines used in their culture.
authors.affiliation: Department of Allergy and Clinical Immunology, National Heart and Lung Institute, London, UK.
authors.forename: G M
authors.initials: GM
authors.lastname: Walsh
authors.forename: A
authors.initials: A
authors.lastname: Hartnell
authors.forename: R
authors.initials: R
authors.lastname: Moqbel
authors.forename: O
authors.initials: O
authors.lastname: Cromwell
authors.forename: L
authors.initials: L
authors.lastname: Nagy
authors.forename: B
authors.initials: B
authors.lastname: Bradley
authors.forename: T
authors.initials: T
authors.lastname: Furitsu
authors.forename: T
authors.initials: T
authors.lastname: Ishizaka
authors.forename: A B
authors.initials: AB
authors.lastname: Kay
mesh_terms: D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D000943:Antigens, Differentiation / Q000276:immunology / Q000502:physiology; D015815:Cell Adhesion Molecules / Q000276:immunology / Q000502:physiology; D002455:Cell Division / Q000187:drug effects; D002465:Cell Movement / Q000187:drug effects; D002478:Cells, Cultured; D002633:Chemotaxis / Q000276:immunology / Q000502:physiology; D015923:Complement C1r / Q000276:immunology / Q000502:physiology; D015926:Complement C3a / Q000276:immunology / Q000502:physiology; D004804:Eosinophils / Q000166:cytology* / Q000502:physiology / Q000648:ultrastructure; D005312:Fetal Blood / Q000166:cytology*; D005434:Flow Cytometry; D006684:HLA-DR Antigens / Q000276:immunology / Q000502:physiology; D006801:Humans; D007141:Immunoglobulin Fc Fragments / Q000276:immunology / Q000502:physiology; D007074:Immunoglobulin G / Q000276:immunology / Q000502:physiology; D007142:Immunoglobulin gamma-Chains / Q000276:immunology / Q000502:physiology; D016167:Integrin alphaXbeta2; D018799:Intercellular Adhesion Molecule-1; D016169:Lymphocyte Function-Associated Antigen-1; D010972:Platelet Activating Factor / Q000494:pharmacology; D011948:Receptors, Antigen, T-Cell / Q000276:immunology / Q000502:physiology; D016693:Receptors, Antigen, T-Cell, alpha-beta; D011956:Receptors, Cell Surface / Q000276:immunology* / Q000502:physiology; D016028:Receptors, Leukocyte-Adhesion / Q000276:immunology / Q000502:physiology; D012397:Rosette Formation; D013189:SRS-A / Q000494:pharmacology; D012550:Schistosoma mansoni / Q000276:immunology
chemical_list: D000911:Antibodies, Monoclonal; D000943:Antigens, Differentiation; D015815:Cell Adhesion Molecules; D006684:HLA-DR Antigens; D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D007142:Immunoglobulin gamma-Chains; D016167:Integrin alphaXbeta2; D016169:Lymphocyte Function-Associated Antigen-1; D010972:Platelet Activating Factor; D011948:Receptors, Antigen, T-Cell; D016693:Receptors, Antigen, T-Cell, alpha-beta; D011956:Receptors, Cell Surface; D016028:Receptors, Leukocyte-Adhesion; D013189:SRS-A; D018799:Intercellular Adhesion Molecule-1; D015926:Complement C3a; D015923:Complement C1r