Abstract
Abstract Eosinophils attach themselves closely to large non-phagocytosable, antibody-coated targets, such as helminths, and release their granule contents directly on to the surface of the target. A model system has been developed in which human peripheral blood eosinophils flatten down and degranulate on to antibody-coated agar layers, which are too large to be phagocytosed. The agar layer contains tetanus toxoid antigen and the eosinophil chemotactic factor ala-glyser-glu (10 −6 M), and is coated with human antitetanus immunoglobulin. Changes in the organization of the eosinophil membrane proteins were detected by lactoperoxidase catalysed iodination. A protein of molecular weight 55,000 appeared at the cell surface as an early and specific consequence of interaction with antibody coated non-phagocytosable targets. The appearance of this protein preceded degranulation. A second protein of molecular weight 58,000, was seen when no chemotactic factor was present. In the complete system this protein may be blocked by the chemotactic factor. The role of these proteins in the attachment of eosinophils to antibody-coated targets is discussed.
Published Version
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