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CD16 and CR3 receptors distinguish between the two mechanisms of tumour cytotoxicity in neutrophils
Author(s) -
Gavioli Riccardo,
Spisani Susanna,
Giuliani Anna Lisa,
Risso Angela,
Traniello Serena
Publication year - 1991
Publication title -
british journal of haematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.907
H-Index - 186
eISSN - 1365-2141
pISSN - 0007-1048
DOI - 10.1111/j.1365-2141.1991.tb04518.x
Subject(s) - cd16 , cytotoxicity , cytolysis , lysis , lytic cycle , receptor , antibody , k562 cells , chemistry , biology , microbiology and biotechnology , in vitro , immunology , biochemistry , antigen , cd3 , virus , cd8
Summary Previous studies have suggested that phorbol ester‐activated neutrophils kill both antibody non‐coated and antibody‐coated K562 target cells. In this report the contribution of the receptors FcγIII (CD16) and CR3 (CD11b/CD18) in the lytic process was investigated. In neutrophils CD16 and CR3 are up‐regulated by the phorbol ester up to 4 and 10 times, respectively. As expected, lysis of non‐immunized K562 targets is not affected by the treatment of neutrophils with anti CD16, AB8.28, whereas lysis of immunized targets is decreased by 50%. In addition, the interaction of CD16 and AB8.28 induces calcium mobilization and increases granule secretion. Surprisingly, the simultaneous binding of AB8.28 and anti‐CR3 0KM1 to neutrophils completely abolishes the lysis of antibody‐coated targets. Unlike CD16, CR3 does not possess a functional role and binding of 0KM1 to CR3 does not affect cytotoxicity of immunized K562 targets, but it blocks lysis of non‐coated target almost completely, indicating a function as adhesion protein for CR3. These studies demonstrate a distinct role of CD16 and CR3 in mediating antibody‐dependent and antibody‐independent cellular cytotoxicity, respectively.