Effect of cytochalasin B on human monocyte binding and sphering of IgG-coated human erythrocytes.
The ability of human mononuclear phagocytic cells to bind IgG-coated human erythrocytes (EA) and to cause bound EA to become osmotically fragile (sphered) was investigated in the presence of cytochalasin B, a known inhibitor of phagocytosis. Cytochalasin B inhibited the binding of EA to mononuclear cells in a dose-dependent fashion; 80% inhibition of binding was observed at a concentration of 5 mug/ml. This profound effect on EA binding together with presently available data suggested a role for IgG receptor mobility in the macrophage binding of IgG-coated erythrocytes. Cytochalasin B, however, had a minimal effect on the capacity of mononuclear cells to sphere adherent EA, suggesting that the processes involved in macrophage-induced spherocytosis may differ from those operable in phagocytosis.
D002448:Cell Adhesion / Q000187:drug effects; D003571:Cytochalasin B / Q000494:pharmacology*; D004913:Erythrocytes, Abnormal / Q000276:immunology*; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism*; D009000:Monocytes / Q000378:metabolism; D009996:Osmotic Fragility / Q000187:drug effects; D011955:Receptors, Drug / Q000187:drug effects; D013102:Spherocytes / Q000276:immunology*; D013997:Time Factors
D007074:Immunoglobulin G; D011955:Receptors, Drug; D003571:Cytochalasin B