Mechanisms of red cell destruction mediated by non-complement binding IgG antibodies: the essential role in vivo of the Fc part of IgG.
F(ab')2G anti-D was prepared by limited digestion of IgG anti-D with pepsin. Conditions of digestion were chosen in order to obtain a nearly complete conversion of the anti-D antibody molecules as tested by immunochemical and serological techniques. The F(ab')2G anti-D was not capable of inducing adherence of rhesus D positive red cells to monocytes in vitro or of eliminating such cells in vivo in normal volunteers. These findings are compatible with a role of the Fc-receptor-mediated adherence to cells of the macrophage system in vivo in the destruction of erythrocytes by non-complement binding IgG antibodies.
D002470:Cell Survival; D004912:Erythrocytes / Q000276:immunology*; D006801:Humans; D007122:Immunoelectrophoresis; D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D007158:Immunologic Techniques; D007518:Isoantibodies; D009000:Monocytes / Q000276:immunology; D010434:Pepsin A; D012204:Rh-Hr Blood-Group System
D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D007518:Isoantibodies; D012204:Rh-Hr Blood-Group System; D010434:Pepsin A