C3b acceptors on macrophages: inhibition of Fc gamma-receptor-mediated phagocytosis by acceptor-bound C3b.
The binding of nascent human C3b (i.e. the fragment of C3 just after trypsin cleavage) to mouse peritoneal macrophages was demonstrated by immune adherence. Acceptor-bound C3b could be detected longer than 24 h on the cell membrane. The rosette formation and phagocytosis of SRBC coated with anti-SRBC rat IgG was inhibited by preincubation of the cells with C3 and trypsin (15 min, 37 degrees C). However, the phagocytosis of opsonized yeast particles was not influenced by acceptor-bound C3b, proving that C3b-C3b acceptor interaction did not alter the function of C3b-receptors. Acceptor-bound C3b on the macrophages failed to mediate phagocytosis of human 0,Rh+ red cells having C3b-receptors.
D000818:Animals; D001665:Binding Sites; D003179:Complement C3b / Q000378:metabolism*; D004306:Dose-Response Relationship, Immunologic; D006801:Humans; D008264:Macrophages / Q000276:immunology*; D051379:Mice; D010587:Phagocytosis; D011951:Receptors, Complement / Q000378:metabolism*; D017463:Receptors, Complement 3b; D011961:Receptors, Fc / Q000276:immunology*; D017452:Receptors, IgG; D012397:Rosette Formation
D011951:Receptors, Complement; D017463:Receptors, Complement 3b; D011961:Receptors, Fc; D017452:Receptors, IgG; D003179:Complement C3b