Effects of immobilized immune complexes on Fc- and complement-receptor function in resident and thioglycollate-elicited mouse peritoneal macrophages.
We have examined the Fc- and complement-receptor function of resident and thioglycollate-elicited mouse peritoneal macrophages plated on surfaces coated with rabbit antibody-antigen complexes and with complement. We derive four major conclusions from these studies. (a) The trypsin-resistant Fc receptors of resident and thioglycollate-elicited macrophages are completely modulated when these cells are plated on rabbit antibody-antigen complexes. Residual Fc receptor activity is a result of the incomplete modulation of trypsin-sensitive IgG2a receptors. (b) The complement receptors of thioglycollate-elicited macrophages, but not of resident macrophages, are modulated when these cells are plated on complement-coated surfaces. The capacity of the two cell types to modulate their complement receptors is correlated with their ability to ingest complement-coated erythrocytes. (c) The complement and Fc receptors of both types of macrophages move independently of one another. (d) Complement masks the Fc segments of IgG in immune complexes thereby rendering them ineffective as ligands for macrophage Fc receptors.
D000818:Animals; D000936:Antigen-Antibody Complex; D001202:Ascitic Fluid / Q000276:immunology; D001665:Binding Sites; D003165:Complement System Proteins; D007141:Immunoglobulin Fc Fragments; D008264:Macrophages / Q000187:drug effects / Q000276:immunology*; D051379:Mice; D008954:Models, Biological; D010587:Phagocytosis; D013864:Thioglycolates / Q000494:pharmacology*; D014357:Trypsin / Q000494:pharmacology
D000936:Antigen-Antibody Complex; D007141:Immunoglobulin Fc Fragments; D013864:Thioglycolates; D003165:Complement System Proteins; D014357:Trypsin