IgG-binding sites on macrophage cell membrane. I. Identification of two distinct Fc receptors on mouse peritoneal macrophages.
Evidence is presented concerning the existence on mouse peritoneal macrophages of two separate and distinct Fc receptors, one for cytophilic monomeric IgG (mIgG) and the other for polymeric IgG. The latter Fc receptor recognizes both heat-aggregated IgG and antigen-complexed IgG. The major findings of our studies are: (a) the different susceptibility of the two Fc receptor types by pronase, trypsin or phospholipase C; (b) the independent modulation of these two binding sites on the cell membrane; (c) the inability of mIgG to inhibit the binding of particulate antigen-complexed IgG ligand; (d) the ability of mIgG molecules which are devoid of the cytophilic property to attach to the macrophage surface upon their polymerization induced by heating or antigen. The results are discussed in terms of "cytophilic" and "opsonic" Fc receptor types which may provide different functional abilities for normal macrophages.
D000818:Animals; D002462:Cell Membrane / Q000032:analysis / Q000276:immunology; D004912:Erythrocytes / Q000276:immunology; D006801:Humans; D007074:Immunoglobulin G / Q000276:immunology; D008264:Macrophages / Q000032:analysis / Q000276:immunology* / Q000648:ultrastructure; D051379:Mice; D011402:Pronase; D011961:Receptors, Fc / Q000032:analysis* / Q000276:immunology; D012397:Rosette Formation; D014357:Trypsin
D007074:Immunoglobulin G; D011961:Receptors, Fc; D014357:Trypsin; D011402:Pronase