Superoxide anion production from mouse peritoneal macrophages stimulated with surface-bound IgG and immune complexes: adsorption characteristics of IgG in relationship to biological activity.
The bridging of IgG antibody molecules by either multivalent antigen or protein A adsorbed to a polymer surface triggers superoxide anion (O-2) generation from mouse peritoneal macrophages. Macrophages, upon stimulation with IgG adsorbed to a hydrophobic polymer, polystyrene, also significantly generated O-2. In contrast, soluble IgG did not stimulate macrophages. From these results we speculated that IgG adsorbed to polystyrene produces the same kind of a conformational change in its Fc region as seen in immune complexes, and leads to enhancement of the ability of the Fc region to bind macrophage Fc receptors, acting as a multivalent cross-linking agent to aggregate the Fc receptors. The surface charge density of the immunosorbent did not affect the antigen recognition function of antibody, but markedly affected its effector function. These findings suggest that activation of the Fc receptor-mediated function of macrophages requires, on the one hand, optimal conformational change and orientation of IgG and immune complexes adsorbed to the polymer surface and, on the other hand, the bridging of IgG molecules by multivalent agents.
D000327:Adsorption; D000818:Animals; D000936:Antigen-Antibody Complex; D005260:Female; D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D007164:Immunosorbents; D066298:In Vitro Techniques; D008264:Macrophages / Q000276:immunology / Q000378:metabolism*; D051379:Mice; D010100:Oxygen / Q000378:metabolism*; D011487:Protein Conformation; D011961:Receptors, Fc; D013481:Superoxides / Q000378:metabolism*
D000936:Antigen-Antibody Complex; D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D007164:Immunosorbents; D011961:Receptors, Fc; D013481:Superoxides; D010100:Oxygen