Binding and uptake of rabbit IgG complexes by diploid fibroblasts via plasma membrane Fc receptors.
The existence of IgG receptors on the plasma membrane of diploid human fibroblasts is demonstrated. The receptors specifically bind heat-aggregated rabbit IgG as well as rabbit IgG within antigen-antibody complexes. Monomeric rabbit IgG were only poor ligands of the receptor. Competition experiments with Fab and Fc fragments of IgG revealed that the receptor specifically recognizes the Fc domain of the IgG molecule. Heat-aggregated IgG or antigen-antibody IgG complexes are specifically bound to the receptors, endocytosed and subsequently degraded. The receptors do not seem to be recycled because protein synthesis is a prerequisite for further cycles of endocytosis.
D001692:Biological Transport; D002462:Cell Membrane / Q000378:metabolism; D004705:Endocytosis; D005347:Fibroblasts / Q000276:immunology / Q000378:metabolism*; D006801:Humans; D007074:Immunoglobulin G / Q000378:metabolism*; D046911:Macromolecular Substances; D011485:Protein Binding; D011961:Receptors, Fc / Q000378:metabolism*
D007074:Immunoglobulin G; D046911:Macromolecular Substances; D011961:Receptors, Fc