IgG Fc membrane receptor on normal human glomerular visceral epithelial cells.
This study demonstrates that human glomerular epithelial cells are able to bind heat aggregated immunoglobulins and antigen-antibody complexes. This has been observed on kidney cryostat sections, on whole glomeruli and on cultured visceral epithelial cells. Binding depends on the presence of the Fc portion of IgG and occurs in the absence of complement, showing that the IgG Fc receptor is different from the C3b receptor. The use of heat aggregated anti-peroxidase IgG and of peroxidase anti-peroxidase complexes allowed us to demonstrate, at the ultrastructural level, that the binding of the reagents at the plasma membrane was followed by their internalization within coated pits of vesicles. These observations strongly suggest that glomerular visceral epithelial cells are capable of receptor mediated endocytosis. The role of this process in glomerular diseases remains to be established.
D000936:Antigen-Antibody Complex / Q000378:metabolism; D002478:Cells, Cultured; D004705:Endocytosis; D004848:Epithelium / Q000276:immunology; D005455:Fluorescent Antibody Technique; D006801:Humans; D007124:Immunoenzyme Techniques; D007074:Immunoglobulin G / Q000378:metabolism*; D007678:Kidney Glomerulus / Q000276:immunology*; D008854:Microscopy, Electron; D011961:Receptors, Fc / Q000378:metabolism*; D017452:Receptors, IgG; D011971:Receptors, Immunologic / Q000378:metabolism
D000936:Antigen-Antibody Complex; D007074:Immunoglobulin G; D011961:Receptors, Fc; D017452:Receptors, IgG; D011971:Receptors, Immunologic