Fc receptors have been found on many different cells including B and T lymphocytes, macrophages, neutrophils, and K cells, as well as cells not involved in the immune system. Some cellular functions such as phagocytosis of IgG-coated particles (1, 2) and the antibody-dependent cell-mediated cytotoxicity reaction (3) can clearly be attributed to this surface activity. On the other hand, the functional significance of Fc receptors on other cells such as B and T lymphocytes has not as yet been elucidated. As part of our investigations of the possible function of Fc receptors, we have studied the specificity of receptors for immunoglobulins of different IgG subclasses, as well as the degree of polymerization of the immunoglobulin capable of binding to these receptors. For this purpose myeloma proteins of different IgG subclasses were chemically crosslinked by bis-diazotized benzidine (BDB).' Monomer IgG and IgG aggregates of comparable size, representative of the different subclasses, were examined for their capacity to bind to receptors on different established cell lines and normal cells. Our findings indicate that the binding of myeloma proteins is dependent both upon subclass and degree of polymerization. Furthermore, studies on a macrophage-like cell line (P388) strongly suggest the presence of at least two different receptors for IgG on this cell, one characterized by its reactivity with monomeric IgG2a and the other for its activity with aggregated IgG of all subclasses.
Materials and MethodsMyeloma Proteins. The following IgG myeloma proteins were used in this study: MOPC-21 (IgG1), PC-5, and HOPC-1 (IgG2a), MOPC-141 (IgG2b), and J606 (IgGz). The myeloma proteins were isolated by starch block electrophoresis. Only the peak tubes of the myeloma protein-containing fractions were used. The myeloma proteins were cross-linked with BDB according to a modification of the method of Ishizaka (4) resulting in soluble complexes with a wide range of size.