Human Monocytes: Distinct Receptor Sites for the Third Component of Complement and for Immunoglobulin G

H. Huber(University of California San Francisco Medical Center), Margaret J. Polley(Scripps Health), William D. Linscott(University of California San Francisco Medical Center), H. Hugh Fudenberg(University of California San Francisco Medical Center), Hans J. Müller‐Eberhard(Scripps Health)
Science
December 13, 1968
Cited by 487

Abstract

Human monocytes contain two distinct receptor sites, one specific for the third component of complement (C'3), the other for immunoglobulin G(gammaG). The two receptors may function either independently or cooperatively in the induction of phagocytosis. Ingestion of erythrocytes coated with immunoglobulin M antibody requires a relatively large number of bound C'3 molecules per cell. Ingestion of erythrocytes sensitized with gammaG antibody is independent of complement; however, the reaction is inhibited by concentrations of gammaG far below those in normal serum. Inhibition by gammaG-globulin is overcome by a relatively small number of bound C'3 molecules per cell. The two monocyte receptors exert a cooperative effect on ingestion by monocytes of erythrocytes coated with gammaG antibody in the presence of inhibitory amounts of free gammaG.


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