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Science 13 December 1968:
Vol. 162. no. 3859, pp. 1281 - 1283
DOI: 10.1126/science.162.3859.1281
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Articles

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

Heinz Huber 1, Margaret J. Polley 2, William D. Linscott 3, H. Hugh Fudenberg 3, and Hans J. Müller-Eberhard 4

1 Department of Medicine, University of California School of Medicine, San Francisco Medical Center, San Francisco
2 Department of Experimental Pathology, Scripps Clinic and Research Foundation, La Jolla, California
3 Department of Medicine University of California School of Medicine, San Francisco Medical Center
4 Department of Experimental Pathology, Scripps Clinic and Research Foundation

Human monocytes contain two distinct receptor sites, one specific for the third component of complement (C'3), the other for immunoglobulin G(ggrG). 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 ggrG antibody is independent of complement; however, the reaction is inhibited by concentrations of ggrG far below those in normal serum. Inhibition by ggrG-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 ggrG antibody in the presence of inhibitory amounts of free ggrG.


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