Differentiation of human IgM subclasses by the ability to interact with a factor resembling the first component of complement.
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Biomedical subjects
Publications and source records attributed to H H Fudenberg.
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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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An immunoglobulin A of the secretory variety, present in the gastric juice of a patient with pernicious anemia, was shown to have specificity for intrinsic factor. This is the first demonstration in gastric juice of antibody activity restricted to secretory IgA; further, this is the first example of an exocrine (gastric) immune system producing an autoantibody specifically directed toward a product synthesized by that same exocrine organ.
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