Abstract
IT is now well established that an optimal immune response resulting in the production of antibody to most antigens requires interaction between three distinct cell types: T (thymus-derived) and B (thymus-independent) lymphocytes1, and macrophages2. Studies to elucidate the mechanism of interaction or collaboration have implicated soluble factors released by T cells which include both non-specific components3–6 and antigen-specific components6–9 which are bound by macrophages8,9. IgM has been demonstrated in T cell membranes10,11 in monomeric form11. Antigen binding by T cells, as judged by rosette formation12 or specific helper function at low doses of antigen13, can be inhibited by antibody to IgM determinants. Evidence suggests that the specific collaborative factor released by T cells consists of antigen complexed with monomeric IgM, which becomes bound to the surface of macrophage-like cells (refs. 9, 14 and 15 and E-P. Rieber and G. Reithmuller, submitted for publication). Macrophage binding of antigen specific factors released by T cells has also been shown in studies on the killing of allogeneic tumour cells in vitro16. Here I show that a receptor for monomeric IgM is present on macrophages from guinea-pig spleen. Pentameric (19S) IgM is not bound by these cells to any significant extent. Splenic macrophages were defined by the following characteristics: (1) rapid uptake of neutral red stain; (2) ingestion of carbonyl iron particles; (3) presence of a receptor for the Fc portion of guinea-pig γG2; (4) uptake in vivo of alum precipitated bovine serum albumin (BSA).
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RHODES, J. Receptor for Monomeric IgM on Guinea-pig Splenic Macrophages. Nature 243, 527–528 (1973). https://doi.org/10.1038/243527a0
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DOI: https://doi.org/10.1038/243527a0
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