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The Journal of Immunology, Vol 147, Issue 4 1377-1382, Copyright © 1991 by American Association of Immunologists

ARTICLES

Aggregated bovine IgG inhibits mannose receptor expression of murine bone marrow-derived macrophages via activation

S Schreiber, WF Stenson, RP MacDermott, JC Chappel, SL Teitelbaum and SL Perkins
Division of Gastroenterology, Washington University School of Medicine, St. Louis, MO 63110.

We previously described the presence of an inhibitory protein contained in the 20 to 40% (NH4)2SO4 precipitable fraction of FCS that down- regulates expression of mannose receptors on bone marrow-derived macrophages. We now identify aggregated bovine IgG as the main inhibitory component. Heat-aggregated bovine IgG was capable of down- regulating expression of the macrophage mannose receptor in a dose- dependent manner without inducing changes in ligand affinity whereas neither F(ab')2 fragments nor nonaggregated IgG displayed any inhibitory effect. Depleting of IgG from heat inactivated FCS by protein G affinity chromatography completely removes the inhibitory activity. Moreover, readdition of the Ig eluate from the protein G chromatography column restored inhibition in a dose-dependent manner. Macrophages were able to clear exogenously added aggregated bovine IgG, thus leading to loss of inhibitory activity in macrophage-conditioned media as compared to sham-conditioned media containing aggregated IgG. These results indicate that aggregated IgG down-regulates mannose receptor expression by macrophage activation via interaction with Fc- gamma R.




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