Human red blood cells sensitized with concanavalin A became bound to homologous peripheral blood monocytes. Binding occured at a concentration of 10(5) molecules of tetrameric Con A per red blood cell (RBC) and increased with additional Con A. RBC binding began within 5 min and was maximal at 90 min. Phagocytosis of sensitized RBCs was minimal. RBC attachment was prevented by 0.01 M alpha-methyl-D-mannopyranoside, and, once the RBC-monocyte rosette was established, bound RBCs were largely removed with this specific saccharide inhibitor of Con A. RBCs attached to monocytes became spherocytic and osmotically fragile. The recognition of concanavalin A (Con A)-coated RBCs was not mediated through the monocyte IgG-Fc receptor. These studies demonstrate that, like IgG and C3b, Con A is capable of mediating the binding of human RBCs to human monocytes. Red cells so bound are damaged at the monocyte surface.
Concanavalin A-mediated binding and sphering of human red blood cells by homologous monocytes.
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D Guerry, M A Kenna, A D Schrieber, R A Cooper; Concanavalin A-mediated binding and sphering of human red blood cells by homologous monocytes.. J Exp Med 1 December 1976; 144 (6): 1695–1700. doi: https://doi.org/10.1084/jem.144.6.1695
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