Interaction between immune complexes and C3b receptors on erythrocytes.
We studied the interaction between immune complexes (IC) and C3b receptors (CR1) on erythrocytes (E) and showed that activation of the classical complement pathway is essential for the binding of IC to CR1, that C3b inactivator (I) and beta 1H (H) are essential for the release of IC from CR1, that CR1 retain the capacity to bind IC after repeated binding and release of IC, and that on the other hand, IC lose the capacity to bind to CR1 after repeated binding and release. These results suggest a dynamic in vivo interaction between IC and CR1 on E which are supposed to transport IC to the reticuloendothelial system. CR1 on E, with a help of I and H, might make IC less harmful to the tissues in the process of releasing IC from E.
D000936:Antigen-Antibody Complex; D004910:Erythrocyte Membrane / Q000276:immunology*; D006801:Humans; D012157:Mononuclear Phagocyte System / Q000276:immunology; D011951:Receptors, Complement / Q000276:immunology*; D017463:Receptors, Complement 3b; D013997:Time Factors
D000936:Antigen-Antibody Complex; D011951:Receptors, Complement; D017463:Receptors, Complement 3b