How are immune complexes bound to the primate erythrocyte complement receptor transferred to acceptor phagocytic cells?
Immune complexes (IC) bound to the primate erythrocyte (E) complement receptor (CR1) are cleared from the circulation of primates and localized to phagocytic cells in the liver and spleen without E destruction. IC can be bound to E CRI either via C3b opsonization or with cross-linked mAb complexes (heteropolymers, HP) which contain a mAb specific for CRI and a mAb specific for an antigen. The long-term goal of our work is to apply the HP system to the treatment of human diseases associated with blood-borne pathogens. This review discusses the mechanism by which the E-bound IC are transferred to acceptor cells. Our studies in animal models as well as our in vitro investigations indicate that IC transfer is rapid (usually >90% in 10 min) and does not lead to lysis or phagocytosis of the E. Experiments with specific inhibitors and the use of IC prepared with Fab’ fragments suggest that transfer depends mainly upon recognition by Fc receptors on the acceptor cell. Moreover, we find that IC
Related Questions
- Does reduced erythrocyte C3b receptor (CR1) activity contribute to the pathogenesis of yersinia triggered reactive arthritis?
- I’ve contacted InMotion Hosting and have acquired or transferred my domain name and hosting. What are the next steps?
- How does the customers payment get transferred to the payee corporation?
