Abstract
The binding of 125I-labelled bovine serum albumin (BSA)-anti-BSA immune complexes (IC) to Raji cells and polymorphonuclear (PMN) cells in vitro was studied. The IC were reacted for 1 h at 37 degrees C with normal human serum (NHS) diluted 1:2 in the presence or absence of human erythrocytes (E) before presentation for Raji cells or PMN cells. The IC showed a two to three fold increased binding to C3d, g receptors (CR2) on Raji cells, when E-CR1 had been present during the reaction with NHS, compared to IC similarly reacted with NHS only. Blocking of the E-CR1 by a polyclonal anti-CR1 antibody reduced the subsequent binding of IC to Raji cells to the same level as that obtained with IC reacted with serum only. Binding to PMN granulocytes of IC reacted with NHS in the presence of E-CR1 showed a 60% reduction compared to the binding of IC reacted with NHS only. It is concluded that interaction of complement-reacted IC with CR1 on erythrocytes leads to a more efficient generation of CR2-binding C3d, g-containing IC with reduced reactivity to PMN cells.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
