Interaction of complement-solubilized immune complexes (IC) with CR1 receptors on human erythrocytes. Polysulfated...

The effect of the polysulfated compounds heparin, dextran sulfate, chondroitin sulfate and suramin, and non-sulfated poly-, oligo-, and monosaccharides on binding and release of complement-solubilized 125I BSA-anti BSA immune complexes (IC) reacting with complement C3b receptors (CR1) on human erythrocytes (E) was investigated. Following presolubilization of IC in normal autologous human serum (NHS) a clear dose-dependent inhibition of IC-binding to E-CR1 was obtained by addition of polysulfated compounds. The inhibitory effect was dependent on the sulfate content of the reagents used but independent of their anticoagulant activity as heparin preparations with high and low affinity for antithrombin III inhibited IC binding to E-CR1 to approximately the same extent. Dextran sulfate caused a stronger inhibition than heparin while chondroitin sulfate was inhibitory only at high concentrations. The inhibitory effect was exerted at the IC-C3b level as normal IC-binding occurred following preincubation of E with the polysulfated compounds. Non-sulfated saccharides showed no inhibition of IC binding to E-CR1. All polysulfated compounds, apart from chondroitin sulfate, induced a dose-dependent release of E-CR1 bound IC in the absence of NHS. No release was obtained by use of non-sulfated saccharides. Heparin induced IC-release was rapid (40-45% after 3 min) and incubation beyond 30 min caused only an insignificant further release of IC from E-CR1. Following release of IC the E-CR1 retained full binding capacity for freshly added IC-C3b.