Binding of subclasses of rat immunoglobulin G to detergent-isolated Fc receptor from neonatal rat intestine.

Brush borders of cells lining the proximal small intestine of neonatal rats express a receptor specific for the Fc portion of IgG that mediates transport of IgG from gut lumen to blood. We have investigated the interaction of subclasses of rat IgG with this receptor, extracted in Triton X-114 solution, using phase separation to separate receptor-immunoglobulin complexes from free immunoglobulin. Binding of immunoglobulin showed the same pH dependence as is found in vivo, being active at pH 6 and reversibly inhibited at pH 8. The numbers of binding sites for each IgG subclass were similar, but polyclonal IgG2a was bound with higher affinity (1.2 X 10(8) M-1) than monoclonal IgG1 or IgG2b (2-3 X 10(7) M-1). Radiolabeled monoclonal IgG2c did not show specific binding, apparently as a result of the iodination process. Competition studies showed cross-inhibition between all IgG subclasses. IgG2a being approximately 10-fold more effective at competing for receptor than other isotypes, in the order IgG2a much greater than IgG1 greater than IgG2b greater than or equal to IgG2c. These data suggest that a single receptor capable of binding all subclasses of IgG is active in the detergent extract. However, investigation of radiolabeled immunoglobulins that were bound to isolated gut cells before detergent extraction showed evidence for other types of interaction in vivo.