Studies on translocation of immunoglobulins across intestinal epithelium. IV. Evidence for binding of IgA and IgM to secretory component in intestinal epithelium.

We conducted studies concerning the issue of whether secretory component (SC) is a specific receptor on intestinal epithelial cells for IgA and IgM. Initially, frozen sections of human intestinal mucosa were incubated with dimeric monoclonal human IgA, conjugated to horseradish peroxidase; adjacent sections were reacted with peroxidase-conjugated antibodies to SC. The conjugated IgA and anti-SC bound to similar sites in the epithelium, that is to basolateral margins and supranuclear cytoplasm of columnar epithelial cells, principally in gland crypts. In subsequent tests of binding specificity, binding of the dimeric IgA conjugate was inhibited by pretreating the tissues with unconjugated dimeric IgA or 19S IgM, pretreating the tissues with unconjugated antibodies to SC, or preincubating the dimeric IgA conjugate with free SC. Binding was not inhibited or only partially inhibited by pretreating the tissues with monomeric IgA or IgG, pretreating the tissues with antibodies to human or heterologous immunoglobulins, or preincubating the dimeric IgA conjugate with 11S secretory colostral IgA. The findings indicate that dimeric IgA and 19S IgM are capable of binding in vitro to specific sites on intestinal epithelial cells, most likely to SC. This supports the hypothesis that transport of these immunoglobulins into intestinal fluids involves their combination with SC in the epithelium.