Immunoglobulin A receptor of rat small intestinal enterocytes is unaffected by aging.

The receptor for polymeric immunoglobulins is responsible for the transport of immunoglobulin A (IgA) through epithelial cells and its subsequent delivery to mucosal surfaces. We have extended our previous studies of the IgA receptor in the liver of the aging Fischer rat to include the small intestine. Basolateral membrane-enriched fractions prepared from rat small intestinal enterocytes exhibit a single binding site for dimeric IgA. This receptor is specific for molecules that interact with rat secretory component, e.g., rat dimeric IgA and IgM and human polymeric IgA but not human monomeric IgA or rat secretory IgA. Inhibition of binding by rabbit-antirat secretory component also indicated that binding is specific for secretory component. Both liver and intestinal membranes showed virtually identical binding specificity. Membranes from crypt cells show increased IgA binding (320 fmol bound per milligram protein) compared with villous cells (105 fmol bound per milligram protein); however, other than increased binding, crypt cells show the same binding characteristics as villous cells. In contrast to our previous findings, in which liver plasma membranes from old rats showed a four-fold decrease in IgA binding compared with young adult rats, membrane fractions from rat enterocytes showed no alterations in dimeric IgA binding with increased age.