Abstract
Rat hepatocytes in short-term monolayer cultures bound radiolabeled polymeric rat IgA but not IgG. The binding of 125I-IgA was inhibited equally well by unlabeled polymeric IgA and by antiserum to rat secretory component (SC). The antibody to SC, after specific purification and radiolabeling, was bound to hepatocytes as effectively as the IgA. These results indicate that SC acts as the receptor for polymeric IgA on rat hepatocytes as it does on human gut epithelia, and that the transport of IgA from blood to bile in rats across the liver is analogous to that of IgA across human enterocytes.
Highlights
Rat hepatocytes in short-term monolayer cultures bound radiolabeled polymeric rat IgA but not IgG
The antibody to secretory component (SC), after specific purification and radiolabeling, was bound to hepatocytes as effectively as the IgA. These results indicate that SC acts as the receptor for polymeric IgA on rat hepatocytes as it does on human gut epithelia, and that the transport of IgA from blood to bile in rats across the liver is analogous to that of IgA across human enterocytes
These results indicate that secretory component (SC) acts as the receptor for polymeric IgA on rat hepatocytes as it does on human gut epithelia, and that the transport of IgA from blood to bile in rats across the liver is analogous to that of IgA across human enterocytes
Summary
Preparationof lmmunoglobulins, FreeSC, and Purified Antibody to SC. The preparation and properties of the polymeric rat IgA formed by the IR 461 plasmacytoma have been described [1]. Rat IgG was the fraction of normal rat serum eluted from DEAE cellulose with 0.01 M phosphate buffer at pH 7.2. Reactive with antibody to either a-chain or to SC, eluted together with a phosphate buffer (0.05 M, pH 6.2) that contained 0.2-0.3 M NaCI. Gel filtration of this material on a column of Ultrogel AcA34 Further gel filtration of these two fractions on Ultrogel AcA22 and AcA34, respectively, yielded a preparation of pure polymeric s-IgA and one of free SC that still contained some serum albumin; the antigenic properties of the biliary SC are shown in Fig. I a
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