The role of J chain in epithelial polymeric IgA (pIgA)-transport, shown by Brandtzaeg in 1975, is evidenced by lack of binding of J chain-deficient pIgA to free secretory component (SC) and to surface membrane SC on HT-29 colon carcinoma cells. Also, antibodies (Abs) to J chain inhibit such binding of J chain-containing pIgA. These in vitro data needed confirmation by functional experimental test systems. Here, we show inhibition of receptor-media ted epithelial transport of pIgA By anti-J chain Abs, and lack of transport of J chain-deficient pIgA, by two functional tests: in vivo rat hepatobiliary transport of intravenously-injected human pIgA, and apical transport of pIgA by cultured SC-expressing Madin-Darby canine kidney (SC-MDCK) cells grown as confluent monolayers on permeable filters separating the apical from the basolateral medium. Rabbit Abs to J chain, but not normal rabbit IgG, incubated with purified human pIgA inhibited its rat biliary transport in a dose- and time-dependent manner: F(ab')2 and Fab' fragments of anti-J chain Abs also inhibited, excluding Fc gamma-dependent clearance and excessive size of the immune complexes. Abs to J chain also inhibited pIgA transport by SC-MDCK cells. In addition, of three purified tetrameric IgA (tIgA) myeloma proteins only the two that contained J chain by several criteria, readily combined with SC by various methods In the functional transport tests, only the same two pIgAs were actively transported. Altogether our functional data convincingly confirmed the crucial role of the J chain in the epithelial transport of pIgA.
Vaerman, JP., Langendries, A., Giffroy, D., Brandtzaeg, P., & Kobayashi, K. (1998). Crucial role of J chain in receptor-mediated epithelial transport of polymeric IgA: in vivo and in vitro data. Periodicum Biologorum, 100(4), 501-506. https://hdl.handle.net/2078.5/141041 (Original work published 1998)