We expressed cDNA for the rabbit polymeric immunoglobulin receptor in polarized Madin-Darby Canine Kidney epithelial cells, which normally do not produce this receptor. The receptor appeared to function as in vivo; dimeric IgA was transported from the basolateral to the apical surface and released into the apical medium, together with the cleaved fragment of the receptor, known as secretory component. This system enabled us, for the first time, to study quantitatively IgA transcytosis in vitro and thus make the following observations. First, greater than 90% of the newly made receptor that is ultimately cleaved to secretory component and released into the apical medium goes first to the basolateral surface. Second, transport of the receptor does not depend on ligand binding. Third, transcytosis of bound ligand has a t 1/2 of 30 min.