Abstract
Mouse polymeric immunoglobulin receptor (pIgR) cDNA was stably introduced into a hamster-derived fibroblastic cell line, Chinese hamster ovary (CHO) cell, by the calcium phosphate method. Surface expression of pIgR was detected by immunostaining and FACS analysis. The immunoprecipitated products of cell lysates revealed that the molecular mass of the most mature form of pIgR was approximately 120 kDa. Western blotting and metabolic labeling experiments followed by immunoprecipitation with an anti-mouse secretory component (SC) Ab demonstrated the existence of a 110 kDa immature form of pIgR. The reason for the existence of two forms of pIgR molecule was examined by conducting pulse-chase experiments which revealed the pIgR underwent molecular maturation. During this process, the 110 kDa form of pIgR was converted into a 120 kDa form by glycosylation. Moreover, tunicamycin treatment revealed the core form of pIgR had a molecular mass of approximately 100 kDa. The pIgR expressed on the surface of the transfectant could specifically bind and take up mouse polymeric IgA (MOPC 315), suggesting that, at least in this mouse system, cell type-specific molecules are not necessary for surface pIgR expression and polymeric immunoglobulin (pIg) binding and uptake.
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