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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1994 Jan 4;91(1):163–166. doi: 10.1073/pnas.91.1.163

Stimulation of transcytosis of the polymeric immunoglobulin receptor by dimeric IgA.

W Song 1, M Bomsel 1, J Casanova 1, J P Vaerman 1, K Mostov 1
PMCID: PMC42906  PMID: 8278358

Abstract

The polymeric immunoglobulin receptor (pIgR) is transcytosed from the basolateral to the apical surface of polarized epithelial cells. We have previously shown that phosphorylation of Ser-664 in the cytoplasmic domain of the pIgR is a signal for its transcytosis. We now report that binding of a physiological ligand, dimeric IgA, to pIgR stimulates pIgR transcytosis. This stimulation occurs in both the presence or absence of Ser-664 phosphorylation. We have used three methods to measure transcytosis of the pIgR. (i) The pIgR was biosynthetically labeled and its cleavage to secretory component after transcytosis was measured. (ii) The pIgR was labeled with biotin at the basolateral surface. After transcytosis, release of the biotin-labeled secretory component into the apical medium was measured. (iii) Transcytosis of a ligand bound to the pIgR was measured. All three methods indicated that dimeric IgA stimulates transcytosis of the pIgR.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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