Stimulation of Transcytosis of the Polymeric Immunoglobulin Receptor by Dimeric IgA

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 phys...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1994-01, Vol.91 (1), p.163-166
Main Authors: Song, Wenxia, Bomsel, Morgane, Casanova, James, Vaerman, Jean-Pierre, Mostov, Keith
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Biological Transport
Canines
Cell Line
Cell physiology
Cell Polarity
Cellular biology
Dogs
Endosomes
Epithelial cells
Epithelium - metabolism
Fundamental and applied biological sciences. Psychology
Immunoglobulin A - metabolism
Immunoglobulin Fab Fragments - metabolism
Leupeptins - pharmacology
Ligands
Membrane and intracellular transports
Molecular and cellular biology
Mutagenesis, Site-Directed
Phosphorylation
Phosphoserine - metabolism
Polymeric immunoglobulin receptors
Radioactive decay
Receptors
Receptors, Immunologic
Secretion
Secretory Component - metabolism
Structure-Activity Relationship
Transcytosis
Transferrin - metabolism
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.91.1.163