Regulation of Protein Traffic in Polarized Epithelial Cells: The Polymeric Immunoglobulin Receptor Model

1995 ◽  
Vol 60 (0) ◽  
pp. 775-781 ◽  
Author(s):  
K.E. Mostov ◽  
Y. Altschuler ◽  
S.J. Chapin ◽  
C. Enrich ◽  
S.-H. Low ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Polymeric Immunoglobulin Receptor ◽  
Receptor Model ◽  
Immunoglobulin Receptor ◽  
Protein Traffic ◽  
Polarized Epithelial Cells

scholarly journals IgA-coated particles of Hepatitis A virus are translocalized antivectorially from the apical to the basolateral site of polarized epithelial cells via the polymeric immunoglobulin receptor

2005 ◽  
Vol 86 (10) ◽  
pp. 2747-2751 ◽  
Author(s):  
Andreas Dotzauer ◽  
Meike Brenner ◽  
Ulrike Gebhardt ◽  
Angelika Vallbracht
Keyword(s):  
Epithelial Cells ◽  
Hepatitis A ◽  
Hepatitis A Virus ◽  
Intestinal Barrier ◽  
Oral Route ◽  
Polymeric Immunoglobulin Receptor ◽  
Immunoglobulin Receptor ◽  
Coated Particles ◽  
Acute Infections ◽  
Polarized Epithelial Cells

Although Hepatitis A virus (HAV) is transmitted by the faecal–oral route, its target for replication is the liver. Little is known of its interactions with cells of the gastrointestinal tract, and it is not known by which mechanisms HAV crosses the intestinal epithelium. In this study, it is shown that HAV associated with IgA is translocated from the apical to the basolateral compartment of polarized epithelial cells via the polymeric immunoglobulin receptor by IgA-mediated reverse transcytosis. The relevance of this mechanism, by which HAV–IgA complexes may overcome the intestinal barrier and contribute to infections of the liver, results from the fact that HAV–IgA complexes are infectious for hepatocytes and that significant amounts of intestinal HAV–IgA are present during acute infections, which are also partly transmitted. Besides supporting the primary infection, this mechanism may play a role in relapsing infections by establishing an enterohepatic cycle for HAV.

scholarly journals Targeting Mucosal Sites by Polymeric Immunoglobulin Receptor-directed Peptides

2002 ◽  
Vol 196 (4) ◽  
pp. 551-555 ◽  
Author(s):  
Kendra D. White ◽  
J. Donald Capra
Keyword(s):  
Epithelial Cells ◽  
Fluorescent Protein ◽  
Secretory Component ◽  
In Vivo Studies ◽  
Polymeric Immunoglobulin Receptor ◽  
Immunoglobulin Receptor ◽  
Potential Binding Site ◽  
Green Fluorescent

Polymeric immunoglobulins provide first line humoral defense at mucosal surfaces to which they are specifically transported by the polymeric immunoglobulin receptor (pIgR) on mucosal and glandular epithelial cells. Previous studies from our laboratory suggested that amino acids 402–410 of the Cα3 domain of dimeric IgA (dIgA) represented a potential binding site for the pIgR. Here by binding human secretory component to overlapping decapeptides of Cα3, we confirm these residues and also uncover an additional site. Furthermore, we show that the Cα3 motif appears to be sufficient to direct transport of green fluorescent protein through the pIgR-specific cellular transcytosis system. An alternative approach identified phage peptides, selected from a library by the in vitro Madin Darby Canine Kidney transcytosis assay, for pIgR-mediated transport through epithelial cells. Some transcytosis-selected peptides map to the same 402–410 pIgR-binding Cα3 site. Further in vivo studies document that at least one of these peptides is transported in a rat model measuring hepatic bile transport. In addition to identifying small peptides that are both bound and transported by the pIgR, this study provides evidence that the pIgR-mediated mucosal secretion system may represent a means of targeting small molecule therapeutics and genes to mucosal epithelial cells.

scholarly journals The Polymeric Immunoglobulin Receptor Translocates Pneumococci across Human Nasopharyngeal Epithelial Cells

Cell ◽  
2000 ◽  
Vol 102 (6) ◽  
pp. 827-837 ◽  
Author(s):  
Jing-Ren Zhang ◽  
Keith E Mostov ◽  
Michael E Lamm ◽  
Masanobu Nanno ◽  
Shin-ichiro Shimida ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Polymeric Immunoglobulin Receptor ◽  
Immunoglobulin Receptor ◽  
Nasopharyngeal Epithelial

Opposite sorting and transcytosis of the polymeric immunoglobulin receptor in transfected endothelial and epithelial cells

1998 ◽  
Vol 111 (9) ◽  
pp. 1197-1206
Author(s):  
T. Su ◽  
K.K. Stanley
Keyword(s):  
Endothelial Cells ◽  
Steady State ◽  
Epithelial Cells ◽  
Cell Line ◽  
Mdck Cells ◽  
Basolateral Membrane ◽  
Secretory Component ◽  
Polymeric Immunoglobulin Receptor ◽  
Apical Surface ◽  
Immunoglobulin Receptor

We have transfected a polarised endothelial cell line, ECV 304, and an epithelial cell line, MDCK, with a well characterised epithelial protein, the rat polymeric immunoglobulin receptor (pIgR), in order to study the protein sorting and transcytosis in endothelial cells. The expressed protein was normally processed and the steady state distribution between apical and basolateral surfaces was similar in both cell types. MDCK cells, however, showed a marked polarity in the delivery of newly synthesised pIgR to the cell surface, and in the release of secretory component. 88% of newly synthesised pIgR in MDCK cells was first delivered to the basolateral surface and 99% of secretory component was released from the apical surface. In contrast the basolateral targeting signal of pIgR was only partially recognised in endothelial cells, with 63% of the newly synthesised pIgR being first delivered to the basolateral surface. At steady state only 43% of the pIgR was found on the basolateral membrane. The direction of dimeric IgA transcytosis in endothelial cells was from apical to basolateral surfaces, opposite to that in MDCK cells. These data suggest that endothelial cells poorly recognise the targeting signals of proteins from epithelial cells, and that the direction of transcytosis is linked to the biological role of the cells.

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