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Wortmannin inhibits transcytosis of dimeric IgA by the polymeric immunoglobulin receptor
Author(s) -
Cardone Michael,
Mostov Keith
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01251-8
Subject(s) - transcytosis , polymeric immunoglobulin receptor , wortmannin , biology , microbiology and biotechnology , receptor , immune system , antibody , immunoglobulin a , immunology , signal transduction , pi3k/akt/mtor pathway , endocytosis , immunoglobulin g , biochemistry
Phosphatidyl inositol 3‐kinase (PI3K) plays an essential role in numerous signaling events, and increasingly has been implicated in regulation of certain membrane traffic events. The polymeric immunoglobulin receptor (pIgR) transcytoses dimeric IgA (dIgA) across epithelial cells and into external secretions, where the dIgA forms the first specific immunological defense against infection. We show here that wortmannin, a highly specific inhibitor of PI3K, inhibits transcytosis of dIgA by the pIgR. Instead, the dIgA is recycled back to the basolateral surface of the epithelial cell. PI3K therefore plays an essential role in regulating the transcytosis of dIgA, a key step in the mucosal immune response.