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Lack of SC/pIgR‐mediated epithelial transport of a human polymeric IgA devoid of J chain: in vitro and in vivo studies
Author(s) -
JeanPierre Vaerman,
Agnès Langendries,
D Giffroy,
Per Brandtzæg,
Kunihiko Kobayashi
Publication year - 1998
Publication title -
immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.297
H-Index - 133
eISSN - 1365-2567
pISSN - 0019-2805
DOI - 10.1046/j.1365-2567.1998.00560.x
Subject(s) - secretory component , in vitro , in vivo , antibody , j chain , biology , microbiology and biotechnology , polymeric immunoglobulin receptor , immunoglobulin light chain , chemistry , biochemistry , immunology
Three human polymeric IgA (pIgA) myeloma proteins of tetrameric size were compared for their J‐chain content, their in vitro secretory component (SC)‐binding ability, and their capacity to be transcytosed by polymeric immunoglobulin receptor (pIgR)‐expressing epithelial cells in vitro and rat hepatocytes in vivo. One of the three pIgA preparations, pIgA‐L, was shown to lack J chain and was unable to combine with purified free human and rat SC, whereas pIgA‐G and pIgA‐C contained J chain and combined readily with SC. Furthermore, pIgA‐L was not transferred into rat bile after intravenous injection, and was hardly transported apically by polarized Madin–Darbey canine kidney cell monolayers expressing the human pIgR, whereas pIgA‐G and pIgA‐C were efficiently transported in both test systems. Together with our recent demonstration that antibodies to human J chain block the SC/pIgR‐mediated epithelial transport of pIgA, these data unanimously confirm the proposed key role of J chain in the epithelial transport of polymeric immunoglobulins into exocrine secretions.