Vaerman, Jean-Pierre
[UCL]
Langendries, Agnès
[UCL]
Giffroy, D
Brandtzaeg, P.
Kobayashi, K.
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.
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Bibliographic reference |
Vaerman, Jean-Pierre ; Langendries, Agnès ; Giffroy, D ; Brandtzaeg, P. ; Kobayashi, K.. Lack of SC/pIgR-mediated epithelial transport of a human polymeric IgA devoid of J chain: in vitro and in vivo studies.. In: Immunology, Vol. 95, no. 1, p. 90-6 (1998) |
Permanent URL |
http://hdl.handle.net/2078.1/24182 |