Antibody against the human J chain inhibits polymeric Ig receptor‐mediated biliary and epithelial transport of human polymeric IgA

To emphasize the requirement for a J chain in native polymeric immunoglobulins for their selective transport into exocrine secretions, IgG, purified from two different antisera specific for the human J chain, was shown to: (i) bind in vitro to human polymeric IgA (pIgA) by density gradient ultracent...

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Published in:	European journal of immunology Vol. 28; no. 1; pp. 171 - 182
Main Authors:	Vaerman, Jean‐Pierre, Langendries, Agnes E., Giffroy, Didier A., Kaetzel, Charlotte S., Tamer Fiani, Carol M., Moro, Itaru, Brandtzaeg, Per, Kobayashi, Kunihiko
Format:	Journal Article
Language:	English
Published:	Weinheim WILEY‐VCH Verlag GmbH 01-01-1998
Subjects:	Animals Bile - metabolism Binding Sites Biological Transport Cell Line Dogs Epithelial Cells - metabolism Epithelial transport Humans Immune Sera - pharmacology Immunoglobulin A - chemistry Immunoglobulin A - metabolism Immunoglobulin Fab Fragments - immunology Immunoglobulin J-Chains - immunology Immunoglobulin J-Chains - physiology J chain antibody Kidney - cytology Liver - metabolism Male Mice Mice, Knockout Polymeric IgA Polymeric immunoglobulin receptor/secretory component Propionates - pharmacology Protein Binding - drug effects Protein Denaturation Rabbits Rats Rats, Wistar Receptors, Polymeric Immunoglobulin - drug effects Rodent bile Secretory Component - metabolism
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Summary:	To emphasize the requirement for a J chain in native polymeric immunoglobulins for their selective transport into exocrine secretions, IgG, purified from two different antisera specific for the human J chain, was shown to: (i) bind in vitro to human polymeric IgA (pIgA) by density gradient ultracentrifugation; (ii) inhibit binding in vitro of rat secretory component to human pIgA; (iii) inhibit hepatic transport of human pIgA into rat bile in vivo; and (iv) inhibit apical transcytosis of pIgA in vitro by polarized human polymeric immunoglobulin receptor (pIgR)‐expressing Madin‐Darby canine kidney cells. Inhibition of biliary transport increased with the molar ratio of anti‐J chain antibodies against pIgA and their incubation time. Anti‐J chain F(ab ′ )2 and Fab fragments also inhibited biliary transport, excluding a role for phagocytic clearance or excessive size of the immune complexes. Anti‐human‐Fcα Fab, bound to human pIgA in complexes of larger size than those with anti‐J chain Fab, did not inhibit biliary transport of human pIgA. Propionic acid‐denatured human pIgA, although containing J chains, was very poorly transported into rat bile. Altogether, our data strongly support, now also by in vivo experiments, the crucial role of the J chain of native pIgA in its selective pIgR‐mediated transport into secretions, as suggested long ago by in vitro data only. Recent data on J chain‐knockout mice, with low IgA levels in bile and feces, cannot explain the role of the J chain in contributing to the secretory component/pIgR‐binding site of normal pIgA, but otherwise agree with our study.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-1 content type line 23 ObjectType-Article-1 ObjectType-Feature-2
ISSN:	0014-2980 1521-4141
DOI:	10.1002/(SICI)1521-4141(199801)28:01<171::AID-IMMU171>3.0.CO;2-#