Abstract
The binding, uptake and processing of polymeric IgA (pIgA) by cultured rat hepatocytes have been studied in conditions where the cells reassociate into hepatic-like trabeculae and reform bile caniculi.
The cells synthesise secretory component (SC), partly secreted in the culture medium, and partly exposed at the cell surface. At 4°, hepatocytes bind specifically pIgA and competition experiments indicate that SC is the receptor responsible for the major part of this binding.
Lactoferrin but not asialofetuin inhibits both the low temperature binding and the uptake at 37°. This suggests that in our in vitro conditions 3H-labelled pIgA is taken up for a part through binding sites which recognise also lactoferrin possibly through the presence of exposed fucose residues.
At 37°, pIgA is taken up by the cells and rapidly interiorised. A minor part of the cell bound pIgA reappears after a Zag phase into the culture medium as low molecular weight labelled material; another major part reappears more rapidly as secretory IgA, most probably after its secretion at the biliary pole of the hepatocyte.
J.N.L. is Aspirant of the Belgian FNRS.
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© 1981 ECSC, EEC, EAEC, Brussels-Luxembourg
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Limet, J.N., Schneider, YJ., Trouet, A., Vaerman, J.P. (1981). Binding, Uptake and Processing of Polymeric IgA by Cultured Rat Hepatocytes. In: Bourne, F.J. (eds) The Mucosal Immune System. Current Topics in Veterinary Medicine and Animal Science, vol 12. Springer, Dordrecht. https://doi.org/10.1007/978-94-009-8331-1_4
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DOI: https://doi.org/10.1007/978-94-009-8331-1_4
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