Secretory component as the receptor for polymeric IgA on rat hepatocytes

نویسندگان

  • E Orlans
  • J Peppard
  • J F Fry
  • R H Hinton
  • B M Mullock
چکیده

Rat hepatocytes in short-term monolayer cultures bound radiolabeled polymeric rat IgA but not IgG. The binding of 125I-IgA was inhibited equally well by unlabeled polymeric IgA and by antiserum to rat secretory component (SC). The antibody to SC, after specific purification and radiolabeling, was bound to hepatocytes as effectively as the IgA. These results indicate that SC acts as the receptor for polymeric IgA on rat hepatocytes as it does on human gut epithelia, and that the transport of IgA from blood to bile in rats across the liver is analogous to that of IgA across human enterocytes.

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Brie£ Dehnitive Report Secretory Component as the Receptor for Polymeric Iga on Rat Hepatocytes

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Polymeric IgA is t ransported from blood to bile by the rat liver (1, 2) in a manner which may be analogous to the transport of polymeric IgA across the mucosal epithelium. Such transport is thought to be mediated by secretory component (SC) 1 an epithelial cell glycoprotein which acts as a receptor for polymeric IgA on these cells (3-8). Fisher et al. (9) recently reported that Ig transport by...

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Brie£ DeHnitive Report

The rapid and active transport of polymeric IgA from the blood to the bile (1, 2) is selective (3, 4), which suggests the existence of a specific receptor for this molecule. The liver cells responsible for the transfer have been identified as the hepatocytes by autoradiography and electron microscopy of the livers o f rats killed 5, 30, and 60 min after the injection of radiolabeled IgA (5). 5 ...

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Identification of secretory component as an IgA receptor on rat hepatocytes

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Biogenesis of the polymeric IgA receptor in rat hepatocytes. I. Kinetic studies of its intracellular forms

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عنوان ژورنال:
  • The Journal of Experimental Medicine

دوره 150  شماره 

صفحات  -

تاریخ انتشار 1979