IgA interaction with the asialoglycoprotein receptor.

RJ Stockert, MS Kressner, JC Collins… - Proceedings of the …, 1982 - National Acad Sciences
RJ Stockert, MS Kressner, JC Collins, I Sternlieb, AG Morell
Proceedings of the National Academy of Sciences, 1982National Acad Sciences
IgA present in normal human serum reacts with the hepatic receptor specific for
asialoglycoproteins as demonstrated by inhibition of receptor-mediated erythroagglutination.
Inhibition is reversibly abolished by the oxidation of the galactose or N-acetylgalactosamine
residues of IgA with galactose oxidase. The site of receptor recognition appears to be the O-
glycosidically linked oligosaccharides present on the hinge region of the IgAI subtype of IgA.
The demonstration of a specific binding, in vitro, of IgA by the hepatic receptor suggests that …
IgA present in normal human serum reacts with the hepatic receptor specific for asialoglycoproteins as demonstrated by inhibition of receptor-mediated erythroagglutination. Inhibition is reversibly abolished by the oxidation of the galactose or N-acetylgalactosamine residues of IgA with galactose oxidase. The site of receptor recognition appears to be the O-glycosidically linked oligosaccharides present on the hinge region of the IgAI subtype of IgA. The demonstration of a specific binding, in vitro, of IgA by the hepatic receptor suggests that the uptake of polymeric IgA by the liver in vivo may be mediated by this reaction.
National Acad Sciences