IgA Interaction with the Asialoglycoprotein Receptor

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 ox...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1982-10, Vol.79 (20), p.6229-6231
Main Authors: Stockert, Richard J., Kressner, Michael S., Collins, Janna C., Sternlieb, Irmin, Morell, Anatol G.
Format: Article
Language:English
Subjects:
Agglutination
Animals
Asialoglycoprotein Receptor
Asialoglycoproteins
Biochemistry
Chemical suspensions
Cirrhosis
Glycoproteins
Hemagglutination
Humans
immunoglobulin A
Immunoglobulin A - metabolism
Liver
Liver Cirrhosis - blood
Macromolecular Substances
Oxidases
Rats
Receptors
Receptors, Cell Surface - metabolism
Sodium
Structure-Activity Relationship
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Description
Summary: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 IgA1 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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.79.20.6229