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 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.
D000818:Animals; D037263:Asialoglycoprotein Receptor; D006384:Hemagglutination; D006801:Humans; D007070:Immunoglobulin A / Q000378:metabolism*; D008103:Liver Cirrhosis / Q000097:blood; D046911:Macromolecular Substances; D051381:Rats; D011956:Receptors, Cell Surface / Q000378:metabolism*; D013329:Structure-Activity Relationship
D037263:Asialoglycoprotein Receptor; D007070:Immunoglobulin A; D046911:Macromolecular Substances; D011956:Receptors, Cell Surface