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. 1982 Oct;79(20):6229–6231. doi: 10.1073/pnas.79.20.6229

IgA interaction with the asialoglycoprotein receptor.

R J Stockert, M S Kressner, J C Collins, I Sternlieb, A G Morell
PMCID: PMC347093  PMID: 6292896

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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