IgA interaction with the asialoglycoprotein receptor.

AUTOR(ES)

Stockert, R J

RESUMO

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.

Documentos Relacionados

• Phosphorylation of the rat hepatic polymeric IgA receptor.
• Identification and quantification of the rat hepatocyte asialoglycoprotein receptor.
• Circulating complexes containing IgA and fibronectin in patients with primary IgA nephropathy.
• TRAC Variants Associate with IgA Nephropathy
• Renal biopsy in children with IgA vasculitis