Lectin Mediates Homing of Sialidase-Treated Erythrocytes of the Liver as Revealed by Scintigraphy

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Abstract
Mammalian erythrocytes loose their normal circulatory pattern following desialylation by sialidase and are trapped in the liver. The mechanism responsible for this phenomenon was studied by a new scintigraphic method. The retention of asialo-erythrocytes in the [rat] liver is due to the interaction between a lectin-like receptor on Kupffer cells and terminal D-galactosyl residues exposed on erythrocytes after sialidase treatment. Kinetics of asialo-erythrocyte accumulation in the liver are identical in conventional and germfree animals, demonstrating that the presence of serum antibody is not essential. Trapping of asialo-erythrocytes can be substantially inhibited by i.v. injection of N-acetyl-D-galactosamine or galactosylated bovine serum albumin, other saccharides or glycoproteins are less or not at all effective. This specificity pattern is characteristic for the D-galactose-specific lectin on Kupffer cells. The retention of sialidase-treated erythrocytes in the liver is probably lectin- and not antibody-mediated.