title: Lectin mediates homing of sialidase-treated erythrocytes of the liver as revealed by scintigraphy.
abstract: Mammalian erythrocytes loose their normal circulatory pattern following desialylation by sialidase and are trapped in the liver. The mechanism responsible for this phenomenon has been studied by a new scintigraphic method. We report here that the retention of asialo-erythrocytes in the 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. The major findings supporting the conclusion are: First, 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. Second, trapping of asialo-erythrocytes can be substantially inhibited by intravenous 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. It therefore appears that the retention of sialidase-treated erythrocytes in the liver is lectin- and not antibody mediated.
mesh_terms: D000818:Animals; D004912:Erythrocytes / Q000187:drug effects* / Q000378:metabolism; D007728:Kupffer Cells / Q000378:metabolism; D037102:Lectins / Q000378:metabolism / Q000494:pharmacology*; D008099:Liver / Q000166:cytology*; D009439:Neuraminidase / Q000494:pharmacology*; D051381:Rats; D011919:Rats, Inbred Strains; D011975:Receptors, Mitogen / Q000378:metabolism
chemical_list: D037102:Lectins; D011975:Receptors, Mitogen; D009439:Neuraminidase