Lectin mediates homing of sialidase-treated erythrocytes of the liver as revealed by scintigraphy.
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.
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
D037102:Lectins; D011975:Receptors, Mitogen; D009439:Neuraminidase