Glycobiology Advance Access originally published online on April 2, 2003
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Glycobiology, 2003, Vol. 13, No. 7 529-537
© 2003 Oxford University Press
Molecular characterization of the rat Kupffer cell glycoprotein receptor
The Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX21 3QU, United Kingdom
Received on December 19, 2002; revised on March 10, 2003; accepted on March 12, 2003
The Kupffer cell receptor for glycoproteins has been reported to have a role in clearance of galactose- and fucose-terminated glycoproteins from circulation. Although the gene and a cDNA encoding the receptor have been described, there has been little study of the receptor protein. To address some questions about possible ligands and functions for this receptor, fragments representing portions of the extracellular domain have been expressed and characterized. The extracellular domain consists of a trimer stabilized by an extended coiled-coil of 
-helices. The receptor displays monosaccharide-binding characteristics similar to the hepatic asialoglycoprotein receptor, but with somewhat less selectivity. The two best monosaccharide ligands are GalNAc and galactose. -Methyl fucoside is a particularly poor ligand. Analysis of Kupffer cell receptor binding to glycoproteins and oligosaccharides released from them reveals highest affinity for desialylated, complex N-linked glycans. The best glycoprotein ligands contain multiple highly branched oligosaccharides. A human ortholog of the rat receptor gene does not encode a full-length protein and is not expressed in liver. These characteristics suggest that the receptor may have functions parallel to those of the hepatocyte asialoglycoprotein receptor in some (but not all) mammalian species.
1 Present address: Cancer Research UK, 44 Lincoln's Inn Fields, London WC2A 3PX, United Kingdom.
2 To whom correspondence should be addressed; e-mail: kd{at}glycob.ox.ac.uk
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