Skip Navigation



Glycobiology Advance Access published online on April 2, 2003
Glycobiology, doi:10.1093/glycob/cwg068
This Article
Right arrow Advance Access manuscript (PDF) Freely available
Right arrow All Versions of this Article:
13/7/529    most recent
cwg068v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrowRequest Permissions
Right arrow Disclaimer
Google Scholar
Right arrow Articles by Fadden, A. J.
Right arrow Articles by Drickamer, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Fadden, A. J.
Right arrow Articles by Drickamer, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Submitted on December 19, 2002
Revised on March 10, 2003
Accepted on March 12, 2003

© 2003 Oxford University Press

ORIGINAL ARTICLES

Molecular characterization of the rat Kupffer cell glycoprotein receptor

Andrew J. Fadden 1, Oliver J. Holt 1, Kurt Drickamer 1*

1 The Glycobiology Institute, Department of Biochemistry, University of Oxford, Oxford OX21 3QU, United Kingdom

* To whom correspondence should be addressed. E-mail: kd{at}glycob.ox.ac.uk.

Abstract

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. In order 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 {alpha}-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. {alpha}-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.


Kupffer cell, glycoprotein, clearance, receptor, lectin
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
A. S. Powlesland, T. Fisch, M. E. Taylor, D. F. Smith, B. Tissot, A. Dell, S. Pohlmann, and K. Drickamer
A Novel Mechanism for LSECtin Binding to Ebola Virus Surface Glycoprotein through Truncated Glycans
J. Biol. Chem., January 4, 2008; 283(1): 593 - 602.
[Abstract] [Full Text] [PDF]

Home page
 GlycobiologyHome page
P. J. Coombs, M. E. Taylor, and K. Drickamer
Two categories of mammalian galactose-binding receptors distinguished by glycan array profiling
Glycobiology, August 1, 2006; 16(8): 1C - 7C.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
A. S. Powlesland, E. M. Ward, S. K. Sadhu, Y. Guo, M. E. Taylor, and K. Drickamer
Widely Divergent Biochemical Properties of the Complete Set of Mouse DC-SIGN-related Proteins
J. Biol. Chem., July 21, 2006; 281(29): 20440 - 20449.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.