Rapid clearance of sialylated glycoproteins by the asialoglycoprotein receptor

Eric I. Park, Stephen M. Manzella, Jacques U. Baenziger

Research output: Contribution to journalArticle

50 Scopus citations

Abstract

The asialoglycoprotein-receptor (ASGP-R) located on liver parenchymal cells was originally identified and characterized on the basis of its ability to bind glycoproteins bearing terminal galactose (Gal) or N-acetylgalactosamine (GalNAc); however, endogenous ligands for the ASGP-R have not to date been definitively identified. We have determined that the rat ASGP-R specifically binds oligosaccharides terminating with the sequence Siaα2,6GalNAcβ1,4GlcNAcβ1,2Man. Bovine serum albumin chemically modified with 10-15 tetrasaccharides with the sequence Siaα2,6GalNAcβ1,4GlcNAcβ1,2Man is cleared from the blood of the rat with a half-life of <1 min by a receptor located in the liver. We have isolated the receptor and identified it as the ASGP-R. Furthermore, we have determined that subunit 1 of the ASGP-R accounts for the binding of terminal Siaα2,6GalNAcβ. Based on the newly defined specificity of the rat ASGP-R we hypothesize that glycoproteins bearing structures that are selectively modified with terminal Siaα2, 6GalNAcβ and are released into the blood may be endogenous ligands for the rat ASGP-R.

Original languageEnglish
Pages (from-to)4597-4602
Number of pages6
JournalJournal of Biological Chemistry
Volume278
Issue number7
DOIs
StatePublished - Feb 14 2003

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