Rapid clearance of sialylated glycoproteins by the asialoglycoprotein receptor
Rapid clearance of sialylated glycoproteins by the asialoglycoprotein receptor
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DOI：
10.1074/jbc.m210612200
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发表时间：
2003-02-14
影响因子：
4.8
通讯作者：
Baenziger, JU
中科院分区：
文献类型：
--
作者：
Park, EI;Manzella, SM;Baenziger, JU
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-acetylgalac-tosamine (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 Siaalpha2,6GalNAcbeta1,4GlcNAcbeta1,2Man. Bovine serum albumin chemically modified with 10-15 tetrasaccharides with the sequence Siaalpha2,6GalNAcbeta1,4GlcNAcbeta1,2Man 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 Siaalpha2,6GalNAcbeta. Based on the newly defined specificity of the rat ASGP-R we hypothesize that glycoproteins bearing structures that are selectively modified with terminal Siaalpha2,6GalNAcbeta and are released into the blood may be endogenous ligands for the rat ASGP-R.
