Carbohydrate-Specific Receptors of the Liver

Carbohydrate-Specific Receptors of the Liver Desialylated serum glycoproteins have drastically reduced survival times in the circulation compared to native forms of the same proteins. A specific receptor on hepatocytes mediates their clearance by recognition of galactose residues made terminal by removal of sialic acid. This phenomenon was first demonstrated using desialylated ceruloplasmin (7). The newly exposed galactose moieties were implicated as recognition determinants by the findings that treatment of asialoceruloplasmin with galactose oxidase or ,a-galactosidase (7) or enzymatic replacement of the missing sialic acid residues (8) markedly prolonged survival in circulation. Subsequently, the generality of the original observation has been established by extension to alternate serum glycoproteins (7) and by the growing list of known glyco­ proteins susceptible to enhanced clearance due to desialylation (fable 1). Upon the foundation of these initial studies [summarized in an earlier review, see (9)], our current understanding of this process has been built and continues to grow. Two broad and overlapping categories define the studies that have contributed to this understanding. In some, the nature of the receptor molecule and its interaction with ligands have been examined. In others, the relationship between the receptor molecule and the cell in which it resides has been probed. Here, we http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Annual Review of Biochemistry Annual Reviews

Carbohydrate-Specific Receptors of the Liver

Annual Review of Biochemistry, Volume 51 (1) – Jul 1, 1982

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Publisher
Annual Reviews
Copyright
Copyright 1982 Annual Reviews. All rights reserved
Subject
Review Articles
ISSN
0066-4154
eISSN
1545-4509
DOI
10.1146/annurev.bi.51.070182.002531
Publisher site
See Article on Publisher Site

Abstract

Desialylated serum glycoproteins have drastically reduced survival times in the circulation compared to native forms of the same proteins. A specific receptor on hepatocytes mediates their clearance by recognition of galactose residues made terminal by removal of sialic acid. This phenomenon was first demonstrated using desialylated ceruloplasmin (7). The newly exposed galactose moieties were implicated as recognition determinants by the findings that treatment of asialoceruloplasmin with galactose oxidase or ,a-galactosidase (7) or enzymatic replacement of the missing sialic acid residues (8) markedly prolonged survival in circulation. Subsequently, the generality of the original observation has been established by extension to alternate serum glycoproteins (7) and by the growing list of known glyco­ proteins susceptible to enhanced clearance due to desialylation (fable 1). Upon the foundation of these initial studies [summarized in an earlier review, see (9)], our current understanding of this process has been built and continues to grow. Two broad and overlapping categories define the studies that have contributed to this understanding. In some, the nature of the receptor molecule and its interaction with ligands have been examined. In others, the relationship between the receptor molecule and the cell in which it resides has been probed. Here, we

Journal

Annual Review of BiochemistryAnnual Reviews

Published: Jul 1, 1982

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