Cell Biology of the Asialoglycoprotein Receptor System: A Model of Receptor-Mediated Endocytosis

Philip P. Breitfeld, Charles F. Simmons, Ger J.A.M. Strous, Hans J. Geuze, Alan L. Schwartz

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65 Scopus citations


The cell biology and biochemistry of the asialoglycoprotein receptor (ASGP-R) system provide unique insights into the fundamental process of receptor-mediated endocytosis. This chapter focuses on specific aspects of the structure, morphology, and functions of the ASGP-R during receptor-mediated endocytosis. It presents comparisons with other systems of receptor-mediated uptake of macromolecules. The ASGP-R is an integral membrane glycoprotein the isolation of which requires detergent. Under these conditions, the receptor retains a fraction of its original ligand-binding activity. In the presence of nonionic detergent, the ASGP-R from rabbit or rat liver is approximately 250,000 daltons as determined by gel filtration or sedimentation equilibrium analysis. The ASGP-R from each species is a glycoprotein composed of oligosaccharides in N-linkage, primarily to asparagine residues. In addition to oligosaccharide modification, the ASGP-R is posttranslationally modified by the addition of phosphate residues.

Original languageEnglish
Pages (from-to)47-95
Number of pages49
JournalInternational Review of Cytology
Issue numberC
StatePublished - Jan 1 1985


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