TY - JOUR
T1 - Cell Biology of the Asialoglycoprotein Receptor System
T2 - A Model of Receptor-Mediated Endocytosis
AU - Breitfeld, Philip P.
AU - Simmons, Charles F.
AU - Strous, Ger J.A.M.
AU - Geuze, Hans J.
AU - Schwartz, Alan L.
N1 - Funding Information:
The authors are indebted to their colleagues in their respective laboratories and to Ms. Ireta Ashby for typing the manuscript. The authors were supported by U.S. N.I.H. (GM 32477), the National Foundation, U.S. N.S.F. (INT-8317418), Koningin Wilhelmina Fonds, The Netherlands (UUKC 83-6) and NATO (818/83). A.L.S. was supported as a John A. and George Hartford Foundation Fellow and C.F.S. was supported as a Charles A. Janeway Fellow.
PY - 1985/1/1
Y1 - 1985/1/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0022272208&partnerID=8YFLogxK
U2 - 10.1016/S0074-7696(08)62348-7
DO - 10.1016/S0074-7696(08)62348-7
M3 - Article
C2 - 3000971
AN - SCOPUS:0022272208
SN - 0074-7696
VL - 97
SP - 47
EP - 95
JO - International Review of Cytology
JF - International Review of Cytology
IS - C
ER -