Immunological Evidence for the Transmembrane Nature of the Rat Liver Receptor for Asialoglycoproteins

Antibodies raised in goats against the rat hepatic receptor for desialylated glycoproteins were perfused through a rat liver and were specifically retained by the liver. These antireceptor antibodies also bound specifically to hepatocyte plasma membranes oriented with their cytoplasmic surface outwa...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1981-03, Vol.78 (3), p.1557-1561
Main Authors: Harford, Joe, Ashwell, G. Gilbert
Format: Article
Language:English
Subjects:
Animals
Antibodies
Antigen-Antibody Complex
Asialoglycoprotein Receptor
Asialoglycoproteins
Cell Membrane - metabolism
Cell membranes
Gels
Glycoproteins - metabolism
Hepatocytes
Immunoassay
Kinetics
Ligands
Liver
Liver - metabolism
Male
P branes
Perfusion
Rats
Receptors
Receptors, Cell Surface - metabolism
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Summary:Antibodies raised in goats against the rat hepatic receptor for desialylated glycoproteins were perfused through a rat liver and were specifically retained by the liver. These antireceptor antibodies also bound specifically to hepatocyte plasma membranes oriented with their cytoplasmic surface outward on polylysine-derivatized beads. These two phenomena were judged to be properties of distinct subpopulations of the antibody preparation because: (i) maximal adsorption of antibodies with membranes on polylysine beads did not affect subsequent retention by the perfused liver, and (ii) whereas perfusion resulted in a depletion of antibodies capable of blocking ligand binding, adsorption by the everted membrane preparation led to a relative enrichment of blocking antibodies. These results are interpreted as indicative of distinct antigenic determinants of the receptor being present on the two faces of the membrane and demonstrate a transbilayer disposition of the asialoglycoprotein receptor.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.78.3.1557