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 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.
D000818:Animals; D000906:Antibodies; D000936:Antigen-Antibody Complex; D037263:Asialoglycoprotein Receptor; D002462:Cell Membrane / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism*; D007118:Immunoassay; D007700:Kinetics; D008099:Liver / Q000378:metabolism*; D008297:Male; D051381:Rats; D011956:Receptors, Cell Surface / Q000378:metabolism*
D000906:Antibodies; D000936:Antigen-Antibody Complex; D037263:Asialoglycoprotein Receptor; D006023:Glycoproteins; D011956:Receptors, Cell Surface