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Volume 271, Number 35, Issue of August 30, 1996 pp. 21160-21166
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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The Major Subunit of the Asialoglycoprotein Receptor Is Expressed on the Hepatocellular Surface in Mice Lacking the Minor Receptor Subunit

(Received for publication, December 26, 1995, and in revised form, June 6, 1996)

From the Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas Texas 75235, the ^¶ Third Department of Internal Medicine, Faculty of Medicine, University of Tokyo, 7-3-1 Hongo, Bunkyoku, Tokyo 113, Japan, and the ^'' NIDDK, National Institutes of Health, Bethesda, Maryland 20892

The mammalian asialoglycoprotein receptor (ASGPR) is located on the sinusoidal membrane of hepatocytes where it binds and endocytoses galactose-terminated glycoproteins (asialoglycoproteins). ASGPR is composed of two highly homologous subunits, termed hepatic lectin 1 and 2. Despite numerous studies the contribution of both subunits to biosynthesis and functional activity of ASGPR in vivo has remained controversial. Mice lacking the murine hepatic lectin (MHL)-2 subunit are viable and fertile without obvious phenotypic abnormalities. In the absence of MHL-2, knockout mice express MHL-1 protein at reduced levels. Here, we examine the intracellular fate and function of this remaining subunit. The results show that MHL-1 reaches the hepatocellular surface in knockout mice but is unable to effectively remove any one of three different radiolabeled ligands within 30 min. A small but detectable residual ligand clearance in knockout mice at 4 h is apparently not mediated by remaining MHL-1. Serum concentrations of galactose-terminating glycoproteins are not elevated in these ASGPR-deficient mice. However, competitive in vitro degradation experiments suggest that other endogenous ASGPR ligands, the nature of which remain to be determined, accumulate in serum of knockout animals.

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