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Endocytosis and Function of the Hepatic Asialoglycoprotein Receptor

  • Paul H. Weigel
Chapter
Part of the Subcellular Biochemistry book series (SCBI, volume 19)

Abstract

When desialylated, plasma glycoproteins, including some hormones, become ligands for recognition by this galactosyl (Gal) receptor (Ashwell and Harford, 1982; Schwartz, 1984). The interaction of the receptor with most ligands is of high affinity; dissociation constants are in the nM range. The ligand used most predominantly is desialylated αl-acid glycoprotein (also called orosomucoid), which is a soluble-plasma acute-phase protein. Neoglycoproteins, synthetic polymers, or solid surfaces containing a sufficient density of Gal groups will also be bound by the receptor. The receptor is found only in hepatocytes. Only 10–25% of the total cellular receptors are on the cell surface, while 75–90% are inside the cell. There are about a half-million receptors per cell. The receptor recycles both in vivo and in vitro. Ligand dissociation occurs below pH 6, and Ca2+ is required for binding. Oligosaccharide binding to the receptor requires a relatively high Ca2+ concentration; the apparent Kd is approximately 1.5 mM, and about 3Ca2+ are bound/polypeptide chain of the rabbit receptor (Andersen et al., 1982). Very little ligand binding (<1%) occurs in the absence of Ca2+ or the presence of chelators such as ethylenediaminetetraacetic acid (EDTA). This fact is often used as the basis for most easily determining the nonspecific binding of radiolabeled ligands.

Keywords

Kupffer Cell Lysosomal Enzyme Asialoglycoprotein Receptor Receptor Recycling Ligand Dissociation 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Paul H. Weigel
    • 1
  1. 1.Department of Human Biological Chemistry and GeneticsUniversity of Texas Medical BranchGalvestonUSA

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