Abstract
In plants and animals carbohydrate/protein interactions are fundamental to biological function. This form of biomolecular recognition usually involves binding of a carbohydrate ligand to a lectin receptor [1]. One of the well known and thoroughly studied lectin systems in mammals is the asialoglycoprotein receptor (ASGP-R) found on hepatocytes [2–5]. This receptor binds ligands with terminal galactose or N-acetylgalactosamine and routes these to lysosomes before recycling to the cell surface [6]. The natural ligands for the ASGP-R are believed to be serum glycoproteins which lose their terminal sialic acid during circulation exposing clusters of subterminal galactose residues on their N-linked oligosaccharides. Thereby, the ASGP-R is believed to be primarily involved in maintaining the serum concentration of structurally diverse glycoproteins.
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Rice, K.G., Chiu, M.H., Wadhwa, M.S., Thomas, V.H., Stubbs, H.J. (1995). In Vivo Targeting Function of N-Linked Oligosaccharides. In: Alavi, A., Axford, J.S. (eds) Glycoimmunology. Advances in Experimental Medicine and Biology, vol 376. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1885-3_30
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DOI: https://doi.org/10.1007/978-1-4615-1885-3_30
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