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In Vivo Targeting Function of N-Linked Oligosaccharides

Pharmacokinetic and Biodistribution of N-linked Oligosaccharides

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Glycoimmunology

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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© 1995 Springer Science+Business Media New York

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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

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-5768-1

  • Online ISBN: 978-1-4615-1885-3

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