Abstract
The functions of heparan sulfate (HS) are determined by specific saccharide motifs within HS chains. These sequences confer selective protein-binding properties and the ability to modulate protein bioactivities (1,2). HS chains consist of an alternating disaccharide repeat of glucosamine (GlcN; N-acetylated or N-sulfated) and uronic acid (glucuronic [GlcA] or iduronic acid [IdoA]). The initial biosynthetic product containing N-acetylglucosamine (GlcNAc) and GlcA is modified by N-sulfation of the GlcN, ester (O)-sulfation (at positions 3 and 6 on the GlcN and at position 2 on the uronic acids) and by epimerization of GlcA to IdoA. The extent of these modifications is incomplete, and their degree and distribution varies in HS between different cell types. In HS chains, N- and O-sulfated sugars are predominantly clustered in sequences of up to 8 disaccharides separated by N-acetyl-rich regions with a low sulfate content (3).
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© 2001 Humana Press Inc., Totowa, NJ
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Turnbull, J.E. (2001). Integral Glycan Sequencing of Heparan Sulfate and Heparin Saccharides. In: Iozzo, R.V. (eds) Proteoglycan Protocols. Methods in Molecular Biology™, vol 171. Humana Press. https://doi.org/10.1385/1-59259-209-0:129
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DOI: https://doi.org/10.1385/1-59259-209-0:129
Publisher Name: Humana Press
Print ISBN: 978-0-89603-759-5
Online ISBN: 978-1-59259-209-8
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