Abstract
A powerful approach for studying the relationship of proteoglycan (PG) structure to function employs inhibitors to block glycosaminoglycan (GAG) biosynthesis. Although true enzyme-based, active site-directed inhibitors of the glycosyltransferases and sulfotransferases have not yet been described, decoys consisting of β-D-xylose linked to hydrophobic aglycones have been available for some time (1). As shown over 25 years ago (2), xylosides block PG assembly by serving as alternate substrates, thereby diverting GAG assembly from xylosylated proteoglycan core proteins onto the exogenous xyloside primer. This method of derailing PG biosynthesis has been used to explore PG function in cells, tissues, and animals. The priming of oligosaccharides on xylosides has also been used to define the nature of mutations in cell lines deficient in PG biosynthesis (3-5), to co-localize glycosyltransferases in Golgi subcompartments (6-8), and as a model for glycoside primers that affect other kinds of glycoconjugates (9-12).
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References
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Fritz, T.A., Esko, J.D. (2001). Xyloside Priming of Glycosaminoglycan Biosynthesis and Inhibition of Proteoglycan Assembly. In: Iozzo, R.V. (eds) Proteoglycan Protocols. Methods in Molecular Biology™, vol 171. Humana Press. https://doi.org/10.1385/1-59259-209-0:317
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DOI: https://doi.org/10.1385/1-59259-209-0:317
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