Abstract
Glycosaminoglycans (GAGs) including chondroitin sulfate, dermatan sulfate, heparan sulfate, and keratan sulfate, except for hyaluronan that is a free polysaccharide, are covalently attached to core proteins to form proteoglycans. More than 50 gene products are involved in the biosynthesis of GAGs. We recently developed a comprehensive glycosylation mapping tool, GlycoMaple, for visualization and estimation of glycan structures based on gene expression profiles. Using this tool, the expression levels of GAG biosynthetic genes were analyzed in various human tissues as well as tumor tissues. In brain and pancreatic tumors, the pathways for biosynthesis of chondroitin and dermatan sulfate were predicted to be upregulated. In breast cancerous tissues, the pathways for biosynthesis of chondroitin and dermatan sulfate were predicted to be up- and down-regulated, respectively, which are consistent with biochemical findings published in the literature. In addition, the expression levels of the chondroitin sulfate-proteoglycan versican and the dermatan sulfate-proteoglycan decorin were up- and down-regulated, respectively. These findings may provide new insight into GAG profiles in various human diseases including cancerous tumors as well as neurodegenerative disease using GlycoMaple analysis.
Highlights
Glycosaminoglycans (GAGs) are linear polysaccharides consisting of repeating disaccharide units
We focused on GAG biosynthetic pathways
We applied GlycoMaple analysis to visualize the expression of genes involved in GAG biosynthesis and PG levels and to estimate glycan changes based on gene expression
Summary
Glycosaminoglycans (GAGs) are linear polysaccharides consisting of repeating disaccharide units. Among these are heparin, heparan sulfate (HS), chondroitin sulfate (CS), dermatan sulfate (DS), and keratan sulfate (KS), which are covalently bound to core proteins, forming proteoglycans (PGs) (Kjellen and Lindahl, 1991; Iozzo, 1998; Lindahl et al, 2015). CS, DS, and HS are covalently linked to specific serine residues usually flanked by a glycine residue on core proteins via a common linker tetrasaccharide region, GlcAβ1–3Gaβ1– 3Galβ1–4Xylβ1–O–, where GlcA, Gal, and Xyl stand for glucuronic acid, galactose, and xylose, respectively (Lindahl and Rodén, 1972; Sugahara and Kitagawa, 2000). The biosynthesis of the linker tetrasaccharide is initiated by the transfer of β-Xyl from uridine diphosphate
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