Abstract
The general features of the biosynthetic assembly of all proteoglycans (see refs. 1–9 for reviews), except the keratan sulfate portions of cartilage and cornea (see Note 1), consist of sequential: (1) synthesis of the core protein; (2) xylosylation of specific Ser moieties of the core protein; (3) addition of two galactose (Gal) residues to the xylose (Xyl); (4) completion of a common tetrasaccharide linkage region by addition of a glucuronic acid (GlcA) residue; (5) addition of an N-acetylgalactosamine (GalNAc) or N-acetylglucosamine (GlcNAc) residue to initiate the chondroitin/dermatan or heparan glycosaminoglycan, respectively; (6) repeat addition of hexosamine residues alternating with GlcA residues to form the large heteropolymer glycosaminoglycan chains; and (7) modification of these glycosaminoglycan chains by variable N-deacetylation/N-sulfation, and/or O-sulfation, and variable epimerization of GlcA to iduronic acid (IdceA). The Xyl may occasionally be 2-phosphorylated in some chondroitin sulfate (10) and heparan sulfate (11), and one or both of the Gal residues of the chondroitin sulfate linkage region may be 4-O- (12) or 6-O-sulfated (13). However, Gal sulfation has not been found in the identical oligosaccharide linkage region of heparin/heparan sulfate (14). In addition, glycoprotein-like N-linked glycosylation and/or O-linked glycosylation takes place before or while the synthesis of the oligosaccharide linkage region and glycosaminoglycans are being formed.
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Sugumaran, G., Silbert, J.E. (2001). Particulate and Soluble Glycosaminoglycan-Synthesizing Enzymes. In: Iozzo, R.V. (eds) Proteoglycan Protocols. Methods in Molecular Biology™, vol 171. Humana Press. https://doi.org/10.1385/1-59259-209-0:103
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DOI: https://doi.org/10.1385/1-59259-209-0:103
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