The addition of glycosaminoglycans to syndecan is controlled by a series of post- translation events. The preferential site for the addition of glycosaminoglycans is on a serine residue followed by glycine residue, where the linker is attached for the elongation of the glycosaminoglycans by α-N-acetylglucosaminyltransferase I [1]. The linker is composed of four saccharides, first one being xylose, which is an unusual sugar in a unique place, attached to serine of the protein core and sequentially followed by two galactose and a  β-D-glucuronic acid [1, 12].
The addition of glycosaminoglycans to syndecan is regulated through a series of post-translational processes. The most common attachment site for these molecules is on a serine residue followed by glycine, where the linker is attached to enable the extension of glycosaminoglycans by α-N-acetylglucosaminyltransferase I [1]. This linker comprises four sugars, including an unusual xylose residue linked to the protein core and followed by two galactose and a β-D-glucuronic acid [1, 12].