ABSTRACT
If one views in vivo AA amyloidogenesis, in part, as an interactive process between the amyloidogenic protein serum amyloid A and the common components, such as heparan sulfate proteoglycan, then the identification of the complementary binding faces on these two molecules should provide information for the design and synthesis of molecules that will interfere with this interaction. Heparan sulfate biosynthesis takes place in the Golgi where a serine residue(s) in the protein moiety of the proteoglycan serves as an attachment point for the synthesis of a tetrasaccharide composed of xylose-galactose-galactose-glucuronate, the xylose being linked to the serine. The enzymatic addition of the N-acetylglucosamine to the glucuronate at the growing end of the polysaccharide chain takes place through an appropriate transferase that utilizes the UDP activated form of N-acetylglucosamine linking its C-1 hydroxyl to the C-4 hydroxyl of the glucuronate.
