Preparation and enzymatic degradation of monosulfogangliotriaosylceramide

Gangliotriaosylceramide 3'-sulfate (GgOse3Cer-II3-sulfate) contains the sugar sequence similar to that of GM2 ganglioside except that the NeuAc in GM2 is replaced by a sulfate group. Due to this structural similarity, we have studied the in vitro synthesis of GgOse3Cer-II3-sulfate using the system for GM2. Our results showed that GgOse3Cer-II3-sulfate could be synthesized from lactosylceramide 3'-sulfate and UDP-GalNAc catalyzed by N-acetylgalactosaminyltransferase prepared from rat brain (Dicesare, J. L., and Dain, J. A. (1971) Biochim. Biophys. Acta 231, 385-393). As in the case of GM2, the GgOse3Cer-II3-sulfate biosynthesized in vitro or isolated from rat kidney could also be cleaved by human beta-hexosaminidase A in the presence of GM2-activator (Li, S.-C., Hirabayashi, Y., and Li, Y.-T. (1981) J. Biol. Chem. 256, 6234-6240). The fact that the GM2-activator could stimulate beta-hexosaminidase A to hydrolyze both GM2 and Gg-Ose3Cer-II3-sulfate indicates that these two glycolipids may be catabolyzed by the same mechanism.