Abstract
Several glycosyltransferases participating in ganglioside biosynthesis were measured in Golgi-rich fractions from rat liver. Addition of those UDP-amino sugars to the enzyme assays which accumulate in liver after treatment of rats with d-galactosamine inhibited the transferases to different degrees. The simultaneous presence of UDP-GalN, UDP-GalNAc, UDP-GlcN, and UDP-GlcNAc in concentrations resembling their overall content in livers 6 h after d-galactosamine administration led to an inhibition of the glycolipid galactosyltransferases, G 12 and G M1 synthases of 44 and 64%, respectively. G M2 synthase was moderately inhibited whereas the sialyltransferases (G M3, G D3, and G D1a synthases) were almost unimpaired. Induction of liver cell damage by d-galactosamine did not cause any change of glycosyltransferase activities as determined in rat liver homogenates and Golgi-rich fractions. These results indicate a possible role for UDP-amino sugars in the depression of ganglioside biosynthesis observed in vivo after GalN administration.
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