ABSTRACT
In chicks submitted to light stimulation, the synthesis of gangliosides of the retina ganglion cell increases with respect to chicks maintained in the dark. In an attempt to elucidate if the activation of glycosyltransferases participates in the establishment of these light-dark differences detected in vivo, we examined the activity of a key ganglioside glycosyltransferase, the GalNAc-T (N-acetylgalactosaminyltransferase) that converts GM3 to GM2, in the retina ganglion cells isolated from light and dark exposed chicks. We found that GalNAc-T and other glycosyltransferases are active in these ganglion cell preparations; the kinetic parameters for GalNAc-T were similar to those previously reported for chick retina. The other glycosyltransferase activities assayed were the galactosyltransferase (Gal-T2) that converts GM2 to GM1 and the N-acetylneuraminyltransferase (Sialyl-T1) that converts lactosylceramide to GM3. The three glycosyltransferase activities were higher in the ganglion cell preparations obtained from chicks exposed to light compared to those maintained in the dark. For the GalNAc-T activity, the differences disappear when the cell preparations are sonicated or if the assays are carried out in the presence of detergents or if the end product of the reaction is added to the incubates. The results indicate that the activation of the glycosyltransferases is part of the phenomenon required for cells to achieve the precise rate of synthesis of gangliosides needed in vivo.
