UPD-galactose:ceramide galactosyltransferase activity in dissociated cell cultures from brain hemispheres of newborn rats.

Primary cultures enriched in oligodendroglial cells were prepared from dissociated newborn rat brain. Enzymatic study revealed the presence of high specific activities of UDP-galactose:ceramide galactosyltransferase (CGalT) and 2',3'-cyclic nucleotide-3'-phosphohydrolase (CNP). The specific activity of CGalT was twice as high as that of brain. The CGalT activity increased from 16 days in culture, reached a maximum at about 50 days and declined thereafter. The CNP activity reached a maximum after 60-70 days in culture and remained more or less stable in the following period. The results indicate that in oligodendroglial cells in vitro the regulation of CGalT activity proceeds in a manner similar to that of myelinating brain.