ACTIVATION OF UDP-GALACTOSE GLOBOTRIAOSYLCERAMIDE ALPHA-1-3-GALACTOSYLTRANSFERASE DURING PC12D CELL-DIFFERENTIATION INDUCED BY GALACTOSYLCERAMIDE

Citation
T. Ariga et al., ACTIVATION OF UDP-GALACTOSE GLOBOTRIAOSYLCERAMIDE ALPHA-1-3-GALACTOSYLTRANSFERASE DURING PC12D CELL-DIFFERENTIATION INDUCED BY GALACTOSYLCERAMIDE, Biochemistry, 32(31), 1993, pp. 7904-7908
Citations number
48
Categorie Soggetti
Biology
Journal title
ISSN journal
00062960
Volume
32
Issue
31
Year of publication
1993
Pages
7904 - 7908
Database
ISI
SICI code
0006-2960(1993)32:31<7904:AOUGA>2.0.ZU;2-L
Abstract
We measured the activities of UDP-galactose:globotriaosylceramide alph a1-3-galactosyltransferase (alpha-GalTase) and protein kinase C (PKC) in PC12D pheochromocytoma (PC12D) cells which were induced to differen tiation by nerve growth factor (NGF), forskolin (FRK), staurosporine ( STP), retinoic acid (RA), 2-chloroadenosine (ClAd), and/or galactosylc eramide (GalCer). NGF, STP, FRK, and RA were found to be stimulators f or the PKC activity, whereas ClAd appeared to be an inhibitor of the e nzyme. At the concentration of 25 muM, GalCer having normal fatty acid s was found to be a stimulator, whereas GalCer having hydroxy fatty ac ids was ineffective in modulating the PKC activity. Interestingly, all stimulators of PKC activities, including GalCer having normal fatty a cids, appeared to be activators for the alpha-GalTase activity. On the other hand, GalCer having alpha-hydroxy fatty acids had no effect and ClAd was found to be a potent inhibitor for the alpha-GalTase activit y. These data suggest that alpha-GalTase activity during PC12D cell di fferentiation may be regulated by a PKC-dependent process.