Vandamme V, Pierce A, Verbert A, Delannoy P
Laboratoire de Chimie Biologique (UMR n. 111 du Centre National de la Recherche Scientifique), Université des Sciences et Technologies de Lille, Villeneuve d'Ascq, France.
Eur J Biochem. 1993 Jan 15;211(1-2):135-40. doi: 10.1111/j.1432-1033.1993.tb19879.x.
The beta-galactoside alpha-2,6-sialyltransferase activity of Fisher rat fibroblasts is enhanced by dexamethasone while the activity of the beta-galactoside alpha-2,3-sialyltransferase remains unchanged. This glucocorticoid-dependent activation can be inhibited by the antagonist RU 38,486 and results from an elevated transcription rate of the 4.7-kb mRNA previously characterized in rat fibroblasts, distinct from the 4.3-kb liver-restricted mRNA. As shown by the binding of radiolabelled Sambucus nigra agglutinin, this activation leads to an increase of NeuNAc(alpha 2-6)Gal sequences on glycoproteins isolated from the dexamethasone-treated cells.