Transient expression of a p58 protein kinase cDNA enhances mammalian glycosyltransferase activity

• Published in: Biochemical and biophysical research communications Vol. 171; no. 1; pp. 196 - 203
• Main Authors: Bunnell, Bruce A., Adams, Donald E., Kidd, Vincent J.
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 31.08.1990; Elsevier
• Subjects: Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Blotting, Northern; Blotting, Western; Cell Line; Cercopithecus aethiops; Cloning, Molecular; DNA - genetics; Electrophoresis, Gel, Two-Dimensional; Enzyme Activation; Enzymes and enzyme inhibitors; Fundamental and applied biological sciences. Psychology; Galactosyltransferases - metabolism; Gene Expression; In Vitro Techniques; Molecular Weight; Phosphorylation; Plasmids; Protein Kinases - physiology; Transferases; GalTase; CHO; GTA; MMTV-LTR; CAT; Construction; Phosphorylation; Enzyme; Activation; Gene expression; Immunological method; Plasmid; Autoradiography; Vertebrata; Cell line; Mammalia; Enzymatic activity; Protein kinase
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/0006-291X(90)91376-4

The effect of expression of a p58 protein kinase on mammalian β-1,4 galactosyltransferase enzyme activity was examined in vitro and in vivo . We found that p58 protein kinase expression enhanced galactosyltransferase enzyme activity approximately three-fold in vivo when compared to reporter gene activity. Galactosyltransferase enzyme activity was also substantially reduced in vitro when dephosphorylated, or when p58 specific antibodies were used to inhibit kinase activity. These results suggest that galactosyltransferase activity is influenced by phosphorylation, and that the p58 protein kinase may mediate this effect.