Transient expression of a p58 protein kinase cDNA enhances mammalian glycosyltransferase activity.
The effect of expression of a p58 protein kinase on mammalian beta-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.
Bunnell
B A
BA
Department of Microbiology, University of Alabama at Birmingham 35294.
Adams
D E
DE
Kidd
V J
VJ
D000818:Animals; D015152:Blotting, Northern; D015153:Blotting, Western; D002460:Cell Line; D002522:Chlorocebus aethiops; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D015180:Electrophoresis, Gel, Two-Dimensional; D004789:Enzyme Activation; D005700:Galactosyltransferases / Q000378:metabolism*; D015870:Gene Expression; D066298:In Vitro Techniques; D008970:Molecular Weight; D010766:Phosphorylation; D010957:Plasmids; D011494:Protein Kinases / Q000502:physiology*
D004247:DNA; D005700:Galactosyltransferases; D011494:Protein Kinases