The role of protein phosphorylation in alpha2,6(N)-sialyltransferase activity

Abstract

Sialoglycoproteins play a key role in both brain development and neuronal plasticity with their sialylation state being controlled by the sialyltransferase (STN) family of enzymes. In this study, we have determined the role of specific kinase enzymes in the expression and catalytic activity of the alpha2,6 STN (ST6N) isozyme. The catalytic activity was moderately decreased following the inhibition of GSK3beta with LiCl. However, there was a significant increase in catalytic activity following activation of protein kinase C (PKC) by phorbol ester. There was no change in the expression levels of the enzyme protein following any of the treatments. The changes in enzyme catalytic activity were also mirrored by the expression of both protein-bound sialic acid and the polysialic acid oligosaccharide group attached to the neural cell adhesion molecule, NCAM. These results provide further evidence for the role of second messenger-associated kinase enzymes in the modulation of the cell glycosylation potential.