Abstract
Glycosylation is key posttranslational modification for membrane-bound and secreted proteins that can influence both the secondary structure and the function of the protein backbone. In order to investigate the effect of altered cellular glycosylation potential, we have generated a number of clonal cell lines over-expressing the alpha2,3(N) sialyltransferase enzyme (ST3N). In general, there was a decrease in total sialyltransferase (ST) enzyme activity in the clones transfected with the ST3N cDNA, with this decrease being inversely proportional to the quantity of the mRNA coding for the enzyme. The ST3N enzyme was, however, functional and there was an increase in both MAA lectin staining and the expression of polysialic acid, which is attached to the NCAM protein backbone primarily via an alpha2,3 linkage. These results suggest that the overexpression of a sialyltransferase may upset the sialylation potential of the cell.
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