Effect of tunicamycin on polarized membrane functions of an established kidney epithelial cell line.

We have explored the relationship between glycoprotein biosynthesis, cell proliferation and function of a differentiated polarized membrane assessed by dome formation in the MDCK epithelial cell line. At 0.1 microgram/ml tunicamycin, complete inhibition of cell proliferation was observed in either serum-containing or serum-free, hormone-supplemented growth medium. By contrast, no inhibition of either spontaneous dome formation or that triggered by inducers of cell differentiation such as hexamethylene bisacetamide was observed at 0.5 microgram/ml tunicamycin, although total glycosylation of cellular proteins was inhibited by 75%. Our results suggest that the polarized sorting out of epithelial membrane proteins to apical and basolateral surfaces and their functions related to vectorial transepithelial fluid transport, monitored by dome formation, can persist unimpaired despite considerable underglycosylation of cellular glycoproteins and inhibition of cell proliferation.