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Am J Physiol Cell Physiol 281: C1797-C1803, 2001;
0363-6143/01 $5.00
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Vol. 281, Issue 6, C1797-C1803, December 2001

Insulin increases plasma membrane content and reduces phosphorylation of Na+-K+ pump alpha 1-subunit in HEK-293 cells

Gary Sweeney1,2, Wenyan Niu1, Victor A. Canfield3, Robert Levenson3, and Amira Klip1

1 Programme in Cell Biology, Hospital for Sick Children, Toronto M5G 1X8; 2 Department of Biology, York University, Toronto, Ontario, Canada M3J 1P3; and 3 Department of Pharmacology, The Milton S. Hershey Medical Center, The Pennsylvania State University College of Medicine, Hershey, Pennsylvania 17033

Insulin stimulates K+ uptake and Na+ efflux via the Na+-K+ pump in kidney, skeletal muscle, and brain. The mechanism of insulin action in these tissues differs, in part, because of differences in the isoform complement of the catalytic alpha -subunit of the Na+-K+ pump. To analyze specifically the effect of insulin on the alpha 1-isoform of the pump, we have studied human embryonic kidney (HEK)-293 cells stably transfected with the rat Na+-K+ pump alpha 1-isoform tagged on its first exofacial loop with a hemagglutinin (HA) epitope. The plasma membrane content of alpha 1-subunits was quantitated by binding a specific HA antibody to intact cells. Insulin rapidly increased the number of alpha 1-subunits at the cell surface. This gain was sensitive to the phosphatidylinositol (PI) 3-kinase inhibitor wortmannin and to the protein kinase C (PKC) inhibitor bisindolylmaleimide. Furthermore, the insulin-stimulated gain in surface alpha -subunits correlated with an increase in the binding of an antibody that recognizes only the nonphosphorylated form of alpha 1 (at serine-18). These results suggest that insulin regulates the Na+-K+ pump in HEK-293 cells, at least in part, by decreasing serine phosphorylation and increasing plasma membrane content of alpha 1-subunits via a signaling pathway involving PI 3-kinase and PKC.

ouabain; phosphatidylinositol 3-kinase; protein kinase C; hemagglutinin


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