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1-subunit in HEK-293 cells
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 
-subunit of the
Na+-K+ pump. To analyze specifically the effect
of insulin on the 1-isoform of the pump, we have studied
human embryonic kidney (HEK)-293 cells stably transfected with the rat
Na+-K+ pump 1-isoform tagged on
its first exofacial loop with a hemagglutinin (HA) epitope. The plasma
membrane content of 1-subunits was quantitated by
binding a specific HA antibody to intact cells. Insulin rapidly increased the number of 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 -subunits correlated with an increase in the binding of an
antibody that recognizes only the nonphosphorylated form of
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 1-subunits via a signaling
pathway involving PI 3-kinase and PKC.
ouabain; phosphatidylinositol 3-kinase; protein kinase C; hemagglutinin
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