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1 Roudebush Veterans Medical
Center and Biology Department,
Insulin stimulates amiloride-sensitive sodium
transport in models of the distal nephron. Here we demonstrate that, in
the A6 cell line, this action is mediated by the insulin receptor tyrosine kinase and that activation of phosphatidylinositol 3-kinase (PI 3-kinase) lies downstream of the receptor tyrosine kinase. Functionally, a specific inhibitor of PI 3-kinase, LY-294002, blocks
basal as well as insulin-stimulated sodium transport in a
dose-dependent manner (IC50 
6 µM). Biochemically, PI 3-kinase is present in A6 cells and is
inhibited both in vivo and in vitro by LY-294002. Furthermore, a
subsequent potential downstream signaling element, pp70 S6 kinase, is
activated in response to insulin but does not appear to be part of the
pathway involved in insulin-stimulated sodium transport. Together with
previous reports, these results suggest that insulin may induce the
exocytotic insertion of sodium channels into the apical membrane of A6
cells in a PI 3-kinase-mediated manner.
amiloride-sensitive sodium channel; insulin signaling; receptor tyrosine kinase; renal epithelia
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