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Am J Physiol Cell Physiol 277: C531-C536, 1999;
0363-6143/99 $5.00
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Vol. 277, Issue 3, C531-C536, September 1999

Phosphoinositide 3-kinase is required for aldosterone-regulated sodium reabsorption

Bonnie L. Blazer-Yost1, Teodor G. Păunescu2, Sandy I. Helman2, Kimberly D. Lee1, and Chris J. Vlahos3

1 Biology Department, Indiana University, Purdue University at Indianapolis, Indianapolis 46202; 3 Lilly Research Laboratories, Eli Lilly and Company, Indianapolis, Indiana 46285; and 2 Department of Molecular and Integrative Physiology, University of Illinois at Urbana-Champaign, Urbana, Illinois 61801

Aldosterone, a steroid hormone, regulates renal Na+ reabsorption and, therefore, plays an important role in the maintenance of salt and water balance. In a model renal epithelial cell line (A6) we have found that phosphoinositide 3-kinase (PI 3-kinase) activity is required for aldosterone-stimulated Na+ reabsorption. Inhibition of PI 3-kinase by the specific inhibitor LY-294002 markedly reduces both basal and aldosterone-stimulated Na+ transport. Further, one of the products of PI 3-kinase, phosphatidylinositol 3,4,5-trisphosphate, is increased in response to aldosterone in intact A6 monolayers. This increase occurs just before the manifestation of the functional effect of the hormone and is also inhibited by LY-294002. With the use of blocker-induced noise analysis, it has been demonstrated that inhibition of phosphoinositide formation causes an inhibition of Na+ entry in both control and aldosterone-pretreated cultures by reducing the number of open functional epithelial Na+ channels (ENaCs) in the apical membrane of the A6 cells. These novel observations indicate that phosphoinositides are required for ENaC expression and suggest a mechanism for aldosterone regulation of channel function.

epithelial sodium channels; noise analysis; electrophysiology; kidney; cortical collecting ducts; A6 cell line


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