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Articles in PresS, published online ahead of print October 16, 2002
Am J Physiol Cell Physiol, 10.1152/ajpcell.00398.2002
Submitted on August 29, 2002
Accepted on October 7, 2002
1 Cellular and Molecular Physiology, Yale University, New Haven, CT, USA
* To whom correspondence should be addressed. E-mail: cecilia.canessa{at}yale.edu.
The purpose of this study is to examine the role of the serum- and glucocorticoid-induced kinase (SGK) in the activation of the epithelial sodium channel (ENaC) by aldosterone, vasopressin (AVP) and insulin. We employed a tetracycline-inducible system to control the expression of wild-type (SGKTwt), constitutively active (SGKTS425D), or inactive (SGKTK130M) SGK, in A6 cells independently of hormonal stimulation. The effect of SGK expression on ENaC activity was monitored by measuring transepithelial amiloride-sensitive short circuit current (Isc) of transfected A6 cell lines. Expression of SGKTwt or SGKTS425D and aldosterone stimulation have additive effects on Isc. Although SGK could play some role in the aldosterone response, our results suggest that other mechanisms take place. SGKTS425D abrogates the responses to AVP and insulin hence, in the signaling pathways of these hormones there is a shared step that is stimulated by SGK. Considering that AVP and insulin induce fusion of vesicles to the apical membrane, our results support the notion that SGK promotes incorporation of channels to the apical membrane.
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