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Am J Physiol Renal Physiol (December 26, 2006). doi:10.1152/ajprenal.00214.2006
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Submitted on June 13, 2006
Accepted on December 20, 2006

Transactivation of the IGF-1R by aldosterone

Jennifer Holzman1*, Lian Liu1, Billie Jeanne Duke1, Alexandra Kemendy2, and Douglas C. Eaton3

1 Physiology, Emory University Medical School, Atlanta, Georgia, United States
2 Physiology, Emory University School of Medicine, Atlanta, Georgia, United States
3 Department of Physiology, Emory University Medical School, Atlanta, Georgia, United States

* To whom correspondence should be addressed. E-mail: jlholzm{at}learnlink.emory.edu.

Activation of epithelial sodium channels (ENaC) by aldosterone, insulin, or insulin-like growth factor-1 (IGF-1) in renal epithelial cells (including the Xenopus renal cell line, A6) appears to share some common signaling elements subsequent to the initial insulin or IGF-1 receptor activation. Previously, the convergence point for insulin or IGF-1 and aldosterone signaling was assumed to be downstream of the receptor at the level of phosphatidylinositol 3-kinase (PI3-K); however, this study shows aldosterone directly transactivates the IGF-1 receptor (IGF-1R). In A6 cells, 10 minute exposure to aldosterone increased the phosphorylation of the IGF-1 receptor, insulin receptor substrate-1 (IRS-1), and Akt (protein kinase B, PKB). Furthermore, aldosterone activated PI3-K and phosphorylation of the most downstream element, Akt, was blocked by the specific PI3-K inhibitor LY-294002. Transactivation requires aldosterone binding to the mineralocorticoid/glucocorticoid receptor and does not require transcription.




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