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Transactivation of the IGF‐1R by aldosterone is MR mediated, but transcriptionally independent, and involves activation of Src kinase

Aldosterone, insulin, and insulin‐like growth factor‐1 (IGF‐1) all activate PI‐3 kinase in the Xenopus A6 renal epithelial cell line. Previously, our laboratory has shown that the convergence of these three signaling pathways is prior to PI3‐K, and involves transactivation of the IGF‐1 receptor (IGF‐1R). This transactivation event occurs within 10 minutes of treatment of A6 cells with 1.5μM aldosterone. We have found this transactivation event to be transcriptionally independent since aldosterone‐mediated phosphorylation of Akt, the downstream marker of the IGF‐1R signaling cascade, is the same in the presence of 790nM actinomycin D. Additionally, the mineralo/gluco‐corticoid receptor inhibitors spironolactone or RU‐486, prevent phosphorylation of Akt in the presence of aldosterone. Together, these data show that aldosterone acts in a transcriptionally‐independent, but steroid‐receptor‐dependent manner to cause the rapid transactivation of the IGF‐1R and its signaling cascade. A6 cells were treated with the Src‐family tyrosine kinase inhibitor PP2 to detect changes in Src phosphorylation in the presence and absence of aldosterone, as well as the phosphorylation of Akt and the IGF‐1R. This data shows that PP2 inhibits the action of aldosterone, eliminating Akt phosphorylation. Furthermore, there is a decrease in IGF‐1R phosphorylation in the presence of PP2, suggesting that Src may have a role in activating the receptor in the absence of its ligand.