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Am J Physiol Renal Physiol 282: F669-F679, 2002. First published October 30, 2001; doi:10.1152/ajprenal.00159.2001
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Vol. 282, Issue 4, F669-F679, April 2002

Aldosterone interaction with epidermal growth factor receptor signaling in MDCK cells

Michael Gekle, Ruth Freudinger, Sigrid Mildenberger, and Stefan Silbernagl

Physiologisches Institut, University of Würzburg, 97070 Würzburg, Germany

Epidermal growth factor (EGF) regulates cell proliferation, differentiation, and ion transport by using extracellular signal-regulated kinase (ERK)1/2 as a downstream signal. Furthermore, the EGF-receptor (EGF-R) is involved in signaling by G protein-coupled receptors, growth hormone, and cytokines by means of transactivation. It has been suggested that steroids interact with peptide hormones, in part, by rapid, potentially nongenomic, mechanisms. Previously, we have shown that aldosterone modulates Na+/H+ exchange in Madin-Darby canine kidney (MDCK) cells by means of ERK1/2 in a way similar to growth factors. Here, we tested the hypothesis that aldosterone uses the EGF-R as a heterologous signal transducer in MDCK cells. Nanomolar concentrations of aldosterone induce a rapid increase in ERK1/2 phosphorylation, cellular Ca2+ concentration, and Na+/H+ exchange activity similar to increases induced by EGF. Furthermore, aldosterone induced a rapid increase in EGF-R-Tyr phosphorylation, and inhibition of EGF-R kinase abolished aldosterone-induced signaling. Inhibition of ERK1/2 phosphorylation reduced the Ca2+ response, whereas prevention of Ca2+ influx did not abolish ERK1/2 phosphorylation. Our data show that aldosterone uses the EGF-R-ERK1/2 signaling cascade to elicit its rapid effects in MDCK cells.

epidermal growth factor; aldosterone; extracellular signal-regulated kinase 1/2; calcium; Madin-Darby canine kidney cells


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