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Am J Physiol Cell Physiol 278: C1047-C1054, 2000;
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Vol. 278, Issue 5, C1047-C1054, May 2000

Kinase regulation of hENaC mediated through a region in the COOH-terminal portion of the alpha -subunit

Kenneth A. Volk, Russell F. Husted, Peter M. Snyder, and John B. Stokes

Department of Internal Medicine, University of Iowa and Department of Veterans Affairs Medical Center, Iowa City, Iowa 52242

In an effort to gain insight into how kinases might regulate epithelial Na+ channel (ENaC) activity, we expressed human ENaC (hENaC) in Xenopus oocytes and examined the effect of agents that modulate the activity of some kinases. Activation of protein kinase C (PKC) by phorbol ester increased the activity of ENaC, but only in oocytes with a baseline current of <2,000 nA. Inhibitors of protein kinases produced varying effects. Chelerythrine, an inhibitor of PKC, produced a significant inhibition of ENaC current, but calphostin C, another PKC inhibitor, had no effect. The PKA/protein kinase G inhibitor H-8 had no effect, whereas the p38 mitogen-activated protein kinase inhibitor, SB-203580 had a significant inhibitory effect. Staurosporine, a nonspecific kinase inhibitor, was the most potent tested. It inhibited ENaC currents in both oocytes and in M-1 cells, a model for the collecting duct. Site-directed mutagenesis revealed that the staurosporine effect did not require an intact COOH terminus of either the beta - or gamma -hENaC subunit. However, an intact COOH terminus of the alpha -subunit was required for this effect. These results suggest that an integrated kinase network regulates ENaC activity through an action that requires a portion of the alpha -subunit.

epithelial sodium channel; protein kinase C; staurosporine; mutation; heterologous expression; M-1 cells; oocyte expression


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