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1 Biology Department, Indiana University-Purdue University at Indianapolis, Indianapolis, Indiana 46202; 2 Diabetes Branch, Division of Intramural Research, National Institute of Diabetes and Digestive and Kidney Diseases, Bethesda, Maryland 20892; and 3 Dipartimento di Medicina Sperimentale e Clinica "G. Salvatore," Universita di Catanzaro, Catanzaro, 88100 Italy
To study the role of sgk (serum, glucocorticoid-induced kinase) in hormonal regulation of Na+ transport mediated by the epithelial Na+ channel (ENaC), clonal cell lines stably expressing human sgk, an S422A sgk mutant, or a D222A sgk mutant were created in the background of the A6 model renal epithelial cell line. Expression of normal sgk results in a 3.5-fold enhancement of basal transport and potentiation of the natriferic response to antidiuretic hormone (ADH). Transfection of a S422A mutant form of sgk, which cannot be phosphorylated by phosphatidylinositol-dependent kinase (PDK)-2, results in a cell line that is indistinguishable from the parent line in basal and hormone-stimulated Na+ transport. The D222A sgk mutant, which lacks kinase activity, functions as a dominant-negative mutant inhibiting basal as well as peptide- and steroid hormone-stimulated Na+ transport. Thus sgk activity is necessary for ENaC-mediated Na+ transport. Phosphorylation and activation by PDK-2 are necessary for sgk stimulation of ENaC. Expression of normal sgk over endogenous levels results in a potentiated natriferic response to ADH, suggesting that the enzyme is a rate-limiting step for the hormone response. In contrast, sgk does not appear to be the rate-limiting step for the cellular response to aldosterone or insulin.
insulin; antidiuretic hormone; aldosterone; amiloride; phosphoinositide pathway; epithelial Na+ channel; serum and glucocortoid-induced kinase
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