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Articles in PresS, published online ahead of print November 12, 2002
Am J Physiol Renal Physiol, 10.1152/ajprenal.00299.2002
Submitted on August 19, 2002
Accepted on November 1, 2002
1 Department of Physiology, Dartmouth Medical School, Lebanon, NH, USA
* To whom correspondence should be addressed. E-mail: aniko.fejes-toth{at}dartmouth.edu.
To study the role of SGK1 in mammalian cells, we compared sodium transport rates in wild type (WT) M-1 cortical collecting duct (CCD) cells to M-1 populations stably expressing human full-length (FL)-SGK1, NH2-terminal truncated (
N-60)-SGK1, "kinase-dead" (K127M)-SGK1, and cells which have down-regulated levels of SGK1 mRNA (antisense SGK1). Basal rates of transepithelial Na+ transport were highest in FL-SGK1 populations, compared amongst above populations. Dexamethasone (Dex) treatment increased Na+ transport in WT and FL-SGK1 cells 2.7- and 2-fold, respectively. Modest stimulation of sodium absorption was detected after Dex treatment in N-60-SGK1 populations. However, N-60-SGK1 transport rates remained substantially lower than WT values. Importantly, a combination of high insulin, Dex, and serum failed to significantly stimulate Na+ transport in antisense or K127M-SGK1 cells. Additionally, expression of antisense SGK1 significantly decreased transepithelial resistance values. Overall, we concluded that SGK1 is a critical component in corticosteroid regulated Na+ transport in mammalian CCD cells. Furthermore, our data suggests that the NH2-terminal of SGK1 may contain a Phox homology-like domain that may be necessary for effective Na+ transport.
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