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Articles in PresS, published online ahead of print July 9, 2002
Am J Physiol Endocrinol Metab, 10.1152/ajpendo.00021.2002
Submitted on January 22, 2002
Accepted on July 8, 2002
1 Department of Internal Medicine, University of Iowa, Iowa City, IA, USA
2 Department of Internal Medicine, University of Iowa, Iowa City, IA, USA; Veterans Affairs Medical Center, Iowa City, IA, USA
* To whom correspondence should be addressed. E-mail: christie-thomas{at}uiowa.edu.
In lung and collecting duct epithelia, glucocorticoid-stimulated Na+ transport is preceded by an increase in the protein kinase, sgk1, which, in turn, regulates the activity of the epithelial Na+ channel (ENaC). We investigated the mechanism for glucocorticoid-regulated human sgk1 expression in lung and renal epithelia. Sgk1 mRNA was increased in these epithelia by glucocorticoids and this was inhibited by actinomycin D and superinduced by cycloheximide, consistent with a transcriptional effect that did not require protein synthesis. To understand the basis for transcriptional regulation, the transcription initiation site was mapped and the 5' flanking region cloned by PCR. A 3 kb fragment of the upstream region was coupled to luciferase and transfected into A549 cells. By deletion analysis an imperfect GRE was identified that was necessary and sufficient for GC-responsiveness. When tested with cell extracts, a specific protein recognized by an anti-GR antibody bound the GRE in gel-mobility-shift assays. We conclude that glucocorticoids stimulate sgk1 expression in human epithelial cells via activation of a GRE in the 5' flanking region of sgk1.
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