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Volume 272, Number 7, Issue of February 14, 1997 pp. 4195-4200
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

cGMP Stimulation of Cystic Fibrosis Transmembrane Conductance Regulator Cl- Channels Co-expressed with cGMP-dependent Protein Kinase Type II but Not Type Ibeta

(Received for publication, October 2, 1996)

Arie B. Vaandrager Dagger , Ben C. Tilly Dagger , Albert Smolenski , Sonja Schneider-Rasp , Alice G. M. Bot Dagger , Marcel Edixhoven Dagger , Bob J. Scholte par , Thomas Jarchau , Ulrich Walter , Suzanne M. Lohmann , Wolfgang C. Poller and Hugo R. de Jonge Dagger

From the Dagger  Department of Biochemistry, Cardiovascular Research Institute COEUR and the par  Department of Clinical Genetics, Faculty of Medicine and Health Sciences, Erasmus University Rotterdam, 3000 DR Rotterdam, The Netherlands and  Laboratory of Clinical Biochemistry, Medical University Clinic Würzburg, 97080 Würzburg, Germany

In order to investigate the involvement of cGMP-dependent protein kinase (cGK) type II in cGMP-provoked intestinal Cl- secretion, cGMP-dependent activation and phosphorylation of cystic fibrosis transmembrane conductance regulator (CFTR) Cl- channels was analyzed after expression of cGK II or cGK Ibeta in intact cells. An intestinal cell line which stably expresses CFTR (IEC-CF7) but contains no detectable endogenous cGK II was infected with a recombinant adenoviral vector containing the cGK II coding region (Ad-cGK II) resulting in co-expression of active cGK II. In these cells, CFTR was activated by membrane-permeant analogs of cGMP or by the cGMP-elevating hormone atrial natriuretic peptide as measured by 125I- efflux assays and whole-cell patch clamp analysis. In contrast, infection with recombinant adenoviruses expressing cGK Ibeta or luciferase did not convey cGMP sensitivity to CFTR in IEC-CF7 cells. Concordant with the activation of CFTR by only cGK II, infection with Ad-cGK II but not Ad-cGK Ibeta enabled cGMP analogs to increase CFTR phosphorylation in intact cells. These and other data provide evidence that endogenous cGK II is a key mediator of cGMP-provoked activation of CFTR in cells where both proteins are co-localized, e.g. intestinal epithelial cells. Furthermore, they demonstrate that neither the soluble cGK Ibeta nor cAMP-dependent protein kinase are able to substitute for cGK II in this cGMP-regulated function.


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