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Am J Physiol Cell Physiol 275: C958-C966, 1998;
0363-6143/98 $5.00
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Vol. 275, Issue 4, C958-C966, October 1998

Cystic fibrosis transmembrane conductance regulator activation by cAMP-independent mechanisms

Zhaoping He1, Sasikala Raman1, Yi Guo1, and William W. Reenstra1,2

Departments of 1 Clinical Science and 2 Pediatrics, Alfred I. duPont Hospital for Children, Thomas Jefferson University, Wilmington, Delaware 19803

Recent studies have demonstrated that several compounds with diverse structures can activate wild-type cystic fibrosis transmembrane conductance regulator (CFTR) by non-receptor-mediated mechanisms. Some of these compounds have been shown to enhance cAMP-dependent activation of Delta F508-CFTR. This study was undertaken to compare the mechanisms by which genistein, IBMX, milrinone, 8-cyclopentyl-1,3-dipropylxanthine (CPX), the benzimidazolone NS004, and calyculin A increase CFTR activity. Our studies demonstrate that, in transfected NIH-3T3 cells, maximal enhancements of forskolin-dependent Delta F508-CFTR activity are greatest with genistein, IBMX, and NS004. Milrinone, genistein, CPX, NS004, and calyculin A do not increase cellular cAMP. Because forskolin and calyculin A increase in vivo phosphorylation of cAMP binding response element (CREB), the inability of milrinone, genistein, CPX, and NS004 to increase CREB phosphorylation suggests that they do not stimulate protein kinase A or inhibit phosphatase activity. Our data suggest that the mechanisms by which genistein and NS004 activate CFTR differ. We also demonstrate that, in NIH-3T3 cells, IBMX-dependent enhancement of cAMP-dependent CFTR activity is not due to an increase in cellular cAMP and may involve a mechanism like that of genistein.

genistein; 3-isobutyl-1-methylxanthine; in vivo phosphorylation; adenosine 3',5'-cyclic monophosphate


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