Am J Physiol Cell Physiol Journal of Neurophysiology
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Am J Physiol Cell Physiol 281: C89-C98, 2001;
0363-6143/01 $5.00
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Vol. 281, Issue 1, C89-C98, July 2001

Regulation of ICl,swell in neuroblastoma cells by G protein signaling pathways

Ana Y. Estevez, Tamara Bond, and Kevin Strange

Departments of Anesthesiology and Pharmacology, Anesthesiology Research Division, Laboratories of Cellular and Molecular Physiology, Vanderbilt University Medical Center, Nashville, Tennessee 37232

Guanosine 5'-O-(3-thiotriphosphate) (GTPgamma S) activated the ICl,swell anion channel in N1E115 neuroblastoma cells in a swelling-independent manner. GTPgamma S-induced current was unaffected by ATP removal and broadly selective tyrosine kinase inhibitors, demonstrating that phosphorylation events do not regulate G protein-dependent channel activation. Pertussis toxin had no effect on GTPgamma S-induced current. However, cholera toxin inhibited the current ~70%. Exposure of cells to 8-bromoadenosine 3',5'-cyclic monophosphate did not mimic the effect of cholera toxin, and its inhibitory action was not prevented by treatment of cells with an inhibitor of adenylyl cyclase. These results demonstrate that GTPgamma S does not act through Galpha i/o GTPases and that Galpha s/Gbeta gamma G proteins inhibit the channel and/or channel regulatory mechanisms through cAMP-independent mechanisms. Swelling-induced activation of ICl,swell was stimulated two- to threefold by GTPgamma S and inhibited by 10 mM guanosine 5'-O-(2-thiodiphosphate). The Rho GTPase inhibitor Clostridium difficile toxin B inhibited both GTPgamma S- and swelling-induced activation of ICl,swell. Taken together, these findings indicate that Rho GTPase signaling pathways regulate the ICl,swell channel via phosphorylation-independent mechanisms.

cell volume regulation; Rho GTPase; anion channel


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