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Am J Physiol Renal Physiol 277: F580-F586, 1999;
0363-6127/99 $5.00
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Vol. 277, Issue 4, F580-F586, October 1999

Regulation of the renal Na-HCO3 cotransporter. XI. Signal transduction underlying CO2 stimulation

Ofelia S. Ruiz, R. Brooks Robey, Yi-Yong Qiu, Long Jiang Wang, Cheng Jin Li, Jianfei Ma, and Jose A. L. Arruda

University of Illinois at Chicago, College of Medicine, and Chicago Veterans Affairs Health Care System, West Side Division, Chicago, Illinois 60612-7315

We have previously shown that CO2 stimulation of the renal Na-HCO3 cotransporter (NBC) activity is abrogated by general inhibitors of protein tyrosine kinases. The more selective inhibitor herbimycin also blocked this effect at concentrations known to preferentially inhibit Src family kinases (SFKs). We therefore examined a role for SFKs in CO2-stimulated NBC activity. To this end, we engineered OK cells to express the COOH-terminal Src kinase (Csk), a negative regulator of SFKs. CO2 stimulated NBC activity normally in beta -galactosidase-expressing and untransfected control cells. In contrast, Csk-expressing cells had normal baseline NBC activity that was not stimulated by CO2. CO2 stimulation increased both total SFK activity and specific tyrosine phosphorylation of Src. The specific MEK1/2 inhibitor PD-98059 completely inhibited the CO2 stimulation of NBC activity as well as the accompanying phosphorylation and activation of ERK1/2. Our data suggest the involvement of both SFKs, probably Src, and the "classic" MAPK pathway in mediating CO2-stimulated NBC activity in renal epithelial cells.

Src family kinase; ERK1/2 kinase; phosphorylation


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