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Am J Physiol Renal Physiol 286: F86-F93, 2004. First published September 16, 2003; doi:10.1152/ajprenal.00161.2003
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Regulation of sodium-dicarboxylate cotransporter-3 from winter flounder kidney by protein kinase C

Yohannes Hagos, Birgitta C. Burckhardt, Alexander Larsen, Christian Mathys, Tobias Gronow, Andrew Bahn, Natascha A. Wolff, Gerhard Burckhardt, and Jürgen Steffgen

Zentrum Physiologie und Pathophysiologie, Abt. Vegetative Physiologie und Pathophysiologie, 37073 Göttingen, Germany

Submitted 26 January 2003 ; accepted in final form 11 September 2003

The sodium dicarboxylate cotransporter located at the basolateral side supplies renal proximal tubule cells with Krebs cycle intermediates and maintains the driving force for the exchange of organic anions like PAH against {alpha}-ketoglutarate through the organic anion transporter-1. Recently, we cloned sodium dicarboxylate cotransporter-3 from winter flounder kidney (fNaDC-3). To understand the regulation of fNaDC-3, we preincubated fNaDC-3-expressing oocytes with PMA, a PKC activator. PMA dose and time dependently inhibited fNaDC-3-mediated succinate uptake. Simultaneous preincubation of fNaDC-3-expressing oocytes with 50 nM PMA and either staurosporine or RO 31-8220 for 30 min attenuated PKC-mediated inhibition of succinate uptake. Site-directed mutagenesis of the five putative PKC sites (S7, T167, S174, T188, and S396) resulted in no change in PKC-mediated inhibition of the transporter. In electrophysiological studies performed at -60 mV, the K0.5 for succinate was not significantly affected (56 ± 13 vs. 42 ± 19 µM), but {Delta}Imax was reduced from -139 ± 49 to -20 ± 8 nA by PMA (50 nM, 30 min). Immunofluorescence analysis of fNaDC-3-expressing oocytes revealed that PMA leads to an endocytosis of fNaDC-3 protein. In conclusion, fNaDC-3 expressed in oocytes is downregulated by PMA through endocytosis. PKC consensus sites appear not to be important for this process.

endocytosis; phorbol 12-myristate 13-acetate


Address for reprint requests and other correspondence: Y. Hagos, Zentrum Physiologie und Pathophysiologie, Abt. Vegetative Physiologie und Pathophysiologie, Universität Göttingen, Humboldtallee 23, 37073 Göttingen, Germany (E-mail: hagos{at}veg-physiol.med.uni-goettingen.de).




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