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Originally published In Press as doi:10.1074/jbc.M009403200 on January 17, 2001

J. Biol. Chem., Vol. 276, Issue 15, 12147-12152, April 13, 2001
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The Water Channel Aquaporin-8 Is Mainly Intracellular in Rat Hepatocytes, and Its Plasma Membrane Insertion Is Stimulated by Cyclic AMP*

Fabiana GarcíaDagger , Arlinet KierbelDagger , M. Cecilia LaroccaDagger , Sergio A. GradiloneDagger , Patrick Splinter§, Nicholas F. LaRusso§, and Raúl A. MarinelliDagger

From the Dagger  Instituto de Fisiología Experimental, Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Universidad Nacional de Rosario, Rosario, Santa Fe, Argentina 2000 and the § Center for Basic Research in Digestive Diseases, Departments of Internal Medicine and Biochemistry and Molecular Biology, Mayo Medical School, Clinic, and Foundation, Rochester, Minnesota 55905

We previously found that water transport across hepatocyte plasma membranes occurs mainly via a non-channel mediated pathway. Recently, it has been reported that mRNA for the water channel, aquaporin-8 (AQP8), is present in hepatocytes. To further explore this issue, we studied protein expression, subcellular localization, and regulation of AQP8 in rat hepatocytes. By subcellular fractionation and immunoblot analysis, we detected an N-glycosylated band of ~34 kDa corresponding to AQP8 in hepatocyte plasma and intracellular microsomal membranes. Confocal immunofluorescence microscopy for AQP8 in cultured hepatocytes showed a predominant intracellular vesicular localization. Dibutyryl cAMP (Bt2cAMP) stimulated the redistribution of AQP8 to plasma membranes. Bt2cAMP also significantly increased hepatocyte membrane water permeability, an effect that was prevented by the water channel blocker dimethyl sulfoxide. The microtubule blocker colchicine but not its inactive analog lumicolchicine inhibited the Bt2cAMP effect on both AQP8 redistribution to cell surface and hepatocyte membrane water permeability. Our data suggest that in rat hepatocytes AQP8 is localized largely in intracellular vesicles and can be redistributed to plasma membranes via a microtubule-depending, cAMP-stimulated mechanism. These studies also suggest that aquaporins contribute to water transport in cAMP-stimulated hepatocytes, a process that could be relevant to regulated hepatocyte bile secretion.

* This work was supported by Grant PICT 03589 from Agencia Nacional de Promoción Científica y Tecnológica (to R. A. M.), a grant from Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Grant DK24031 from the National Institutes of Health (to N. F. L.), and a grant from the Mayo Foundation.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Instituto de Fisiología Experimental, Facultad de Ciencias Bioquímicas y Farmacéuticas Universidad Nacional de Rosario, Suipacha 570, 2000 Rosario, Santa Fe, Argentina. Tel.: 54-341-4305799; Fax: 54-341-4399473; E-mail: rmarinel@fbioyf.unr.edu.ar.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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