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(Received for publication, April 5, 1996, and in revised form, July 12, 1996)
From the In this study, we describe the establishment of a
stably transfected epithelial cell line with the cDNA for the rat
aquaporin 2 (AQP2). To this end, we used a human cell line (HCD)
derived from the cortical collecting duct and having characteristics of
principal cells (Prié, D., Friedlander, G., Coureau, C.,
Vandewalle, A., Cassigena, R., and Ronco, P. M. (1995) Kidney
Int. 47, 1310-1318). The HCD cells were first screened for the
constitutive expression of AQPs. By Western blot analysis, we found a
low expression of immunoreactive AQP2 and AQP4 proteins. In contrast,
transfected cells (clone CD8) probed with AQP2 antiserum expressed an
intense 29-kDa protein on immunoblot in addition to a broad band
between 35-45 kDa corresponding to the glycosylated form of the
protein, indicating that full maturity of the protein is attained in
transfected cells. Immunofluorescence demonstrated that AQP2 was
located in intracellular vesicles. After vasopressin stimulation, the
staining redistributed from an intracellular site to the apical pole of
the cells, an effect similar to that described on collecting duct
principal cells in vivo (Sabolic, I., Katsura, T.,
Verbavatz, J. M., and Brown, D. (1995) J. Membr. Biol.
143, 165-175) and in perfused tubules (Nielsen, S., Chou, C. L.,
Marples, D., Christensen, E. I., Kishore, B. K., and Knepper, M. A. (1995) Proc. Natl. Acad. Sci. U. S. A. 92, 1013-1017).
The redistribution of AQP2 in CD8 cells was accompanied by an
approximately 6-fold increase in osmotic water permeability coefficient
(Pf), which was inhibited by 0.3 mM
HgCl2. These data indicate that functional
vasopressin-sensitive water channels are expressed in transfected
cells. The stably transfected cells represent a suitable model to
unravel by direct experimental approach the intracellular signals
involved in the translocation of AQP2 to the apical plasma membrane in
the presence of vasopressin.
Volume 271, Number 40,
Issue of October 4, 1996
pp. 24365-24370
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
and
Istituto di Fisiologia Generale,
Università degli Studi di Bari, Via Amendola 165/A, 70126 Bari,
Italy, ¶ Hopital Tenon, Inserm Unité 64, Paris, France, and
Research Center, Dompé S.p.a., L'Aquila, Italy
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