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J. Biol. Chem., Vol. 277, Issue 42, 40066-40074, October 18, 2002
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From the Volume-sensitive osmolyte and anion channels
(VSOACs) are activated upon cell swelling in most vertebrate cells.
Native VSOACs are believed to be a major pathway for regulatory volume
decrease (RVD) through efflux of chloride and organic osmolytes. ClC-3 has been proposed to encode native VSOACs in Xenopus
laevis oocytes and in some mammalian cells, including
cardiac and vascular smooth muscle cells. The relationship between the
ClC-3 chloride channel, the native volume-sensitive osmolyte and anion
channel (VSOAC) currents, and cell volume regulation in HeLa cells and
X. laevis oocytes was investigated using ClC-3
antisense. In situ hybridization in HeLa cells,
semiquantitative and real-time PCR, and immunoblot studies in HeLa
cells and X. laevis oocytes demonstrated the
presence of ClC-3 mRNA and protein, respectively. Exposing both
cell types to hypotonic solutions induced cell swelling and activated
native VSOACs. Transient transfection of HeLa cells with
ClC-3 antisense oligonucleotide or X. laevis oocytes
injected with antisense cRNA abolished the native ClC-3 mRNA
transcript and protein and significantly reduced the density of native
VSOACs activated by hypotonically induced cell swelling. In addition,
antisense against native ClC-3 significantly impaired the ability of
HeLa cells and X. laevis oocytes to regulate their volume.
These results suggest that ClC-3 is an important molecular component
underlying VSOACs and the RVD process in HeLa cells and X. laevis oocytes.
ClC-3 Is a Fundamental Molecular Component of Volume-sensitive
Outwardly Rectifying Cl
Channels and Volume Regulation in
HeLa Cells and Xenopus laevis Oocytes*
§,
,,, and Instituto de Ciencias Biomédicas,
Facultad de Medicina Universidad de Chile, Santiago 6530499, Chile,
the Departments of ¶ Pharmacology and
Physiology and Cell Biology, Center of
Biomedical Research Excellence, University of Nevada, School of
Medicine, Reno, Nevada 89557, and the ** Depto de Ciencias
Fisiológicas, Facultad de Ciencias Biológicas,
Pontificia Universidad Católica de Chile, Casilla 114-D,
Santiago, Chile
*
This work was supported in part by National Institutes of
Health Grant NCRR P20RR15581 and Fondecyt 3980043.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.
Some of this work was submitted by C. M. S. in partial
fulfillment toward the requirements of a doctoral degree.
§§
To whom correspondence should be addressed: Dept. of
Pharmacology/318, Center of Biomedical Research Excellence, University of Nevada School of Medicine, Reno, NV 89557-0046. Tel.: 775-784-6956; Fax: 775-784-1620; E-mail: joeh@med.unr.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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