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J Biol Chem, Vol. 275, Issue 10, 6777-6782, March 10, 2000
From the Department of Physiology and Biophysics, University of
California, Irvine, California 92697-4560
Aquaporins increase the water permeability in
many cell types across many species. We investigated the effects of
external pH and Ca2+ on water permeability of
Xenopus oocytes injected with aquaporin cRNA by measuring
the rate of swelling in hypotonic solutions. Lowering pH to 6.5 increased the water permeability of aquaporin (AQP0) 3.4 ± 0.4-fold. Diethylpyrocarbonate pretreatment increased water
permeability 4.2 ± 0.5-fold and abolished pH sensitivity, suggesting that the pH regulation is mediated by an external histidine. Lowering Ca2+ increased water permeability 4.1 ± 0.4-fold. The effects of Ca2+ and pH each required the
presence of histidine 40, indicating a critical role of this amino acid
in facilitating the modulation of water permeability. Clamping
intracellular Ca2+ at high or low values abolished
sensitivity to external Ca2+, suggesting that
Ca2+ acts at an internal site. Three different calmodulin
inhibitors each increased AQP0 water permeability, suggesting that
Ca2+ may act through calmodulin. None of the above altered
the water permeability induced by AQP1 or AQP4. Because the greatest
change in AQP0 water permeability is in the normal pH range found in the lens (7.2-6.5), this paper provides evidence for regulation of an
aquaporin by pH under physiological conditions.
pH and Calcium Regulate the Water Permeability of Aquaporin
0*
*
This work was supported by Grant EY5661 from the National
Institutes of Health.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: Dept. of Physiology
and Biophysics, University of California Irvine, Irvine, CA 92697. Tel.: 949-824-7780; Fax: 949-824-3143; E-mail: jhall@uci.edu.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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