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Originally published In Press as doi:10.1074/jbc.M008760200 on April 4, 2001
J. Biol. Chem., Vol. 276, Issue 26, 23413-23420, June 29, 2001
Salivary Acinar Cells from Aquaporin 5-deficient Mice Have
Decreased Membrane Water Permeability and Altered Cell Volume
Regulation*
Carissa M.
Krane ,
James E.
Melvin§,
Ha-Van
Nguyen§,
Linda
Richardson§,
Jennifer E.
Towne ¶,
Thomas
Doetschman , and
Anil G.
Menon
From the Department of Molecular Genetics,
Biochemistry, and Microbiology, University of Cincinnati College of
Medicine, Cincinnati, Ohio 45267-0524 and the § Center for
Oral Biology, University of Rochester School of Medicine and Dentistry,
Rochester, New York 14642
Aquaporins (AQPs) are channel proteins
that regulate the movement of water through the plasma membrane of
secretory and absorptive cells in response to osmotic gradients. In the
salivary gland, AQP5 is the major aquaporin expressed on the apical
membrane of acinar cells. Previous studies have shown that the volume
of saliva secreted by AQP5-deficient mice is decreased, indicating a
role for AQP5 in saliva secretion; however, the mechanism by which AQP5
regulates water transport in salivary acinar cells remains to be
determined. Here we show that the decreased salivary flow rate and
increased tonicity of the saliva secreted by
Aqp5 / mice in response to
pilocarpine stimulation are not caused by changes in whole body fluid
homeostasis, indicated by similar blood gas and electrolyte
concentrations in urine and blood in wild-type and AQP5-deficient mice.
In contrast, the water permeability in parotid and sublingual acinar
cells isolated from Aqp5 / mice
is decreased significantly. Water permeability decreased by 65% in
parotid and 77% in sublingual acinar cells from
Aqp5 / mice in response to
hypertonicity-induced cell shrinkage and hypotonicity-induced cell
swelling. These data show that AQP5 is the major pathway for regulating
the water permeability in acinar cells, a critical property of the
plasma membrane which determines the flow rate and ionic composition of
secreted saliva.
*
This work was supported in part by National Institutes of
Health Grants RO1 DE138283 and ES06096 (to A. G. M.), RO1
DEO8921 (to J. E. M.), NHLBI, National Institutes of Health, Program
of Excellence in Molecular Biology of Heart and Lung Grant HL61781 (to
A. G. M.) and for new investigator support from this program (to
C. M. K.).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.
¶
Supported in part by a predoctoral fellowship from the
University of Cincinnati.
To whom correspondence should be addressed: Dept. of Molecular
Genetics, Biochemistry and Microbiology, University of Cincinnati College of Medicine, 231 Bethesda Ave., 3110 MSB, P. O. Box 670524, Cincinnati, OH 45267-0524. Tel.: 513-558-5534; Fax:
513-558-1885; E-mail: Anil.Menon@UC.edu.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.

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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.
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