Am J Physiol Cell Physiol Information on EB 2010
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Am J Physiol Cell Physiol 278: C1108-C1115, 2000;
0363-6143/00 $5.00
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Web of Science (31)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Yang, B.
Right arrow Articles by Verkman, A. S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yang, B.
Right arrow Articles by Verkman, A. S.
Vol. 278, Issue 6, C1108-C1115, June 2000

Skeletal muscle function and water permeability in aquaporin-4 deficient mice

Baoxue Yang1, Jean-Marc Verbavatz2, Yuanlin Song1, L. Vetrivel1, Geoffrey Manley1, Wei-Ming Kao1, Tonghui Ma1, and A. S. Verkman1

1 Departments of Medicine and Physiology, Cardiovascular Research Institute, University of California, San Francisco, California 94143-0521; and 2 Service de Biologie Cellulaire, CEA/Saclay, Gif-sur Yvette, Cedex, F-91191 France

It has been proposed that aquaporin-4 (AQP4), a water channel expressed at the plasmalemma of skeletal muscle cells, is important in normal muscle physiology and in the pathophysiology of Duchenne's muscular dystrophy. To test this hypothesis, muscle water permeability and function were compared in wild-type and AQP4 knockout mice. Immunofluorescence and freeze-fracture electron microscopy showed AQP4 protein expression in plasmalemma of fast-twitch skeletal muscle fibers of wild-type mice. Osmotic water permeability was measured in microdissected muscle fibers from the extensor digitorum longus (EDL) and fractionated membrane vesicles from EDL homogenates. With the use of spatial-filtering microscopy to measure osmotically induced volume changes in EDL fibers, half times (t1/2) for osmotic equilibration (7.5-8.5 s) were not affected by AQP4 deletion. Stopped-flow light-scattering measurements of osmotically induced volume changes in plasmalemma vesicles also showed no significant differences in water permeability. Similar water permeability, yet ~90% decreased AQP4 protein expression was found in EDL from mdx mice that lack dystrophin. Skeletal muscle function was measured by force generation in isolated EDL, treadmill performance time, and in vivo muscle swelling in response to water intoxication. No differences were found in EDL force generation after electrical stimulation [42 ± 2 (wild-type) vs. 41 ± 2 (knockout) g/s], treadmill performance time (22 vs. 26 min; 29 m/min, 13° incline), or muscle swelling (2.8 vs. 2.9% increased water content at 90 min after intraperitoneal water infusion). Together these results provide evidence against a significant role of AQP4 in skeletal muscle physiology in mice.

water channel; transgenic mice; muscular dystrophy; AQP4; orthogonal array


This article has been cited by other articles:


Home page
Hum Mol GenetHome page
M. D. Sorani, Z. Zador, E. Hurowitz, D. Yan, K. M. Giacomini, and G. T. Manley
Novel variants in human Aquaporin-4 reduce cellular water permeability
Hum. Mol. Genet., August 1, 2008; 17(15): 2379 - 2389.
[Abstract] [Full Text] [PDF]


Home page
Hum Reprod UpdateHome page
H.-F. Huang, R.-H. He, C.-C. Sun, Y. Zhang, Q.-X. Meng, and Y.-Y. Ma
Function of aquaporins in female and male reproductive systems
Hum. Reprod. Update, November 1, 2006; 12(6): 785 - 795.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Heart Circ. Physiol.Home page
T. L. Butler, C. G. Au, B. Yang, J. R. Egan, Y. M. Tan, E. C. Hardeman, K. N. North, A. S. Verkman, and D. S. Winlaw
Cardiac aquaporin expression in humans, rats, and mice
Am J Physiol Heart Circ Physiol, August 1, 2006; 291(2): H705 - H713.
[Abstract] [Full Text] [PDF]


Home page
Mol. Cell. Biol.Home page
A. C.-M. Chang, J. Cha, F. Koentgen, and R. R. Reddel
The Murine Stanniocalcin 1 Gene Is Not Essential for Growth and Development
Mol. Cell. Biol., December 1, 2005; 25(23): 10604 - 10610.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Renal Physiol.Home page
C. Silberstein, R. Bouley, Y. Huang, P. Fang, N. Pastor-Soler, D. Brown, and A. N. Van Hoek
Membrane organization and function of M1 and M23 isoforms of aquaporin-4 in epithelial cells
Am J Physiol Renal Physiol, September 1, 2004; 287(3): F501 - F511.
[Abstract] [Full Text] [PDF]


Home page
FASEB J.Home page
R. H. CROSBIE, S. A. DOVICO, J. D. FLANAGAN, J. S. CHAMBERLAIN, C. L. OWNBY, and K. P. CAMPBELL
Characterization of aquaporin-4 in muscle and muscular dystrophy
FASEB J, July 1, 2002; 16(9): 943 - 949.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Renal Physiol.Home page
Y. Huang, R. Tracy, G. E. Walsberg, A. Makkinje, P. Fang, D. Brown, and A. N. Van Hoek
Absence of aquaporin-4 water channels from kidneys of the desert rodent Dipodomys merriami merriami
Am J Physiol Renal Physiol, May 1, 2001; 280(5): F794 - F802.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Gastrointest. Liver Physiol.Home page
K. S. Wang, A. R. Komar, T. Ma, F. Filiz, J. McLeroy, K. Hoda, A. S. Verkman, and J. A. Bastidas
Gastric acid secretion in aquaporin-4 knockout mice
Am J Physiol Gastrointest Liver Physiol, August 1, 2000; 279(2): G448 - G453.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online