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Originally published In Press as doi:10.1074/jbc.M100322200 on February 9, 2001

J. Biol. Chem., Vol. 276, Issue 22, 18657-18664, June 1, 2001
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Tumor Necrosis Factor-alpha Inhibits Aquaporin 5 Expression in Mouse Lung Epithelial Cells*

Jennifer E. TowneDagger §, Carissa M. KraneDagger , Cindy J. Bachurski, and Anil G. MenonDagger ||

From the Dagger  Department of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati College of Medicine, Cincinnati, Ohio 45267-0524 and the  Division of Pulmonary Biology, Children's Hospital Medical Center, Cincinnati, Ohio 45229

Aquaporin 5 (AQP5), the major water channel expressed in alveolar, tracheal, and upper bronchial epithelium, is significantly down-regulated during pulmonary inflammation and edema. The mechanisms that underlie this decrease in AQP5 levels are therefore of considerable interest. Here we show that AQP5 expression in cultured lung epithelial cells is decreased 2-fold at the mRNA level and 10-fold at the protein level by the proinflammatory cytokine tumor necrosis factor alpha  (TNF-alpha ). Treatment of murine lung epithelial cells (MLE-12) with TNF-alpha results in a concentration- and time-dependent decrease in AQP5 mRNA and protein expression. Activation of the p55 TNF-alpha receptor (TNFR1) with an agonist antibody is sufficient to cause decreased AQP5 expression, demonstrating that the TNF-alpha effect is mediated through TNFR1. Inhibition of nuclear factor kappa B (NF-kappa B) translocation to the nucleus blocks the effect of TNF-alpha on AQP5 expression, indicating that activation of NF-kappa B is required, whereas inhibition of extracellular signal-regulated or p38 mitogen-activated protein kinases showed no effect. These data show that TNF-alpha decreases AQP5 mRNA and protein expression and that the molecular pathway for this effect involves TNFR1 and activated NF-kappa B. The ability of inflammatory cytokines to decrease aquaporin expression may help explain the connection between inflammation and edema.

* This work was supported in part by Grants RO1 DE138283 (to A. G. M.) and RO1 HL60907 from the National Institutes of Health (to C. J. B.), Grant HL61781 from the NHLBI Program of Excellence in Molecular Biology of Heart and Lung, National Institutes of Health (to A. G. M.), and a new investigator grant from this program (to C. M. K.), and by the Caroline Halfter-Spahn Trust.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 and an Albert J. Ryan Foundation fellowship.

|| To whom correspondence should be addressed: Dept. of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati College of Medicine, 231 Albert Sabin Way, 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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