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Am J Physiol Lung Cell Mol Physiol 288: L1099-L1109, 2005. First published January 28, 2005; doi:10.1152/ajplung.00332.2004
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In vitro and in vivo regulation of transepithelial lung alveolar sodium transport by serine proteases

Carole Planès,1,2 Céline Leyvraz,3 Tokujiro Uchida,4 Milena Apostolova Angelova,4 Grégoire Vuagniaux,3 Edith Hummler,3 Michael Matthay,5 Christine Clerici,1 and Bernard Rossier3

1Department of Physiology, Institut National de la Santé et de la Recherche Médicale U426, Faculté de Médecine Xavier Bichat, Université Paris 7, Paris; 2Department of Physiology, Université de Versailles-Saint Quentin, Versailles, France; 3Département de Pharmacologie et Toxicologie, Université de Lausanne, Lausanne, Switzerland; 4Department of Anesthesiology, Tokyo Medical and Dental University, Tokyo, Japan; and 5Cardiovascular Research Institute, University of California, San Francisco, California

Submitted 3 September 2004 ; accepted in final form 27 January 2005

The amiloride-sensitive epithelial sodium channel (ENaC) constitutes a rate-limiting step for sodium (Na+) and water absorption across lung alveolar epithelium. Recent reports suggested that ENaC is regulated by membrane-bound extracellular serine proteases, such as channel-activating proteases (CAPs). The objectives of this study were to examine the role of serine proteases in the regulation of transepithelial alveolar Na+ and water transport in vitro and in vivo and the expression of CAPs in rodent distal lung. In vitro experiments showed that inhibition of endogenous serine proteases by apical aprotinin 1) decreased ENaC-mediated currents in primary cultures of rat and mouse alveolar epithelial cells without affecting the abundance nor the electrophoretic migration pattern of biotinylated {alpha}- and {beta}-ENaC expressed at the cell surface and 2) suppressed the increase in amiloride-sensitive short-circuit current induced by the {beta}2-agonist terbutaline. RT-PCR experiments indicated that CAP1, CAP2, and CAP3 mRNAs were expressed in mouse alveolar epithelial cells, whereas CAP1 was also expressed in alveolar macrophages recovered by bronchoalveolar lavage. CAP1 protein was detected by Western blotting in rat and mouse alveolar epithelial cells, alveolar macrophages and bronchoalveolar lavage fluid. Finally, in vivo experiments revealed that intra-alveolar treatment with aprotinin abolished the increase in Na+-driven alveolar fluid clearance (AFC) induced by terbutaline in an in situ mouse lung model, whereas trypsin potentiated it. These results show that endogenous membrane-bound and/or secreted serine proteases such as CAPs regulate alveolar Na+ and fluid transport in vitro and in vivo in rodent lung.

channel-activating protease; epithelial sodium channel; {beta}-adrenergic agonist; trypsin; lung fluid balance


Address for reprint requests and other correspondence: C. Planès, INSERM U426, 16, rue Henri Huchard - BP 416, 75870 Paris Cedex 18, France (E-mail: carole.planes{at}apr.ap-hop-paris.fr)




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