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The Epithelial Sodium Channel

Activation by Membrane-Bound Serine Proteases

Departments of Pharmacology and of Toxicology, University of Lausanne, Lausanne, Switzerland

Correspondence and requests for reprints should be addressed to Bernard C. Rossier, M.D., Bugnon 27, CH-1005-Lausanne, Switzerland. E-mail: Bernard.Rossier{at}ipharm.unil.ch

The epithelial sodium channel (ENaC) was cloned just 10 years ago. Since that time, the study of human monogenic diseases (pseudohypoaldosteronism type 1 [PHA-1] and Liddle syndrome), as well as mouse models mimicking salt-losing syndromes (PHA-1) or salt-sensitive hypertension (Liddle syndrome), have greatly contributed to our understanding of the function of ENaC in vivo. In this brief review, I will first discuss ENaC as a limiting factor in the control of ionic composition of the extracellular fluid and then, more specifically, the activation of ENaC by membrane-bound serine proteases. Recent in vitro and in vivo experiments indicate that membrane-bound serine proteases (channel activating proteases [CAP-1, -2, or-3]) may be of critical importance in the activation of ENaC in different organs, such as the kidney, the lung or the cochlea.

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