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*Institute of Pharmacology and Toxicology, University of Lausanne, Lausanne, Switzerland; and Institute of Anatomy, University of Zurich, Zurich, Switzerland.
Correspondence to: Prof. Bernard C. Rossier, Institut de Pharmacologie et de Toxicologie, Rue du Bugnon 27, CH-1005 Lausanne, Switzerland. Phone: +4121-692-5351; Fax: +4121-692-5355; E-mail: Bernard.Rossier{at}ipharm.unil.ch
ABSTRACT. Sodium balance, extracellular fluid volume, and ultimately BP are maintained by precise regulation of the activity of the epithelial sodium channel (ENaC). Using a functional complementation assay in the Xenopus laevis oocyte expression system, a channel-activating protease (CAP-1) that increases ENaC activity two to threefold in the Xenopus oocyte expression system is here identified. External application of trypsin mimics the effect of Xenopus CAP-1 (xCAP-1) on ENaC activity, which can be blocked by aprotinin, a serine protease inhibitor, suggesting the existence of a novel extracellular pathway for controlling ENaC activity. Sequence analysis predicts that CAP-1 is a secreted and/or glycosyl-phosphatidyl-inositol (GPI)-anchored protein. The aim of the present study was to determine whether cell-surface expression of xCAP-1 is required for ENaC activation. By site-directed mutagenesis of xCAP-1, the importance of the catalytic site, N-glycosylation, and the GPI anchor of xCAP-1 on ENaC activity were analyzed. Glycosylation or catalytic activity is not required for cell-surface expression of xCAP-1, whereas the deletion of the GPI anchor consensus motif at the C-terminus of xCAP-1 (G305Stop) abolishes cell-surface expression and ENaC activation. G305Stop-mutated xCAP-1 is recovered as a secreted protein in the external medium. A catalytic mutant of xCAP-1 significantly decreased ENaC activation but did not fully abolish the effect of xCAP-1. The data indicate the critical role of the GPI anchor in ENaC activation and suggest that catalytic and noncatalytic mechanisms are involved.
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