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. Author manuscript; available in PMC: 2011 Jan 1.
Published in final edited form as: Curr Opin Nephrol Hypertens. 2010 Jan;19(1):13–19. doi: 10.1097/MNH.0b013e3283330fb2

Figure 1. ENaC is activated by proteolytic cleavage and release of inhibitory peptides.

Figure 1

(A) Non-cleaved trimers of αβγENaC likely represent near-silent channels found on the cell surface with Po<0.1 (46-49). (B) αβγENaC is normally cleaved by furin as it transits the biosynthetic pathway and exhibits an intermediate Po (50). Furin cleaves α twice to release a 26-mer inhibitory peptide (*) and γ is cleaved once (51, 52). (C) Subsequent cleavage of the γ subunit at a site distal to the furin cleavage site, releases a second inhibitory peptide (**) and increases the Po to near 1 (46, 50, 53). Several proteases cleave γ at this distal site (20, 40, 50). For review, see (1, 5).