Kidney-Specific Membrane-Bound Serine Proteases CAP1/Prss8 and CAP3/St14 Affect 
ENaC Subunit Abundances but Not Its Activity

Ehret, Elodie; Stroh, Sevan; Auberson, Muriel; Ino, Frederique; Jager, Yannick; Maillard, Marc; Szabo, Roman; Bugge, Thomas H.; Frateschi, Simona; Hummler, Edith

doi:10.3390/cells12192342

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Kidney-Specific Membrane-Bound Serine Proteases CAP1/Prss8 and CAP3/St14 Affect ENaC Subunit Abundances but Not Its Activity

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Jager, Yannick
Pharmacology, Max Planck Institute for Heart and Lung Research, Max Planck Society;

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Citation

Ehret, E., Stroh, S., Auberson, M., Ino, F., Jager, Y., Maillard, M., et al. (2023). Kidney-Specific Membrane-Bound Serine Proteases CAP1/Prss8 and CAP3/St14 Affect ENaC Subunit Abundances but Not Its Activity. CELLS, 12(19): 2342. doi:10.3390/cells12192342.

Cite as: https://hdl.handle.net/21.11116/0000-000D-E7A8-1

Abstract

The serine proteases CAP1/Prss8 and CAP3/St14 are identified as ENaC channel-activating proteases in vitro, highly suggesting that they are required for proteolytic activation of ENaC in vivo. The present study tested whether CAP3/St14 is relevant for renal proteolytic ENaC activation and affects ENaC-mediated Na+ absorption following Na+ deprivation conditions. CAP3/St14 knockout mice exhibit a significant decrease in CAP1/Prss8 protein expression with altered ENaC subunit and decreased pNCC protein abundances but overall maintain sodium balance. RNAscope-based analyses reveal co-expression of CAP3/St14 and CAP1/Prss8 with alpha ENaC in distal tubules of the cortex from wild-type mice. Double CAP1/Prss8; CAP3/St14-deficiency maintained Na+ and K+ balance on a Na+-deprived diet, restored ENaC subunit protein abundances but showed reduced NCC activity under Na+ deprivation. Overall, our data clearly show that CAP3/St14 is not required for direct proteolytic activation of ENaC but for its protein abundance. Our study reveals a complex regulation of ENaC by these serine proteases on the expression level rather than on its proteolytic activation.