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

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.

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 Creators:
Ehret, Elodie, Author
Stroh, Sevan, Author
Auberson, Muriel, Author
Ino, Frederique, Author
Jager, Yannick1, Author           
Maillard, Marc, Author
Szabo, Roman, Author
Bugge, Thomas H., Author
Frateschi, Simona, Author
Hummler, Edith, Author
Affiliations:
1Pharmacology, Max Planck Institute for Heart and Lung Research, Max Planck Society, ou_2591696              

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 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.

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 Dates: 2023-09-23
 Publication Status: Published online
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 Rev. Type: -
 Identifiers: ISI: 001084852500001
DOI: 10.3390/cells12192342
PMID: 37830556
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Title: CELLS
Source Genre: Journal
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Pages: - Volume / Issue: 12 (19) Sequence Number: 2342 Start / End Page: - Identifier: -