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Summary Anatomy Item Literature (1190) Expression Attributions Wiki
XB-ANAT-721

Papers associated with distal (and prss8)

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Transmembrane serine protease 2 (TMPRSS2) proteolytically activates the epithelial sodium channel (ENaC) by cleaving the channel's γ-subunit., Sure F., J Biol Chem. June 1, 2022; 298 (6): 102004.                                        

Zymogen-locked mutant prostasin (Prss8) leads to incomplete proteolytic activation of the epithelial sodium channel (ENaC) and severely compromises triamterene tolerance in mice., Essigke D., Acta Physiol (Oxf). May 1, 2021; 232 (1): e13640.

Prostasin interacts with the epithelial Na+ channel and facilitates cleavage of the γ-subunit by a second protease., Carattino MD., Am J Physiol Renal Physiol. November 1, 2014; 307 (9): F1080-7.

Functional analysis of a missense mutation in the serine protease inhibitor SPINT2 associated with congenital sodium diarrhea., Faller N., PLoS One. January 1, 2014; 9 (4): e94267.            

Mutations of the serine protease CAP1/Prss8 lead to reduced embryonic viability, skin defects, and decreased ENaC activity., Frateschi S., Am J Pathol. August 1, 2012; 181 (2): 605-15.

TMPRSS4-dependent activation of the epithelial sodium channel requires cleavage of the γ-subunit distal to the furin cleavage site., Passero CJ., Am J Physiol Renal Physiol. January 1, 2012; 302 (1): F1-8.

Plasmin activates epithelial Na+ channels by cleaving the gamma subunit., Passero CJ., J Biol Chem. December 26, 2008; 283 (52): 36586-91.

Epithelial Na+ channels are fully activated by furin- and prostasin-dependent release of an inhibitory peptide from the gamma-subunit., Bruns JB., J Biol Chem. March 2, 2007; 282 (9): 6153-60.

A novel neutrophil elastase inhibitor prevents elastase activation and surface cleavage of the epithelial sodium channel expressed in Xenopus laevis oocytes., Harris M., J Biol Chem. January 5, 2007; 282 (1): 58-64.

Regulation of prostasin by aldosterone in the kidney., Narikiyo T., J Clin Invest. February 1, 2002; 109 (3): 401-8.

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