ArticleAmerican journal of physiology. Renal physiology2021
Cleavage state of γENaC in mouse and rat kidneys.
Article in American journal of physiology. Renal physiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 24 citations in OpenAlex.
- Hyperaldosteronism in Mice Lacking the Distal Polybasic Tract of the γ-Subunit of the Epithelial Sodium Channel During Sodium Restriction.Acta physiologica (Oxford, England) · 2026Article
- ENaC processing in rat kidney: effects of salt loading and ADH.American journal of physiology. Renal physiology · 2026Article
- Processing of ENaC in mouse kidney: effects of aldosterone and a Liddle syndrome mutation.American journal of physiology. Renal physiology · 2026Article
- Activation of the alternative complement pathway and its relevance for sodium retention in experimental nephrotic syndrome.Pflugers Archiv : European journal of physiology · 2026Article
- Acute activation of human epithelial sodium channel (ENaC) by serum and glucocorticoid inducible kinase 1 (SGK1) requires prior cleavage of the channel's γ-subunit at its proximal cleavage site.Pflugers Archiv : European journal of physiology · 2025Article
- Impact of aldosterone deficiency on the development of diuretic resistance in mice.Pflugers Archiv : European journal of physiology · 2025Article
- Epithelial Na+ Channels, Immune Cells, and Salt.Annual review of physiology · 2025Review
- ENaCγ in Urinary Extracellular Vesicles as an Indicator of MR Signaling in Primary Aldosteronism.Hypertension (Dallas, Tex. : 1979) · 2024Article
- Loss of the alpha subunit distal furin cleavage site blunts ENaC activation following NaThe Journal of physiology · 2024Article
- Control of ENaC ubiquitination.American journal of physiology. Renal physiology · 2024Article
- Influence of proteolytic cleavage of ENaC's γ subunit upon NaAmerican journal of physiology. Renal physiology · 2024Article
- Epithelial NaComprehensive Physiology · 2024Review
- Increased ENaC-mediated liquid absorption across vitamin-D deficient human airway epithelia.American journal of physiology. Cell physiology · 2024Article
- Mice lacking γENaC palmitoylation sites maintain benzamil-sensitive Na+ transport despite reduced channel activity.JCI insight · 2023Article
- Bile acids regulate the epithelial NaThe Journal of physiology · 2022Article
- Expression of ENaC subunits in epithelia.The Journal of general physiology · 2022Article
- Transmembrane serine protease 2 (TMPRSS2) proteolytically activates the epithelial sodium channel (ENaC) by cleaving the channel's γ-subunit.The Journal of biological chemistry · 2022Article
- Sodium retention in nephrotic syndrome is independent of the activation of the membrane-anchored serine protease prostasin (CAP1/PRSS8) and its enzymatic activity.Pflugers Archiv : European journal of physiology · 2022Article
- Proteolytic activation of the epithelial sodium channel (ENaC) by factor VII activating protease (FSAP) and its relevance for sodium retention in nephrotic mice.Pflugers Archiv : European journal of physiology · 2022Article
- Sex difference in kidney electrolyte transport III: Impact of low K intake on thiazide-sensitive cation excretion in male and female mice.Pflugers Archiv : European journal of physiology · 2021Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Extracellular proteases can activate the epithelial Na channel (ENaC) by cleavage of the γ subunit. Here, we investigated the cleavage state of the channel in the kidneys of mice and rats on a low-salt diet. We identified the cleaved species of channels expressed in Fisher rat thyroid cells by coexpressing the apical membrane-bound protease channel-activating protease 1 (CAP1; prostasin). To compare the peptides produced in the heterologous system with those in the mouse kidney, we treated both lysates with PNGaseF to remove N-linked glycosylation. The apparent molecular mass of the smallest COOH-terminal fragment of γENaC (52 kDa) was indistinguishable from that of the CAP1-induced species in Fisher rat thyroid cells. Similar cleaved peptides were observed in total and cell surface fractions of the rat kidney. This outcome suggests that most of the subunits at the surface have been processed by extracellular proteases. This was confirmed using nonreducing gels, in which the NH
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