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- W161002956 abstract "Recent studies have shown that the epithelial sodium channel (ENaC) is down-regulated via its ubiquitination induced by Nedd4-2 and is upregulated via its deubiquitination induced by Ubiquitin Carboxyl-Terminal Hydrolase (UCH) L3. In the present study, we used patch-clamp techniques combined with both confocal microscopy and Western blot methods to further determine how ENaC in A6 distal nephron cells is regulated by UCH-L3. Patch-clamp data showed that decreasing the activity of UCH-L3 with a UCH-L3 inhibitor significantly reduced the number of active ENaC in the patch. The data from Western blot experiments showed that treatment of A6 cells with the UCH-L3 inhibitor remarkably reduced the protein levels of α-, β-, and γ-ENaC subunits. Consistent with these data, confocal microscopy experiments showed that the UCH-L3 inhibitor also reduced the density of α- and γ-ENaC at the apical membrane. These results suggest that UCH-L3 upregulates ENaC by maintaining its density at the apical membrane." @default.
- W161002956 created "2016-06-24" @default.
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- W161002956 date "2010-04-01" @default.
- W161002956 modified "2023-10-18" @default.
- W161002956 title "UCH‐L3 upregulates the epithelial sodium channel in A6 distal nephron cells" @default.
- W161002956 doi "https://doi.org/10.1096/fasebj.24.1_supplement.606.29" @default.
- W161002956 hasPublicationYear "2010" @default.
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