| http://purl.uniprot.org/citations/25209858 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25209858 | http://www.w3.org/2000/01/rdf-schema#comment | "During maturation, the α- and γ-subunits of the epithelial Na+ channel (ENaC) undergo proteolytic processing by furin. Cleavage of the γ-subunit by furin at the consensus site γRKRR143 and subsequent cleavage by a second protease at a distal site strongly activate the channel. For example, coexpression of prostasin with ENaC increases both channel function and cleavage at the γRKRK186 site. We generated a polyclonal antibody that recognizes the region 144-186 in the γ-subunit (anti-γ43) to determine whether prostasin promotes the release of the intervening tract between the putative furin and γRKRK186 cleavage sites. Anti-γ43 precipitated both full-length (93 kDa) and furin-processed (83 kDa) γ-subunits from extracts obtained from oocytes expressing αβHA-γ-V5 channels, but only the full-length (93 kDa) γ-subunit from oocytes expressing αβHA-γ-V5 channels and either wild-type or a catalytically inactive prostasin. Although both wild-type and catalytically inactive prostasin activated ENaCs in an aprotinin-sensitive manner, only wild-type prostasin bound to aprotinin beads, suggesting that catalytically inactive prostasin facilitates the cleavage of the γ-subunit by an endogenous protease in Xenopus oocytes. As dietary salt restriction increases cleavage of the renal γ-subunit, we assessed release of the 43-mer inhibitory tract on rats fed a low-Na+ diet. We found that a low-Na+ diet increased γ-subunit cleavage detected with the anti-γ antibody and dramatically reduced the fraction precipitated with the anti-γ43 antibody. Our results suggest that the inhibitory tract dissociates from the γ-subunit in kidneys from rats on a low-Na+ diet."xsd:string |
| http://purl.uniprot.org/citations/25209858 | http://purl.org/dc/terms/identifier | "doi:10.1152/ajprenal.00157.2014"xsd:string |
| http://purl.uniprot.org/citations/25209858 | http://purl.uniprot.org/core/author | "Hughey R.P."xsd:string |
| http://purl.uniprot.org/citations/25209858 | http://purl.uniprot.org/core/author | "Frindt G."xsd:string |
| http://purl.uniprot.org/citations/25209858 | http://purl.uniprot.org/core/author | "Kleyman T.R."xsd:string |
| http://purl.uniprot.org/citations/25209858 | http://purl.uniprot.org/core/author | "Carattino M.D."xsd:string |
| http://purl.uniprot.org/citations/25209858 | http://purl.uniprot.org/core/author | "Palmer L.G."xsd:string |
| http://purl.uniprot.org/citations/25209858 | http://purl.uniprot.org/core/author | "Mueller G.M."xsd:string |
| http://purl.uniprot.org/citations/25209858 | http://purl.uniprot.org/core/author | "Rued A.C."xsd:string |
| http://purl.uniprot.org/citations/25209858 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/25209858 | http://purl.uniprot.org/core/name | "Am J Physiol Renal Physiol"xsd:string |
| http://purl.uniprot.org/citations/25209858 | http://purl.uniprot.org/core/pages | "F1080-7"xsd:string |
| http://purl.uniprot.org/citations/25209858 | http://purl.uniprot.org/core/title | "Prostasin interacts with the epithelial Na+ channel and facilitates cleavage of the gamma-subunit by a second protease."xsd:string |
| http://purl.uniprot.org/citations/25209858 | http://purl.uniprot.org/core/volume | "307"xsd:string |
| http://purl.uniprot.org/citations/25209858 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/25209858 |
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