| http://purl.uniprot.org/citations/15084585 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15084585 | http://www.w3.org/2000/01/rdf-schema#comment | "The delta-subunit of epithelial Na(+) channels (ENaC) is predominately expressed in brain, heart, and pancreas. The amiloride sensitivity, Na(+) conductance, and critical domains for gating are characterized as a cross between proton-activated Na(+) channels and alpha-ENaC. The hypothesis that external protons may activate human delta-ENaC was addressed by expressing deltabetagamma-hENaC in Xenopus oocytes and evaluating proton-activated current with the two-electrode voltage clamp technique. Our results showed that protons transiently evoked a Na(+) current with an EC(50) of pH 6 overlapped on the basal current of deltabetagamma-hENaC. Proton-activated current was not observed in uninjected oocytes. Studies on gating kinetics revealed that activation, desensitization, and recovery times of proton-activated Na(+) current were 3.8 +/- 0.5 s, 253 +/-9.5 s, and 10 +/-3.6 s, respectively (n = 4-12). Alkali metal cation selectivity of the proton-activated current was identical to that of the basal current of deltabetagamma-hENaC. The metabolic acids, lactate, pyruvate, and formate, modified the proton-activated current, as did hypo-osmotic stress. EDTA, hypo-osmolarity, and lactate enhanced proton activation synergistically. Our results suggest that delta-hENaC subunit is essential for proton-activated current and gamma-subunit may potentially regulate the response of delta-hENaC to protons. We have concluded that deltabetagamma-hENaC is a proton-activated cation channel whose closing gate can be regulated by a proton-induced conformational change. Proton-sensitivity of deltabetagamma-hENaC may be an important mechanism for integrating external ischemic signals in inflamed and hypoxic tissues."xsd:string |
| http://purl.uniprot.org/citations/15084585 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m401143200"xsd:string |
| http://purl.uniprot.org/citations/15084585 | http://purl.uniprot.org/core/author | "Benos D.J."xsd:string |
| http://purl.uniprot.org/citations/15084585 | http://purl.uniprot.org/core/author | "Ji H.L."xsd:string |
| http://purl.uniprot.org/citations/15084585 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15084585 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/15084585 | http://purl.uniprot.org/core/pages | "26939-26947"xsd:string |
| http://purl.uniprot.org/citations/15084585 | http://purl.uniprot.org/core/title | "Degenerin sites mediate proton activation of deltabetagamma-epithelial sodium channel."xsd:string |
| http://purl.uniprot.org/citations/15084585 | http://purl.uniprot.org/core/volume | "279"xsd:string |
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