Cleavage state of γENaC in mouse and rat kidneys
Gustavo Frindt, Shujie Shi, Thomas R. Kleyman, Lawrence G. Palmer
Abstract
We have identified the major aldosterone-dependent cleaved form of the epithelial Na channel (ENaC) γ subunit in the kidney as a twice-cleaved peptide. This form appears to be identical in size with a subunit cleaved in vitro by the extracellular protease channel-activating protease 1 (prostasin). In the absence of reducing agents, it has an overall molecular mass less than that of the intact subunit, consistent with the excision of an inhibitory domain.
Topics & Concepts
Epithelial sodium channelCleavage (geology)ProteasesProtein subunitFurinProteaseMolecular massBiochemistryExtracellularChemistryGlycosylationPseudohypoaldosteronismKidneyBiologyMolecular biologyEnzymeEndocrinologySodiumGenePaleontologyFracture (geology)Organic chemistryIon Transport and Channel RegulationElectrolyte and hormonal disordersIon channel regulation and function