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• W1787932272 abstract "Publisher Summary The chapter presents a review of the membrane topology, subunit composition, and stoichiometry of epithelial Na + channel (ENaC). To begin to define the structure of ENaC, the chapter mentions the membrane topology of the rat a subunit (αrENaC). In vitro translation of αrENaC produced a 73-kDa protein, and an additional 93-kDa protein was produced when αrENaC was translated in the presence of microsomal membranes, corresponding to the core-glycosylated form of the protein. Three ENaC subunits have been identified in epithelia of rat and human: α, β, and γ ENaC. It is found that expression of the human, a subunit alone in Xenopus oocytes, produced amiloride-sensitive Na + current. The finding that coexpression of α , β , and γ ENaC is required for maximal Na + current suggests that ENaC is a heteromultimeric channel. Genetic evidence from C. elegans suggests that the degenerins also function as heteromultimers. A biochemical assay is used to determine whether the mass of hENaC was consistent with a complex containing nine subunits. Because α hENaC can form a functional channel by itself, the mass of in vitro is determined, expressed α by sucrose gradient sedimentation." @default.
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• W1787932272 date "1999-01-01" @default.
• W1787932272 modified "2023-09-27" @default.
• W1787932272 title "Chapter 2 Membrane Topology, Subunit Composition, and Stoichiometry of the Epithelial Na+Channel" @default.
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• W1787932272 doi "https://doi.org/10.1016/s0070-2161(08)60950-8" @default.
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