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Cloning, chromosomal localization, and physical linkage of the β and γ subunits (SCNN1B and SCNN1G) of the human epithelia amiloride-sensitive sodium channel
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14. Duc C, Farman N, Canessa CM, Bonvalet JP, Rossier BC: Cell specific expression of epithelial sodium channel alpha, beta and gamma subunits in aldosterone-responsive epithelia from the rat: localization by in situ hybridization and immunocytochemistry. J Cell Biol 1994, 127:1907-1921.
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Renard, S.1
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0029874436
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Functional degenerin-containing chimeras identify residues essential for amiloride-sensitive Na channel function
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18. Waldmann R, Champigny G, Lazdunski M: Functional degenerin-containing chimeras identify residues essential for amiloride-sensitive Na channel function. J Biol Chem 1995, 270:11735-11737. Describes the first and only published attempt to identify the residues that contribute to the pore-forming region of ENaC and related channels. The finding that the channel is expressed when the second hydrophobic domain of ENaC is replaced by the equivalent domain of Mec-4 supports the interpretation that Mec-4 is a channel subunit; this study is complementary to the earlier report [30] that the second hydrophobic domain of αENaC can substitute functionally for that of Mec-4 in C. elegans.
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Liddle's syndrome: A heritable human hypertension caused by mutations in the β subunit of the epithelial sodium channel
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19. Shimkets RA, Warnock DG, Bositis CM, Nelson-Williams C, Hansson JH, Schambelan M, Gill JR, Ulick S, Milora RV, Findling JW et al.: Liddle's syndrome: a heritable human hypertension caused by mutations in the β subunit of the epithelial sodium channel. Cell 1994, 79:407-414.
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Shimkets, R.A.1
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20. Hansson JH, Neslon-Williams C, Suzuki H, Schild L, Shimkets R, Lu Y, Canessa CM, Iwasaki T, Rossier BC, Lifton RP: Hypertension caused by a truncated epithelial sodium channel γ subunit: genetic heterogeneity of Liddle syndrome. Nat Genet 1995, 11:76-82. This paper, together with [19], identifies several families in which carboxy-terminal truncations of the β or γ subunits of ENaC lead to a gain-of-function phenotype; the excessive sodium reabsorption in the kidney results in hypertension.
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0029591506
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+ channel
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+ channel. Cell 1995, 83:969-978. This paper, together with [22•,23•], shows that the gain-of-channel phenotype that occurs as a result of the truncations of channel subunits in Liddle's disease results from an increased expression of channels in the cell membrane, with little change in unitary conductance, selectivity or pharmacological properties. The same increase in expression could be produced by single point mutations in the PPPXY (single-letter code for amino acids) motif in the carboxyl terminus of α, β or γ ENaC, suggesting that loss of regulation by a neural precursor cell expressed developmentally downregulated 4 (NEDD4)-like protein (which can bind to wild-type ENaCs) is responsible (see [17•]).
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23. Schild L, Lu Y, Gautschi I, Schneeberger E, Liftoin RP, Rossier BC: Identification of a PY motif in the epithelial Na channel as a target sequence for mutations causing channel activation found in Liddle syndrome. EMBO J 1996, 15:2381-2387. See annotation [21•].
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Gu, G.1
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Hong, K.1
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31. Green KA, Falconer SW, Cottrell GA: The neuropeptide Phe-Met-Arg-Phe-NH2 (FMRFamide) directly gates two ion channels in an identified Helix neurone. Pflugers Arch 1994, 428:232-240.
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