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Figure 1 | International Archives of Medicine

Figure 1

From: Regulation of the epithelial sodium channel [ENaC] in kidneys of salt-sensitive Dahl rats: Insights on alternative splicing

Figure 1

Structure of the Epithelial Sodium Channel [ENaC]. The amiloride-sensitive epithelial sodium channel [ENaC] is composed of three homologous α, β and γ protein subunits of corresponding 698, 638 and 650 amino acids in length [14, 15]. ENaC α, β and γ subunits share approximately 30% homology at the amino acid level and each subunit correspond to a molecular mass of 70-80 kDa. The three ENaC subunits are inserted into the plasma membrane with a proposed stoichiometry of 2:1:1 [16] as shown in the above figure or 3:3:3 [18]. Each ENaC protein subunit is formed up of four major domains: the cytoplasmic N terminus, the large extracellular loop, the two short hydrophobic segments known as the transmembrane domains 1 and 2 [TM1 and 2] and the cytoplasmic C-terminus. The N- and C-termini face the cytosolic side, while the extracellular loop faces the extracellular side [19]. All three subunits cooperate to form the channel pore via the transmembrane domains.

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