The epithelial sodium channel and the control of sodium balance
نویسندگان
چکیده
منابع مشابه
Renal sodium handling: the role of the epithelial sodium channel.
T he epithelial sodium channel (ENaC) is a critically important final regulator of the balance between intake and excretion of dietary sodium (1), and along with the thiazide-sensitive NaCl co-transporter constitutes the predominant sodium transport systems in the aldosterone-sensitive distal nephron (2). The use of the oocyte expression system for cloning the ENaC subunits was a technical tour...
متن کاملFunctional domains of the epithelial sodium channel.
T he epithelial sodium channel (ENaC) plays an important role in ion transport of many organ systems. In kidney, colon, and sweat gland, ENaC-mediated transepithelial sodium transport helps to adjust sodium excretion in the urine, feces, and sweat to fulfill homeostatic requirements. In lung and airways, ENaC activity is important for alveolar liquid clearance and regulation of mucous fluidity....
متن کاملAmmonium interaction with the epithelial sodium channel.
The purpose of this study was to investigate the direct effect of NH(3)/NH on mouse epithelial Na(+) channels (mENaC) expressed in Xenopus oocytes. Two-electrode voltage-clamp and ion-selective microelectrodes were used to measure the Na(+) current, intracellular pH (pH(i)), and ion activities in oocytes expressing mENaC. In oocytes expressing mENaC, removal of external Na(+) reversibly hyperpo...
متن کاملExtracellular chloride regulates the epithelial sodium channel.
The extracellular domain of the epithelial sodium channel ENaC is exposed to a wide range of Cl(-) concentrations in the kidney and in other epithelia. We tested whether Cl(-) alters ENaC activity. In Xenopus oocytes expressing human ENaC, replacement of Cl(-) with SO4(2-), H2PO4(-), or SCN(-) produced a large increase in ENaC current, indicating that extracellular Cl(-) inhibits ENaC. Extracel...
متن کاملNedd4-2 isoforms ubiquitinate individual epithelial sodium channel subunits and reduce surface expression and function of the epithelial sodium channel.
We previously reported the existence of multiple isoforms of human Nedd4-2 (Am J Physiol Renal Physiol 285: F916-F929, 2003). When overexpressed in M-1 collecting duct epithelia, full-length Nedd4-2 (Nedd4-2), Nedd4-2 lacking the NH(2)-terminal C2 domain (Nedd4-2DeltaC2), and Nedd4-2 lacking WW domains 2 and 3 (Nedd4-2DeltaWW2,3) variably reduce benzamil-sensitive Na(+) transport. We investigat...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
سال: 2010
ISSN: 0925-4439
DOI: 10.1016/j.bbadis.2010.06.014