Amiloride-Sensitive Sodium Channels: Physiology and by Dale J. Benos (Eds.)

By Dale J. Benos (Eds.)

Sodium reabsorbing epithelia play an important function in whole-body sodium homeostasis. a few examples of sodium regulating tissues contain kidney, colon, lung, and sweat ducts. Sodium shipping throughout those membranes is a two-step approach: access via an amiloride-sensitive sodium channel and go out through the ouabain-sensitive sodium/potassium ATPase. The sodium access channels are the rate-limiting determinant for delivery and are regulated by means of a number of assorted hormones. The sodium channels additionally play an important function in a few disorder states, like high blood pressure, edema, drug-induced hyperkalemia, and cystic fibrosis. Amiloride-Sensitive Sodium Channels: body structure and useful range offers the 1st in-depth alternate of rules referring to those sodium channels, their law and involvement in common and pathophysiological occasions. Key beneficial properties * Summarizes present nation of amiloride-sensitive sodium channel box * Analyzes structure-function of epithelial sodium channels * Discusses immunolocalization of epithelial sodium channels * Examines hormonal law of sodium channels * Discusses sodium channels in lymphocytes, kidney, and lung * Considers mechanosensitivity of sodium channels * offers principles on sodium channels and ailment

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And Handler, J. S . (1986). Activators of protein kinase C inhibit sodium transport in A6 epithelia. Am. J. Physiol. 250, C517-C522. Zagotta, W. , and Aldrich, R. W. (1990). Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB. Science 250, 568-571. CHAPTER 2 Membrane Topology,Subunit Composition, and Stoichiometry of the Epithelial NaS Channel Peter M. Snyder,” Chun Cheng,? and Michael J. Welsh? Departments of Internal Medicine and Physiology and Biophysics, Howard Hughes Medical Institute, University of Iowa College of Medicine, Iowa City, Iowa 52242 I.

That each of the six was glycosylated (Fig. 1A), suggesting that they all lie within an extracellular domain. To localize the C-terminus with respect to the plasma membrane, we placed a Flag epitope at the C-terminus (Fc-term). Following in vitro translation and incorporation of the tagged arENaC into microsomal membranes, we determined the sensitivity of the epitope to proteinase K. The C-terminal epitope was not protected from protease digestion (Fig. 2A), indicating that it was oriented on the outside of the microsome, and hence, is located on the intracellular side of the plasma membrane.

Wild-type and mutant hENaC subunits were coexpressed (along with the other two wild-type subunits) in the indicated ratios, and the fraction of Na’ current inhibited by MTSEA (1 mM) is plotted. Adapted from Snyder et al. (1998). within a channel complex was sufficient to abolish sensitivity to MTSEA. Further, wild-type and mutant y subunits (when coexpressed with a and PhENaC) produced equal Na+ currents, suggesting that the channel composition fits a binomial distribution. Using the same equation shown above, the data for yS52gc suggested that hENaC contains three y subunits.

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