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

By Dale J. Benos (Eds.)

Sodium reabsorbing epithelia play a tremendous 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 procedure: 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 various hormones. The sodium channels additionally play an important function in a few sickness states, like high blood pressure, edema, drug-induced hyperkalemia, and cystic fibrosis. Amiloride-Sensitive Sodium Channels: body structure and sensible range offers the 1st in-depth alternate of rules touching on those sodium channels, their legislation and involvement in basic and pathophysiological events. Key gains * Summarizes present country of amiloride-sensitive sodium channel box * Analyzes structure-function of epithelial sodium channels * Discusses immunolocalization of epithelial sodium channels * Examines hormonal rules of sodium channels * Discusses sodium channels in lymphocytes, kidney, and lung * Considers mechanosensitivity of sodium channels * presents rules on sodium channels and illness

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Rogers, J. , and Welsh, M. J. (1998). Electrophysiological and biochemical evidence that DEG/ENaC cation channels are composed of nine subunits. J. Biol. Chem. 273, 681-684. Sorscher, E. , Accavitti, M. , Frizzell, R. , and Benos, D. J. (1988). Antibodies against purified epithelial sodium channel protein from bovine renal papilla. Am. J. Physiol. 255, C835-C843. Stanton, B. , Chalfant, M. , Ismailov, I. , Berdiev, B. , Fuller, C. , Shlyonsky, V. , and Benos, D. J. (1997). Regulation of ENaC by the amino terminus of a-rENaC.

IV. STOICHIOMETRY OF hENaC A. Electrophysiologid Analysis The finding that coexpression of a,p, and yENaC 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 (Tavernarakis and Driscoll, 1997). , 1998). , 1997) previously found that a residue within the second transmembrane lines the channel pore. Wild-type hENaC is segment of yhENaC insensitive to the cysteine-reactive compound MTSET (Fig.

1986b). Epithelial sodium channels: Characterization by using the patch-clamp technique. Fed. , Fed. Am. Exp. Biol. 45,2708-2712. Perez, G . , Adelman, J. , and Toro, L. (1994). Reconstitution of expressed Kc, channels from Xenopus oocytes to lipid bilayers. Biophys. J. 66, 1022-1027. , and Papazian, D. M. (1994). S4 mutations alter gating currents of Shaker K channels. Biophys. J. 66, 345-354. Prat, A. , Bertorello, A. , Ausiello, D. , and Cantiello, H. F. (1993). Activation of epithelial Na' channels by protein kinase A requires actin filaments.

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