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 comprise kidney, colon, lung, and sweat ducts. Sodium delivery throughout those membranes is a two-step technique: 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 shipping and are regulated by way of numerous diversified hormones. The sodium channels additionally play an important function in a couple of sickness states, like high blood pressure, edema, drug-induced hyperkalemia, and cystic fibrosis. Amiloride-Sensitive Sodium Channels: body structure and practical variety presents the 1st in-depth trade of principles pertaining to those sodium channels, their legislation and involvement in general and pathophysiological occasions. Key positive aspects * Summarizes present kingdom 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 * offers principles on sodium channels and illness

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Shlyonsky, V. , and Benos, D. J. (1997). Regulation of ENaC by the amino terminus of a-rENaC. Physiologist 40, A-4 (abstr. 5). , Henry, P. , and Rotin, D. (1996). WW domains of Nedd 4 bind to the proline-rich PY motifs in the epithelial Na+ channel deleted in Liddle’s syndrome. EMBO J. 15, 2371-2380. Stutts, M. , Canessa, C . , Olsen, J. , Cohn, J. , Rossier, B. , and Boucher, R. C. (1995). CFTR as a CAMP-dependent regulator of sodium channels. Science 269,847-850. Stutts, M. , Rossier, B. , and Boucher, R.

A greater amiloride-sensitive current was observed in oocytes expressing all three subunits than in those expressing abENaC alone. 5 ng of each cRNA exhibited a fivefold increase in current following 48 h of expression. Results are 2SEM. Reprinted with permission from Fuller e l al. 1995. was expressed in oocytes. Intracellular PKA consensus sequences have been identified only in the y subunits of the rat and Xenopus isoforms; the human ENaC has no predicted PKA-sensitive sites (Garty and Palmer, 1997).

1998). , 1996). , 1993). , 1998). In abENaC, four of the proposed consensus sites for PKCdependent phosphorylation are predicted to be intracellular. , 1993; Yanase and Handler, 1986). , 1996). , 1995). This observation 8 C. M. Fuller et al. may reflect a specific difference in how abENaC is regulated when expressed by itself; however, similar experiments on the chimeric bENaC/rENaC channel needed to address this question have not yet been performed. 111. THE C TERMINUS OF abENaC: A KINETIC SWITCH?

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