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

By Dale J. Benos (Eds.)

Sodium reabsorbing epithelia play a massive position 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 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 shipping and are regulated through numerous diverse hormones. The sodium channels additionally play an important position in a couple of 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 principles touching on those sodium channels, their legislation and involvement in common and pathophysiological events. Key good points * 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 ailment

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Additional info for Amiloride-Sensitive Sodium Channels: Physiology and Functional Diversity

Sample text

PhENaC that coprecipitated with ahENaC was also quantitated (at 0 h, insufficient p was present for quantitation). Reproduced from Snyder et al. (1998). V.

Channels predicted to be sensitive and insensitive to MTSET are indicated. Adapted from Snyder er al. (1998). inhibited by MTSET should be 7/8 that of the completely mutant channel. This is in close agreement with our results. To confirm the number of y subunits, we used a second mutation which had the opposite effect. In contrast to MTSET, a smaller cysteine-reactive compound (MTSEA) inhibits wild-type hENaC 54% by modifying one or more cysteine within the channel pore (P. M. Snyder, and M. J.

5). If channels containing at least one mutant y are sensitive to MTSET, then the fraction of current 31 2. cec.. 0 0 FIGURE 4 Stoichiometry of yhENaC using y ~ 5 3Wild-type ~ ~ . yG536C,or a mixture, as indicated. (A) Representative time course of current. Amiloride (3 mM) and MTSET (3 mM) added as indicated (bars). yG536C1or combinations of both in the indicated ratios. 5) of each. Channels predicted to be sensitive and insensitive to MTSET are indicated. Adapted from Snyder er al. (1998). inhibited by MTSET should be 7/8 that of the completely mutant channel.

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