Cloning and expression of a chloride-dependent Na+-H+ exchanger.

Electroneutral Na(+)-H(+) exchange is present in virtually all cells, mediating the exchange of extracellular Na(+) for intracellular H(+) and, thus, plays an important role in the regulation of intracellular pH, cell volume, and transepithelial Na(+) absorption. Recent transport studies demonstrated the presence of a novel chloride-dependent Na(+)-H(+) exchange in the apical membrane of crypt cells of rat distal colon. We describe the cloning of a 2.

Regulation of DRA and AE1 in rat colon by dietary Na depletion.

Two distinct Cl/anion exchange activities (Cl/HCO(3) and Cl/OH) identified in apical membranes of rat distal colon are distributed in cell type-specific patterns. Cl/HCO(3) exchange is expressed only in surface cells, whereas Cl/OH exchange is localized in surface and crypt cells. Dietary Na depletion substantially inhibits Cl/HCO(3) but not Cl/OH exchange.

Basolateral K-Cl cotransporter regulates colonic potassium absorption in potassium depletion.

Active potassium absorption in the rat distal colon is electroneutral, Na(+)-independent, partially chloride-dependent, and energized by an apical membrane H,K-ATPase. Both dietary sodium and dietary potassium depletion substantially increase active potassium absorption. We have recently reported that sodium depletion up-regulates H,K-ATPase alpha-subunit mRNA and protein expression, whereas potassium depletion up-regulates H,K-ATPase beta-subunit mRNA and protein expression.

Ouabain-sensitive H,K-ATPase functions as Na,K-ATPase in apical membranes of rat distal colon.

Na,K-ATPase activity has been identified in the apical membrane of rat distal colon, whereas ouabain-sensitive and ouabain-insensitive H,K-ATPase activities are localized solely to apical membranes. This study was designed to determine whether apical membrane Na,K-ATPase represented contamination of basolateral membranes or an alternate mode of H,K-ATPase expression. An antibody directed against the H, K-ATPase alpha subunit (HKcalpha) inhibited apical Na,K-ATPase activity by 92% but did not alter basolateral membrane Na,K-ATPase activity.

Colonic H-K-ATPase alpha- and beta-subunits express ouabain-insensitive H-K-ATPase.

Active K absorption in the rat distal colon is energized by an apical H-K-ATPase, a member of the gene family of P-type ATPases. The H-K-ATPase alpha-subunit (HKcalpha) has been cloned and characterized (together with the beta-subunit of either Na-K-ATPase or gastric H-K-ATPase) in Xenopus oocytes as ouabain-sensitive (86)Rb uptake. In contrast, HKcalpha, when expressed in Sf9 cells without a beta-subunit, yielded evidence of ouabain-insensitive H-K-ATPase.