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Am J Physiol Cell Physiol 281: C133-C141, 2001;
0363-6143/01 $5.00
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Vol. 281, Issue 1, C133-C141, July 2001

Modulation of Na+/H+ exchange activity by Clminus

Orit Aharonovitz1, András Kapus2, Katalin Szászi1, Natasha Coady-Osberg1, Tim Jancelewicz2, John Orlowski3, and Sergio Grinstein1

1 Cell Biology Program, Hospital for Sick Children, Toronto M5G 1X8, and 2 Department of Surgery, Toronto Hospital and University of Toronto, Toronto, Ontario M5G 1L7; and 3 Department of Physiology, McGill University, Montreal, Quebec, Canada H3G 1Y6

Na+/H+ exchanger (NHE) activity is exquisitely dependent on the intra- and extracellular concentrations of Na+ and H+. In addition, Cl- ions have been suggested to modulate NHE activity, but little is known about the underlying mechanism, and the Cl- sensitivity of the individual isoforms has not been established. To explore their Cl- sensitivity, types 1, 2, and 3 Na+/H+ exchangers (NHE1, NHE2, and NHE3) were heterologously expressed in antiport-deficient cells. Bilateral replacement of Cl- with nitrate or thiocyanate inhibited the activity of all isoforms. Cl- depletion did not affect cell volume or the cellular ATP content, which could have indirectly altered NHE activity. The number of plasmalemmal exchangers was unaffected by Cl- removal, implying that inhibition was due to a decrease in the intrinsic activity of individual exchangers. Analysis of truncated mutants of NHE1 revealed that the anion sensitivity resides, at least in part, in the COOH-terminal domain of the exchanger. Moreover, readdition of Cl- into the extracellular medium failed to restore normal transport, suggesting that intracellular Cl- is critical for activity. Thus interaction of intracellular Cl- with the COOH terminus of NHE1 or with an associated protein is essential for optimal activity.

antiport; type 1 Na+/H+ exchanger; anion dependence; osmotic activation; volume regulation


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