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  • Title: Role of a Na+-dependent Cl-/HCO3- exchange in regulation of intracellular pH in fibroblasts.
    Author: L'Allemain G, Paris S, Pouysségur J.
    Journal: J Biol Chem; 1985 Apr 25; 260(8):4877-83. PubMed ID: 2985569.
    Abstract:
    We previously reported that, in a HCO3(-)-free medium, cytoplasmic pH (pHi) of hamster fibroblasts (CCL39) is primarily regulated by an amiloride-sensitive Na+/H+ antiport (L'Allemain, G., Paris, S., and Pouysségur, J. (1984) J. Biol. Chem. 259, 5809-5815). Here we demonstrate the existence of an additional pHi-regulating mechanism in CCL39 cells, namely a Na+-dependent HCO3-/Cl- exchange. Evidence for this system is based on 36Cl- influx studies and on pHi measurements in PS120, a CCL39-derived mutant lacking the Na+/H+ antiport activity. 36Cl- influx rate is a saturable function of external [Cl-] (apparent Km approximately equal to 7 mM), is competitively inhibited by external HCO3- (KI approximately equal to 3 mM), and by stilbene derivatives (KI approximately equal to 20 microM for 4-acetamido-4'-isothiocyanostilbene-2,2'-disulfonic acid). Measurements of pHi recovery after an acute acid load indicate that PS120 cells possess an acid-extruding mechanism dependent on external HCO3-, which is inhibited by stilbene derivatives and requires external Na+. Since 22Na+ influx is stimulated upon addition of HCO3- to acid-loaded cells and this effect is completely abolished by 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid, we conclude that Na+ is co-transported with HCO3-, in exchange for intracellular Cl-. In a HCO3(-)-containing medium, this pHi-regulating mechanism appears to have two essential physiological functions for the Na+/H+ antiport-deficient mutant: protection of the cells against excessive cytoplasmic acidification and establishment of a steady-state pHi permissive for growth, at neutral or slightly acidic pHo values (6.6-7.2).
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