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J. Biol. Chem., Vol. 266, Issue 23, 15406-15413, Aug, 1991
L Bianchini, M Woodside, C Sardet, J Pouyssegur, A Takai and S Grinstein
We determined the effect of okadaic acid (OA), a potent phosphoprotein
phosphatase inhibitor, on the intracellular pH (pHi) of rat thymic
lymphocytes and human bladder carcinoma cells. OA induced a rapid and
sustained cytosolic alkalinization. This pHi increase was Na(+)- dependent
and was inhibited by 5,N-disubstituted analogs of amiloride, indicating
mediation by the Na+/H+ antiport. As described for other stimulants, such
as mitogens and hypertonic challenge, activation of the antiport by OA is
attributable to an upward shift in its pHi dependence. Accordingly, the
alkalinization produced by the phosphatase inhibitor was not additive with
that induced osmotically. Activation of the antiport by OA was accompanied
by a marked increase in phosphoprotein accumulation, revealing the presence
of active protein kinases in otherwise unstimulated cells. We considered
the possibility that phosphorylation of the antiport itself or of an
ancillary protein is responsible for activation of Na+/H+ exchange.
Consistent with this notion, the alkalinization induced by OA was absent in
ATP depleted cells. More importantly, immunoprecipitation experiments
demonstrated increased phosphorylation of the antiport following treatment
with OA. We conclude that, upon inhibition of phosphoprotein phosphatase
activity, constitutively active kinases induce the activation of Na+/H+
exchange, possibly by direct phosphorylation of the antiport.
Okadaic acid, a phosphatase inhibitor, induces activation and phosphorylation of the Na+/H+ antiport
Division of Cell Biology, Hospital for Sick Children, Toronto, Canada.
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