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Am J Physiol Cell Physiol 275: C239-C250, 1998;
0363-6143/98 $5.00
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Vol. 275, Issue 1, C239-C250, July 1998

Na+-K+-2Clminus cotransport in Ehrlich cells: regulation by protein phosphatases and kinases

Thomas Krarup, Lene D. Jakobsen, Bo S. Jensen, and Else K. Hoffmann

Department of Biochemistry, The August Krogh Institute, University of Copenhagen, DK-2100 Copenhagen, Denmark

To identify protein kinases (PK) and phosphatases (PP) involved in regulation of the Na+-K+-2Cl- cotransporter in Ehrlich cells, the effect of various PK and PP inhibitors was examined. The PP-1, PP-2A, and PP-3 inhibitor calyculin A (Cal-A) was a potent activator of Na+-K+-2Cl- cotransport (EC50 = 35 nM). Activation by Cal-A was rapid (<1 min) but transient. Inactivation is probably due to a 10% cell swelling and/or the concurrent increase in intracellular Cl- concentration. Cell shrinkage also activates the Na+-K+-2Cl- cotransport system. Combining cell shrinkage with Cal-A treatment prolonged the cotransport activation compared with stimulation with Cal-A alone, suggesting PK stimulation by cell shrinkage. Shrinkage-induced cotransport activation was pH and Ca2+/calmodulin dependent. Inhibition of myosin light chain kinase by ML-7 and ML-9 or of PKA by H-89 and KT-5720 inhibited cotransport activity induced by Cal-A and by cell shrinkage, with IC50 values similar to reported inhibition constants of the respective kinases in vitro. Cell shrinkage increased the ML-7-sensitive cotransport activity, whereas the H-89-sensitive activity was unchanged, suggesting that myosin light chain kinase is a modulator of the Na+-K+-2Cl- cotransport activity during regulatory volume increase.

dephosphorylation; phosphorylation; bumetanide; myosin light chain kinase; protein kinase A; volume regulation


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