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Am J Physiol Heart Circ Physiol 275: H641-H652, 1998;
0363-6135/98 $5.00
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Vol. 275, Issue 2, H641-H652, August 1998

alpha 1-Adrenergic activation of myocardial Na-K-2Cl cotransport involving mitogen-activated protein kinase

Geir Øystein Andersen, Mette Enger, G. Hege Thoresen, Tor Skomedal, and Jan-Bjørn Osnes

Department of Pharmacology, University of Oslo, N-0316 Oslo; and Merck, Sharpe, and Dohme Cardiovascular Research Center, Rikshospitalet, N-0027 Oslo, Norway

The translocation mechanisms involved in the alpha 1-adrenoceptor-stimulated efflux of the potassium analog 86Rb+ were studied in isolated rat hearts. Phenylephrine (in the presence of a beta -blocker) increased the efflux of 86Rb+ and 42K+, and the Na-K-2Cl (or K-Cl) cotransport inhibitor bumetanide reduced the response by 42 ± 11%. Furosemide inhibited the response with a lower potency than that of bumetanide. The bumetanide-insensitive efflux was largely sensitive to the K+ channel inhibitor 4-aminopyridine. Inhibitors of the Na+/H+ exchanger or the Na+-K+ pump had no effect on the increased 86Rb+ efflux. The activation of the Na-K-2Cl cotransporter was dependent on the extracellular signal-regulated kinase (ERK) subgroup of the mitogen-activated protein (MAP) kinase family. Phenylephrine stimulation increased ERK activity 3.4-fold. PD-98059, an inhibitor of the ERK cascade, reduced both the increased 86Rb+ efflux and ERK activity. Specific inhibitors of protein kinase C and Ca2+/calmodulin-dependent kinase II had no effect. In conclusion, alpha 1-adrenoceptor stimulation increases 86Rb+ efflux from the rat heart via K+ channels and a Na-K-2Cl cotransporter. Activation of the Na-K-2Cl cotransporter is apparently dependent on the MAP kinase pathway.

bumetanide; rat heart; potassium channels


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