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Am J Physiol Heart Circ Physiol 276: H1655-H1663, 1999;
0363-6135/99 $5.00
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Vol. 276, Issue 5, H1655-H1663, May 1999

Early response kinase and PI 3-kinase activation in adult cardiomyocytes and their role in hypertrophy

Klaus-Dieter Schlüter1, Andreas Simm2, Matthias Schäfer1, Gerhild Taimor1, and Hans Michael Piper1

1 Institut für Physiologie, Justus-Liebig-Universität, Giessen; and 2 Theodor-Boveri-Institut, Physiologische Chemie II, Universität Würzburg, Würzburg, Germany

The present study investigated the role of early response kinase (ERK) and phosphatidylinositol 3 (PI 3)-kinase in ventricular cardiomyocytes from adult rat for the hypertrophic response to alpha -adrenoceptor stimulation. Parameters of the hypertrophic response were stimulation of protein synthesis and induction of creatine kinase BB. The alpha -adrenoceptor agonist phenylephrine (10 µmol/l) activated ERK2 and PI 3-kinase. The protein kinase C inhibitor bisindolylmaleimide (5 µmol/l) and the mitogen-activated protein kinase kinase inhibitor PD-98059 (10 µmol/l) but not the tyrosine kinase inhibitor genistein (100 µmol/l) blocked ERK2 activation. Inhibition of ERK2 activation abolished induction of creatine kinase BB by phenylephrine but not the increase in protein synthesis. The PI 3-kinase inhibitor wortmannin (100 nmol/l) blocked protein synthesis under alpha -adrenoceptor stimulation but did not interfere with ERK2 activation. Inhibition of the ERK2 pathway with PD-98059 did not affect PI 3-kinase activation. We conclude that ERK2- and PI 3-kinase-dependent pathways represent two mutually exclusive ways of signaling that lead to different aspects of the hypertrophic response to alpha -adrenoceptor stimulation.

tyrosine kinase; creatine kinase BB; protein synthesis; mitogen-activated protein kinase


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