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Am J Physiol Heart Circ Physiol 282: H320-H327, 2002;
0363-6135/02 $5.00
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Vol. 282, Issue 1, H320-H327, January 2002

Protein kinase C-zeta modulates thromboxane A2-mediated apoptosis in adult ventricular myocytes via Akt

Yukitaka Shizukuda1 and Peter M. Buttrick1,2

1 Program in Cardiovascular Sciences, Section of Cardiology, Department of Medicine, and 2 Department of Physiology and Biophysics, University of Illinois at Chicago, Chicago, Illinois 60612

We hypothesized that thromboxane A2 (TxA2) receptor stimulation directly induces apoptosis in adult cardiac myocytes. To investigate this, we exposed cultured adult rat ventricular myocytes (ARVM) to a TxA2 mimetic [1S-[1alpha ,2alpha (Z),3beta (1E,3S*),4alpha ]]-7-[3-[3-hydroxy-4-(4-iodophenoxy)-1-butenyl]-7-oxabicyclo[2.2.1]hept-2-yl]-5-heptenoic acid (I-BOP) for 24 h. Stimulation with I-BOP induced apoptosis in a dose-dependent manner and was completely prevented by a TxA2 receptor antagonist, SQ-29548. We further investigated the role of protein kinase C (PKC) in this process. TxA2 stimulation resulted in membrane translocation of PKC-zeta but not PKC-alpha , -beta II, -delta , and -epsilon at 3 min and 1 h. The activation of PKC-zeta by I-BOP was confirmed using an immune complex kinase assay. Treatment of ARVM with a cell-permeable PKC-zeta pseudosubstrate peptide (zeta -PS) significantly attenuated apoptosis by I-BOP. In addition, I-BOP treatment decreased baseline Akt activity and its decrease was reversed by treatment with zeta -PS. The inhibition of phosphatidylinositol 3-kinase upstream of Akt by wortmannin or LY-294002 abolished the antiapoptotic effect of zeta -PS. Therefore, our results suggest that the activation of PKC-zeta modulates TxA2 receptor-mediated apoptosis at least, in part, through Akt activity in adult cardiac myocytes.

atypical protein kinase C; eicosanoids; Akt/protein kinase B; mitogen activated protein kinases


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