AJP - Heart Calcium Transients and Cell-Sarcomere
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Am J Physiol Heart Circ Physiol 281: H2500-H2510, 2001;
0363-6135/01 $5.00
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Vol. 281, Issue 6, H2500-H2510, December 2001

Enhanced PKCbeta II translocation and PKCbeta II-RACK1 interactions in PKCepsilon -induced heart failure: a role for RACK1

Jason M. Pass1,2,*, Jiuming Gao1,*, W. Keith Jones3,*, William B. Wead1, Xin Wu1, Jun Zhang2, Christopher P. Baines1,2, Roberto Bolli2, Yu-Ting Zheng1, Irving G. Joshua1, and Peipei Ping1,2

1 Department of Physiology and Biophysics, 2 Division of Cardiology, Department of Medicine, University of Louisville, Louisville, Kentucky 40202; and 3 Department of Pharmacology and Cell Biophysics, University of Cincinnati, Cincinnati, Ohio 45267

Recent investigations have established a role for the beta II-isoform of protein kinase C (PKCbeta II) in the induction of cardiac hypertrophy and failure. Although receptors for activated C kinase (RACKs) have been shown to direct PKC signal transduction, the mechanism through which RACK1, a selective PKCbeta II RACK, participates in PKCbeta II-mediated cardiac hypertrophy and failure remains undefined. We have previously reported that PKCepsilon activation modulates the expression of RACKs, and that altered epsilon -isoform of PKC (PKCepsilon )-RACK interactions may facilitate the genesis of cardiac phenotypes in mice. Here, we present evidence that high levels of PKCepsilon activity are commensurate with impaired left ventricular function (dP/dt = 6,074 ± 248 mmHg/s in control vs. 3,784 ± 269 mmHg/s in transgenic) and significant myocardial hypertrophy. More importantly, we demonstrate that high levels of PKCepsilon activation induce a significant colocalization of PKCbeta II with RACK1 (154 ± 7% of control) and a marked redistribution of PKCbeta II to the particulate fraction (17 ± 2% of total PKCbeta II in control mice vs. 49 ± 5% of total PKCbeta II in hypertrophied mice), without compensatory changes of the other eight PKC isoforms present in the mouse heart. This enhanced PKCbeta II activation is coupled with increased RACK1 expression and PKCbeta II-RACK1 interactions, demonstrating PKCepsilon -induced PKCbeta II signaling via a RACK1-dependent mechanism. Taken together with our previous findings regarding enhanced RACK1 expression and PKCepsilon -RACK1 interactions in the setting of cardiac hypertrophy and failure, these results suggest that RACK1 serves as a nexus for at least two isoforms of PKC, the epsilon -isoform and the beta II-isoform, thus coordinating PKC-mediated hypertrophic signaling.

cardiac phenotype; protein-protein interactions; hypertrophy

* J. M. Pass, J. Gao, and W. K. Jones contributed equally to this study.




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