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Am J Physiol Heart Circ Physiol 282: H2397-H2405, 2002; doi:10.1152/ajpheart.00714.2001
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Vol. 282, Issue 6, H2397-H2405, June 2002

alpha -Adrenergic response and myofilament activity in mouse hearts lacking PKC phosphorylation sites on cardiac TnI

David E. Montgomery1, Beata M. Wolska1,2, W. Glen Pyle1, Brian B. Roman1, Jasmine C. Dowell1, Peter M. Buttrick1,2, Alan P. Koretsky3, Pedro Del Nido4, and R. John Solaro1

Program in Cardiovascular Sciences, 1 Department of Physiology and Biophysics, and 2 Department of Medicine, Section of Cardiology, College of Medicine, University of Illinois at Chicago, Chicago, Illinois 60612; 3 Laboratory of Functional and Molecular Imaging, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, Maryland 20892; and 4 Harvard Medical School, Boston, Massachusetts 02115

Protein kinase C (PKC)-mediated phosphorylation of cardiac myofilament (MF) proteins has been shown to depress the actomyosin interaction and may be important during heart failure. Biochemical studies indicate that phosphorylation of Ser43 and Ser45 of cardiac troponin I (cTnI) plays a substantial role in the PKC-mediated depression. We studied intact and detergent-extracted papillary muscles from nontransgenic (NTG) and transgenic (TG) mouse hearts that express a mutant cTnI (Ser43Ala, Ser45Ala) that lacks specific PKC-dependent phosphorylation sites. Treatment of NTG papillary muscles with phenylephrine (PE) resulted in a transient increase and a subsequent 62% reduction in peak twitch force. TG muscles showed no transient increase and only a 45% reduction in force. There was a similar difference in maximum tension between NTG and TG fiber bundles that had been treated with a phorbol ester and had received subsequent detergent extraction. Although levels of cTnI phosphorylation correlated with these differences, the TG fibers also demonstrated a decrease in phosphorylation of cardiac troponin T. The PKC-specific inhibitor chelerythrine inhibited these responses. Our data provide evidence that specific PKC-mediated phosphorylation of Ser43 and Ser45 of cTnI plays an important role in regulating force development in the intact myocardium.

protein kinase C; troponin I


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