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Am J Physiol Heart Circ Physiol 279: H2658-H2664, 2000;
0363-6135/00 $5.00
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Vol. 279, Issue 6, H2658-H2664, December 2000

Evidence for functional role of epsilon PKC isozyme in the regulation of cardiac Ca2+ channels

Keli Hu1, Daria Mochly-Rosen3, and Mohamed Boutjdir1,2

1 Molecular and Cellular Cardiology Program, Veterans Affairs New York Harbor Healthcare System, and 2 State University of New York Health Science Center, Brooklyn, New York 11209; and 3 Department of Molecular Pharmacology, Stanford University, School of Medicine, Stanford, California 94305

Limited information is available regarding the effects of protein kinase C (PKC) isozyme(s) in the regulation of L-type Ca2+ channels due to lack of isozyme-selective modulators. To dissect the role of individual PKC isozymes in the regulation of cardiac Ca2+ channels, we used the recently developed novel peptide activator of the epsilon PKC, epsilon V1-7, to assess the role of epsilon PKC in the modulation of L-type Ca2+ current (ICa,L). Whole cell ICa,L was recorded using patch-clamp technique from rat ventricular myocytes. Intracellular application of epsilon V1-7 (0.1 µM) resulted in a significant inhibition of ICa,L by 27.9 ± 2.2% (P < 0.01, n = 8) in a voltage-independent manner. The inhibitory effect of epsilon V1-7 on ICa,L was completely prevented by the peptide inhibitor of epsilon PKC, epsilon V1-2 [5.2 ± 1.7%, not significant (NS), n = 5] but not by the peptide inhibitors of cPKC, alpha C2-4 (31.3 ± 2.9%, P < 0.01, n = 6) or beta C2-2 plus beta C2-4 (26.1 ± 2.9%, P < 0.01, n = 5). In addition, the use of a general inhibitor (GF-109203X, 10 µM) of the catalytic activity of PKC also prevented the inhibitory effect of epsilon V1-7 on ICa,L (7.5 ± 2.1%, NS, n = 6). In conclusion, we show that selective activation of epsilon PKC inhibits the L-type Ca channel in the heart.

calcium channels; protein kinase C; whole cell patch clamp; peptides; cardiac myocytes


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