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Am J Physiol Cell Physiol 282: C768-C774, 2002. First published November 21, 2001; doi:10.1152/ajpcell.00494.2001
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Vol. 282, Issue 4, C768-C774, April 2002

Enhancement of L-type Ca2+ current from neonatal mouse ventricular myocytes by constitutively active PKC-beta II

Kris J. Alden1,*, Paul H. Goldspink2,*, Stuart W. Ruch2, Peter M. Buttrick2, and Jesús García1

1 Department of Physiology and Biophysics and 2 Section of Cardiology, Department of Medicine, College of Medicine, University of Illinois at Chicago, Chicago, Illinois 60607

The cardiac L-type calcium current (ICa) can be modified by activation of protein kinase C (PKC). However, the effect of PKC activation on ICa is still controversial. Some studies have shown a decrease in current, whereas other studies have reported a biphasic effect (an increase followed by a decrease in current or vice versa). A possible explanation for the conflicting results is that several isoforms of PKC with opposing effects on ICa were activated simultaneously. Here, we examined the influence of a single PKC isoform (PKC-beta II) on L-type calcium channels in isolation from other cardiac isoforms, using a transgenic mouse that conditionally expresses PKC-beta II. Ventricular cardiac myocytes were isolated from newborn mice and examined for expression of the transgene using single cell RT-PCR after ICa recording. Cells expressing PKC-beta II showed a twofold increase in nifedipine-sensitive ICa. The PKC-beta II antagonist LY-379196 returned ICa amplitude to levels found in non-PKC-beta II-expressing myocytes. The increase in ICa was independent of Cav1.2-subunit mRNA levels as determined by quantitative RT-PCR. Thus these data demonstrate that PKC-beta is a potent modulator of cardiac L-type calcium channels and that this specific isoform increases ICa in neonatal ventricular myocytes.

second messengers; signal transduction

* K. J. Alden and P. H. Goldspink contributed equally to this work.




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