© 2000 American Heart Association, Inc.
Integrative Physiology |
Cardiotrophic Effects of Protein Kinase C 
Analysis by In Vivo Modulation of PKC Translocation
From the Department of Molecular Pharmacology (D.M.-R., T.L.), Stanford University School of Medicine, Stanford, Calif; Departments of Medicine (G.W., H.H., G.W.D.), Physiology (J.N.L.), and Pharmacology (H.O., J.R.), University of Cincinnati Medical Center, Cincinnati, Ohio; and Department of Pediatrics (A.K.), Children’s Hospital Medical Center, Cincinnati, Ohio.
Correspondence to G.W. Dorn II, Division of Cardiology, University of Cincinnati Medical Center, 231 Bethesda Ave, Cincinnati, Ohio 45267-0542. E-mail dorngw{at}ucmail.uc.edu
Abstract—Protein kinase C (PKC)
is a key mediator of many diverse physiological and
pathological responses. Although little is known about the specific in
vivo roles of the various cardiac PKC isozymes, activation-induced
translocation of PKC is believed to be the primary determinant of
isozyme-specific functions. Recently, we have identified a
catalytically inactive peptide translocation inhibitor
(
V1) and translocation activator (
RACK
[receptors for activated C
kinase]) specifically targeting PKC. Using
cardiomyocyte-specific transgenic expression of these
peptides, we combined loss- and gain-of-function approaches to
elucidate the in vivo consequences of myocardial PKC signaling. As
expected for a PKC RACK binding peptide, confocal microscopy showed
that V1 decorated cross-striated elements and intercalated disks of
cardiac myocytes. Inhibition of cardiomyocyte PKC by
V1 at lower expression levels upregulated 
–skeletal actin gene
expression, increased cardiomyocyte cell size, and modestly
impaired left ventricular fractional shortening. At high
expression levels, V1 caused a lethal dilated
cardiomyopathy. In contrast, enhancement of PKC
translocation with RACK resulted in selectively increased ß
myosin heavy chain gene expression and normally functioning concentric
ventricular remodeling with decreased
cardiomyocyte size. These results identify for the first
time a role for PKC signaling in normal postnatal maturational
myocardial development and suggest the potential for PKC
activators to stimulate
"physiological" cardiomyocyte growth.
Key Words: protein kinase C • transgenic mouse • cardiac hypertrophy • cardiomyopathy
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