© 1996 American Heart Association, Inc.
Articles |
Protein Kinase C Isoform Expression in Normal and Failing Rabbit Hearts
Unite INSERM U 400, Faculte de Medecine (P.R.-B., K.M., J.P., N.E.H.B., B.C.), and Unite INSERM U99, Hopital Henri Mondor (M.P.), Creteil, France.
Correspondence to Bertrand Crozatier, INSERM U 400/Faculte de Medecine, 8, rue du General Sarrail, 94010 Creteil, France.
Protein kinase C (PKC) is activated by 
-adrenergic stimulation. Molecular analysis showed that PKC consists of a family of at least 12 isozymes. Studies of their distribution in the heart showed conflicting results. The first goal of our study was thus to characterize cardiac PKC in normal rabbits. PKC plays an important role in gene expression, cell growth, and differentiation and is involved in the hypertrophy phase of cardiac overload, but since its expression has never been evaluated in heart failure, the second goal of our study was to evaluate PKC activity and isoform expression in rabbits with heart failure induced by a double hemodynamic overload (aortic insufficiency followed by an aortic stenosis). In the first part of the study, PKC isoform expression analyzed in normal rabbits by immunoblotting showed that isoforms , ß, 
, and 
were expressed along with PKC
, which had never been detected in the heart. PKC expression was also identified by polymerase chain reaction, and immunofluorescence techniques showed a localization on intercalated disks associated with the membrane localization observed with the other isoforms. In the second part of the study, PKC activity, content, and isoform expression showed a decrease of 37% in the failing group. PKC immunodetection with a monoclonal antibody (Mab 1.9) recognizing the catalytic domain of all PKC isoforms revealed a 20% decrease in the failing ventricles compared with normal left ventricles. Expressed PKC isoforms quantified by Western blot showed, in the failing heart group compared with the control group, a decrease of 27%, 32%, 16%, and 9% of PKC, PKCß1, PKC, and PKC, respectively, whereas PKC was not significantly modified. These results show that, in heart failure, PKC activity and expression of Ca2+-dependent PKC isoforms are decreased. This may lead to alterations of PKC-induced phosphorylations.
Key Words: protein kinase C isoforms • heart failure • signal transduction
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