Inhibition of angiotensin-converting enzyme (ACEI) after myocardial infarction reduces remodeling of the surviving myocardium. The cellular signaling mechanisms contributing to remodeling are not fully elucidated. Goal of the current study was to test whether protein kinase C (PKC) is regulated in the surviving myocardium shortly after infarction and whether this regulation is influenced by ACEI. Rats were subjected to anterior wall myocardial infarction in vivo or sham operation. After 15-45 min, mRNA levels and protein expression of the major cardiac PKC isoforms were measured in the ischemic and the remote myocardium. The influence of ACEI on PKC was tested by pretreating the rats with ramiprilat. In the ischemic region of the myocardium, a significant increase of the mRNA for PKC-delta and PKC-epsilon was observed in close correlation with increased isoform protein expression. In the surviving, remote myocardium, however, only PKC-epsilon expression was significantly augmented both at the mRNA level (158%) and at the protein level (149%). PKC-delta and PKC-alpha were unchanged. Treatment with ramiprilat could abolish this isoform-specific PKC regulation in both areas. These data characterize for the first time an isoform-specific transcriptional regulation process of PKC in the surviving myocardium after infarction. This induction of PKC-epsilon can be prevented by ACEI. It is speculated that PKC-epsilon plays a role in the signal transduction of early remodeling after infarction.

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