Functional Proteomic Analysis of Protein Kinase C e Signaling Complexes in the Normal Heart and During Cardioprotection

Using two-dimensional electrophoresis, mass spectrometry, immunoblotting, and affinity pull-down assays, we found that myocardial protein kinase C e (PKCe) is physically associated with at least 36 known proteins that are organized into structural proteins, signaling molecules, and stress-responsive proteins. Furthermore, we found that the cardioprotection induced by activation of PKCe is coupled with dynamic modulation and recruitment of PKCeassociated proteins. The results suggest heretofore-unrecognized functions of PKCe and provide an integrated framework for the understanding of PKCe-dependent signaling architecture and cardioprotection. (Circ Res. 2001;88:59-62.)