Functional proteomic analysis of protein kinase C epsilon signaling complexes in the normal heart and during cardioprotection

Using two-dimensional electrophoresis, mass spectrometry, immunoblotting, a nd affinity pull-down assays, we found that myocardial protein kinase C eps ilon (PKC epsilon) is physically associated with at least 36 known proteins that are organized into structural proteins, signaling molecules, and stre ss-responsive proteins. Furthermore, we found that the cardioprotection ind uced by activation of PKC epsilon is coupled with dynamic modulation and re cruitment of PKC epsilon -associated proteins. The results suggest heretofo re-unrecognized functions of PKC epsilon and provide an integrated framewor k for the understanding of PKC epsilon -dependent signaling architecture an d cardioprotection.