Functional Proteomic Analysis of Protein Kinase C ε Signaling Complexes in the Normal Heart and During Cardioprotection
Copyright policy )Functional Proteomic Analysis of Protein Kinase C ε Signaling Complexes in the Normal Heart and During Cardioprotection
Abstract— Using two-dimensional electrophoresis, mass spectrometry, immunoblotting, and affinity pull-down assays, we found that myocardial protein kinase C ε (PKCε) 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 PKCε is coupled with dynamic modulation and recruitment of PKCε-associated proteins. The results suggest heretofore-unrecognized functions of PKCε and provide an integrated framework for the understanding of PKCε-dependent signaling architecture and cardioprotection.
- University of Louisville United States
- Lung Institute United States
Proteome, Myocardium, Cardiovascular Agents, Mice, Transgenic, Protein Kinase C-epsilon, Isoenzymes, Mice, Animals, Electrophoresis, Gel, Two-Dimensional, Protein Processing, Post-Translational, Protein Kinase C, Signal Transduction
Proteome, Myocardium, Cardiovascular Agents, Mice, Transgenic, Protein Kinase C-epsilon, Isoenzymes, Mice, Animals, Electrophoresis, Gel, Two-Dimensional, Protein Processing, Post-Translational, Protein Kinase C, Signal Transduction
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