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

Circ Res. 2001 Jan 19;88(1):59-62. doi: 10.1161/01.res.88.1.59.


Using two-dimensional electrophoresis, mass spectrometry, immunoblotting, and affinity pull-down assays, we found that myocardial protein kinase C epsilon (PKCepsilon) 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 PKCepsilon is coupled with dynamic modulation and recruitment of PKCepsilon-associated proteins. The results suggest heretofore-unrecognized functions of PKCepsilon and provide an integrated framework for the understanding of PKCepsilon-dependent signaling architecture and cardioprotection.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Cardiovascular Agents / analysis
  • Electrophoresis, Gel, Two-Dimensional
  • Isoenzymes / analysis*
  • Isoenzymes / genetics
  • Isoenzymes / physiology
  • Mice
  • Mice, Transgenic
  • Myocardium / chemistry*
  • Myocardium / enzymology
  • Protein Kinase C / analysis*
  • Protein Kinase C / genetics
  • Protein Kinase C / physiology
  • Protein Kinase C-epsilon
  • Protein Processing, Post-Translational
  • Proteome / analysis*
  • Proteome / physiology
  • Signal Transduction*


  • Cardiovascular Agents
  • Isoenzymes
  • Proteome
  • Prkce protein, mouse
  • Protein Kinase C
  • Protein Kinase C-epsilon