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Submitted on December 20, 2001
Revised on May 21, 2002
Accepted on May 21, 2002

Protein kinase C epsilon signaling complexes include metabolism- and transcription/translation-related proteins: complimentary electrophoretic separation techniques with LC/MS/MS

Ricky D. Edmondson, Thomas M. Vondriska, Kelli J. Biederman, Jun Zhang, Richard C. Jones, Yuting Zheng, David L. Allen, Joanne X. Xiu, Ernest M. Cardwell, Michael R. Pisano, and Peipei Ping

Physiology and Biophysics, Medicine, University of Louisville, Louisville, KY 40202

Corresponding Author: ping{at}ntr.net

The serine/threonine kinase protein kinase C epsilon (PKCepsilon ) has been demonstrated to be a necessary component in the heart’s resistance to cell death following ischemic insult. Recent studies have indicated that PKCepsilon forms multi-protein signaling complexes in order to accomplish signal transduction in cardiac protection. Using two dimensional electrophoresis (2DE) combined with matrix-assisted laser desorption ionization (MALDI) mass spectrometry (MS), the initial analysis of these complexes identified signaling molecules, structural proteins, and stress-activated proteins (Ping et al Circ Res. 2001;88:59-62). This initial analysis, although fruitful, was limited by the number of proteins revealed on the 2D gels. It was also apparent that many known cardiac protective functions of PKCepsilon could not be fully accounted for by the proteins identified in the initial analysis. Here we report the identification of an additional 57 proteins in PKCepsilon complexes using complimentary separation techniques combined with high sensitivity MS. These techniques include 2DE or large format 1D SDS-PAGE followed by LC/MS/MS, and solution trypsin digestion followed by LC/MS/MS, all of which yielded novel data regarding PKCepsilon protein complexes. Nanoscale LC/MS/MS for the analysis of gel-isolated proteins was performed with sub-femtomole sensitivity. In contrast to 2DE analyses, the identification of proteins from 1D gels was independent of their visualization via staining. Furthermore, 1D SDS-PAGE analyses allowed for the identification of proteins with high isoelectric points. We found that PKCepsilon complexes contain numerous structural and signaling molecules that had escaped detection by our previous analyses. Most importantly, we identified two new groups of proteins that were previously unrecognized as components of the PKCepsilon complex: metabolism-related proteins (such as creatine kinase and ATP synthase) and transcription/translation-related proteins (such as ribosomal proteins and hnRNPs).


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