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(Circulation Research. 2001;88:59.)
© 2001 American Heart Association, Inc.


Molecular Medicine

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

Peipei Ping, Jun Zhang, William M. Pierce, Jr, Roberto Bolli

From the Department of Physiology and Biophysics (P.P., R.B.), the Department of Medicine/Division of Cardiology (P.P., J.Z., R.B.), the Department of Pharmacology and Toxicology (W.M.P.), University of Louisville, and the Jewish Hospital Heart and Lung Institute, Louisville, Ky.

Correspondence to Peipei Ping, PhD, Cardiology Research, Baxter Building, Suite 122, 570 S Preston St, Louisville, KY 40202-1783. E-mail ping{at}ntr.net

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


Key Words: protein kinase C {epsilon} • stress-activated kinases • stress-activated proteins




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