Functional proteomic analysis of protein kinase C epsilon signaling complexes in the normal heart and during cardioprotection.
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.
Ping
P
P
Department of Physiology, Division of Cardiology, University of Louisville, KY, USA.
Zhang
J
J
Pierce
W M
WM
Bolli
R
R
D000818:Animals; D002317:Cardiovascular Agents / Q000032:analysis; D015180:Electrophoresis, Gel, Two-Dimensional; D007527:Isoenzymes / Q000032:analysis* / Q000235:genetics / Q000502:physiology; D051379:Mice; D008822:Mice, Transgenic; D009206:Myocardium / Q000737:chemistry* / Q000201:enzymology; D011493:Protein Kinase C / Q000032:analysis* / Q000235:genetics / Q000502:physiology; D051744:Protein Kinase C-epsilon; D011499:Protein Processing, Post-Translational; D020543:Proteome / Q000032:analysis* / Q000502:physiology; D015398:Signal Transduction
D002317:Cardiovascular Agents; D007527:Isoenzymes; D020543:Proteome; C497256:Prkce protein, mouse; D011493:Protein Kinase C; D051744:Protein Kinase C-epsilon