Journal
CIRCULATION RESEARCH
Volume 88, Issue 1, Pages 59-62Publisher
LIPPINCOTT WILLIAMS & WILKINS
DOI: 10.1161/01.RES.88.1.59
Keywords
protein kinase C epsilon; stress-activated kinases; stress-activated proteins
Funding
- NHLBI NIH HHS [HL-65431, HL-63901, HL-43151] Funding Source: Medline
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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.
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