Molecular Medicine |
Signaling Complexes in the Normal Heart and During Cardioprotection
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
AbstractUsing
two-dimensional electrophoresis, mass spectrometry, immunoblotting, and
affinity pull-down assays, we found that myocardial protein
kinase C
(PKC
) 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
is coupled with
dynamic modulation and recruitment of PKC
-associated proteins. The
results suggest heretofore-unrecognized functions of PKC
and provide
an integrated framework for the understanding of PKC
-dependent
signaling architecture and cardioprotection.
Key Words: protein kinase C
stress-activated kinases stress-activated proteins
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