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with the PKC 
complex undergo changes in expression and post-translational modification
during cardioprotection. Our current studies use established biochemical
and physiological strategies in conjunction with classical proteomic
techniques (1D/2D gel electrophoresis, mass spectrometry) to accomplish
a functional proteomic analysis of this PKC
signaling system. The findings of this ongoing investigation, along
with those from other laboratories, suggest that multi-protein complexes
may serve as a means for signal transduction by forming stimulus
and subcellular location specific signaling modules. These modules
are hypothesized to be a functional unit of signal transduction.
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The
overall objective of our research in the future is to understand
the mechanisms that govern assembly of these modules, and allow
for multipurpose stress-activated proteins and signaling kinases
to serve in a variety of distinct subcellular signaling events.
In addition, we are actively implementing this novel functional
proteomic approach to map other sub-proteomes essential for cardiac
function. The long term goal of these studies is the development
of an integrated framework for signal transduction in the heart
that will facilitate the engineering of pharmacological and/or molecular
strategies to prevent heart disease. |
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eart
disease is the leading cause of death in Western Societies. The
primary focus of our laboratory is to understand the molecular signaling
system that protects the heart against injury due to a lack of blood
flow, or “ischemia”. Specifically, we use a functional
proteomic approach to address the role of the serine /threonine
kinase protein kinase C epsilon (PKC