Journal
CLINICAL SCIENCE
Volume 130, Issue 17, Pages 1499-1510Publisher
PORTLAND PRESS LTD
DOI: 10.1042/CS20160036
Keywords
myocardial remodelling; post translational modification; protein kinase C
Categories
Funding
- National Institutes of Health [R01 GM43154, HL123061]
- UCSD Graduate Training Program in Cellular and Molecular Pharmacology [T32 GM007752]
- NSF Graduate Research Fellowship [DGE1144086]
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Protein phosphorylation is a highly-regulated and reversible process that is precisely controlled by the actions of protein kinases and protein phosphatases. Factors that tip the balance of protein phosphorylation lead to changes in a wide range of cellular responses, including cell proliferation, differentiation and survival. The protein kinase C (PKC) family of serine/threonine kinases sits at nodal points in many signal transduction pathways; PKC enzymes have been the focus of considerable attention since they contribute to both normal physiological responses as well as maladaptive pathological responses that drive a wide range of clinical disorders. This review provides a background on the mechanisms that regulate individual PKC isoenzymes followed by a discussion of recent insights into their role in the pathogenesis of diseases such as cancer. We then provide an overview on the role of individual PKC isoenzymes in the regulation of cardiac contractility and pathophysiological growth responses, with a focus on the PKC-dependent mechanisms that regulate pump function and/or contribute to the pathogenesis of heart failure.
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