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Vol. 62, Issue 2, 193-199, August 2002
Department of Pediatrics, Heart Research Center, Oregon Health and
Science University, Portland, Oregon
The cAMP-dependent protein kinase (PKA) transduces signals in the heart
initiated by 
1-adrenergic, G-protein-coupled receptors after norepinephrine, sympathetic stimulation. Signaling through this
pathway results in a characteristic set of cellular responses, including increases in ion fluxes and contractile strength,
mobilization of energy stores, and changes in gene expression. Not all
receptors that activate adenylate cyclase and increase cAMP levels,
however, cause the cardiac myocyte to react in this manner. Research in the field of signal transduction over the last 25 years has addressed this issue of specificity in signaling by diffusable second messengers. PKA is in part targeted to discrete cellular locations by A-kinase anchoring proteins. Through anchoring and formation of multienzyme complexes, specific, localized signal transduction is possible. I
discuss in this review recent advances in the understanding of PKA
signaling complexes in the cardiac myocyte.
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