Pharmacological PKA Inhibition: All May Not Be What It Seems

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Sci. Signal.  03 Jun 2008:
Vol. 1, Issue 22, pp. re4
DOI: 10.1126/scisignal.122re4

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One of the ways in which cells transduce intracellular signals is through the reversible phosphorylation of proteins by enzymes called protein kinases. Protein kinase A (PKA) is one of these kinases; it is activated in response to increases in intracellular cyclic adenosine monophosphate (cAMP) production and is involved in numerous cellular processes, including exocytosis, cell migration, and regulation of gene transcription. Many of the studies that have examined PKA function in cells have used two pharmacological PKA inhibitors, H89 and KT 5720. Recently, a number of studies have identified actions of these compounds that are not related to their ability to block PKA. This may cast doubt onto some of the accepted functions of PKA in cells, which were established in experiments using these inhibitors. Here, I discuss the nonspecific actions of H89 and KT 5720 and compare their actions to those of other PKA inhibitors.