Pharmacological PKA Inhibition

All May Not Be What It Seems

Andrew John Murray

Research output: Contribution to journalLiterature review

203 Citations (Scopus)

Abstract

Signaling through the cyclic adenosine monophosphate–dependent protein kinase [protein kinase A (PKA)] is an important and widely studied area of signal transduction research. This signaling pathway is commonly investigated through the use of the pharmacological PKA inhibitors H89 and KT 5720. Both of these compounds are thought to block PKA actions through competitive inhibition of the adenosine triphosphate site on the PKA catalytic subunit. Recently, a number of studies have identified actions of H89 and KT 5720 that are independent of their effects on PKA. These nonspecific effects are widespread; they include actions on other protein kinases and signaling molecules and also on basic cellular functions, such as transcription. Here, I summarize the nonspecific effects of these two compounds and compare their actions with those of other PKA inhibitors.
Original languageEnglish
Pages (from-to)re4
JournalScience Signaling
Volume1
Issue number22
DOIs
Publication statusPublished - 3 Jun 2008

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Cyclic AMP-Dependent Protein Kinases
Pharmacology
Protein Kinase Inhibitors
Protein Kinases
Signal transduction
Transcription
Adenosine
Signal Transduction
Catalytic Domain
Adenosine Triphosphate
Molecules
Research

Cite this

Pharmacological PKA Inhibition : All May Not Be What It Seems. / Murray, Andrew John.

In: Science Signaling, Vol. 1, No. 22, 03.06.2008, p. re4.

Research output: Contribution to journalLiterature review

Murray, Andrew John. / Pharmacological PKA Inhibition : All May Not Be What It Seems. In: Science Signaling. 2008 ; Vol. 1, No. 22. pp. re4.
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