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Pharmacol Res. 1999 Apr;39(4):253-9.

Pharmacologic modulation of protein kinase C isozymes: the role of RACKs and subcellular localisation.

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Department of Molecular Pharmacology, Stanford University School of Medicine, Stanford, CA 94305-5332, USA.


Protein kinase C (PKC) isozymes are highly homologous kinases and several different isozymes can be present in a cell. Each isozyme is likely to mediate unique functions, but pharmacological tools to explore their isozyme-specific roles have not been available until recently. In this review, we describe the development and application of isozyme-selective inhibitors of PKC. The identification of these inhibitors stems from the observation that PKC isozymes are each localised to unique subcellular locations following activation. Inhibitors of this isozyme-unique localisation have been shown to act as selective inhibitors of the functions of individual isozymes. The identification of isozyme-specific inhibitors should allow the exploration of individual PKC isozyme function in a wide range of cell systems.

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