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Trends Pharmacol Sci. 2000 May;21(5):181-7.

Identification of PKC-isoform-specific biological actions using pharmacological approaches.

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  • 1Harvard Medical School, Joslin Diabetes Center, One Joslin Place, Boston, MA 02215, USA. kerrie.way@joslin.havard.edu

Abstract

The protein kinase C (PKC) family consists of at least 12 isoforms that possess distinct differences in structure, substrate requirement, expression and localization. To date, identification of the physiological function of individual PKC isoforms has been restricted by the availability of few agents that inhibit or activate the isoforms with specificity. More recent approaches that are used to modulate PKC isoforms include oligonucleotide antisense technology, and peptide fragments to either inhibit or promote translocation of PKC isoforms to specific anchoring proteins. In this review, several currently available inhibitors and activators of PKC that display varying degrees of selectivity for the PKC isoforms will be discussed.

PMID:
10785652
[PubMed - indexed for MEDLINE]
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