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Updated: Aug 16, 2026

Live-imaging of PKC Translocation in Sf9 Cells and in Aplysia Sensory Neurons
Published on: April 6, 2011
Identification of PKC-isoform-specific biological actions using pharmacological approaches
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.
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