Identification of PKC-isoform-specific biological actions using pharmacological approaches.
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.
Way
K J
KJ
Harvard Medical School, Joslin Diabetes Center, One Joslin Place, Boston, MA 02215, USA. kerrie.way@joslin.havard.edu
Chou
E
E
King
G L
GL
D000818:Animals; D020536:Enzyme Activators / Q000494:pharmacology*; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D006801:Humans; D007527:Isoenzymes / Q000037:antagonists & inhibitors / Q000502:physiology; D011493:Protein Kinase C / Q000037:antagonists & inhibitors / Q000378:metabolism*; D013379:Substrate Specificity
D020536:Enzyme Activators; D004791:Enzyme Inhibitors; D007527:Isoenzymes; D011493:Protein Kinase C