Abstract
Intervention in protein kinase C (PKC) has a chequered history, partly because of the poor selectivity of many inhibitors and partly a reflection of the sometimes antagonistic action of related PKC isoforms. Recent advances in targeting PKC isoforms have come from structural work on isolated kinase domains that have provided opportunities to drive selectivity through structure-based avenues. The promise of isoform selective inhibitors and the rationale for their development are discussed in the broader context of the PKC inhibitor arsenal.
MeSH terms
-
Animals
-
Catalytic Domain
-
Clinical Trials as Topic
-
Enzyme Activation
-
Enzyme Inhibitors / chemistry
-
Enzyme Inhibitors / therapeutic use
-
Humans
-
Isoenzymes / antagonists & inhibitors*
-
Isoenzymes / genetics
-
Isoenzymes / metabolism
-
Molecular Structure
-
Multigene Family
-
Neoplasms / drug therapy
-
Oligonucleotides, Antisense / therapeutic use
-
Protein Kinase C / antagonists & inhibitors*
-
Protein Kinase C / genetics
-
Protein Kinase C / metabolism
-
Signal Transduction / physiology
Substances
-
Enzyme Inhibitors
-
Isoenzymes
-
Oligonucleotides, Antisense
-
Protein Kinase C