Potent selective inhibition of 7-O-methyl UCN-01 against protein kinase C

J Pharmacol Exp Ther. 1990 Dec;255(3):1218-21.

Abstract

UCN-01 is a staurosporine-related compound that was isolated from the culture broth of Streptomyces sp. and shows potent and selective inhibitory activity against protein kinase C. Cellular inhibitory activity of UCN-01 against protein kinase C and cytotoxicity of UCN-01 were compared with those of staurosporine. When the mechanism of inhibitory activity was investigated in vitro, UCN-01 as well as staurosporine inhibited the activity of the catalytic domain of protein kinase C. In spite of direct inhibition against the catalytic domain of protein kinase C, cytotoxicity of UCN-01 was much lower than that of staurosporine. In addition, UCN-01 showed more selective inhibitory activity against protein kinase C than did staurosporine because of the sole structural difference at C-7. Therefore, a series of 7-O-alkyl derivatives of UCN-01 was synthesized and investigated. Interestingly, one of the compounds, the beta-methoxy derivative, showed 3-fold greater potency and 17-fold more selective inhibitory activity against protein kinase C than did UCN-01.

Publication types

  • Comparative Study

MeSH terms

  • Alkaloids / pharmacology*
  • Animals
  • Antineoplastic Agents / pharmacology*
  • Cell Survival / drug effects
  • Cells, Cultured
  • Enzyme Activation
  • Kinetics
  • Leukemia, Erythroblastic, Acute / enzymology
  • Leukemia, Erythroblastic, Acute / pathology
  • Mice
  • Protein Kinase C / antagonists & inhibitors*
  • Protein Kinase Inhibitors
  • Staurosporine
  • Tetradecanoylphorbol Acetate / pharmacology
  • Tumor Cells, Cultured

Substances

  • Alkaloids
  • Antineoplastic Agents
  • Protein Kinase Inhibitors
  • 7-O-methyl-UCN 01
  • 7-hydroxystaurosporine
  • Protein Kinase C
  • Staurosporine
  • Tetradecanoylphorbol Acetate