Substrate-dependent inhibition of protein kinase C by specific inhibitors

FEBS Lett. 1990 Apr 9;263(1):169-71. doi: 10.1016/0014-5793(90)80731-w.

Abstract

Protein kinase C (PKC) and its proteolysis-derived protein kinase independent of Ca2+ and phospholipids (PKM), were purified from rat brain. By using histone H1 and protamine as substrates, we assayed the effect of several inhibitors of PKC and PKM. The inhibition turned out to be dependent on both the nature of the kinase and the type of substrate assayed. These results may help to interpret the different responses elicited by PKC inhibitors in vivo.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine
  • Alkaloids / pharmacology
  • Animals
  • Brain / enzymology
  • Chromatography, Affinity
  • Chromatography, Ion Exchange
  • Gossypol / pharmacology
  • Homeostasis
  • Isoquinolines / pharmacology
  • Kinetics
  • Ligands
  • Piperazines / pharmacology
  • Protein Kinase C / antagonists & inhibitors*
  • Protein Kinase C / isolation & purification
  • Quercetin / pharmacology
  • Rats
  • Sphingosine / pharmacology
  • Staurosporine
  • Substrate Specificity

Substances

  • Alkaloids
  • Isoquinolines
  • Ligands
  • Piperazines
  • 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine
  • Quercetin
  • Protein Kinase C
  • Staurosporine
  • Gossypol
  • Sphingosine