2-Aminopurine inhibits the double-stranded RNA-dependent protein kinase both in vitro and in vivo

J Interferon Res. 1993 Oct;13(5):323-8. doi: 10.1089/jir.1993.13.323.


The autophosphorylation of interferon (IFN)-induced double-stranded RNA-dependent p68 protein kinase (PKR) and phosphorylation of the alpha-subunit of the translation initiation factor eIF-2 were inhibited by 10 mM 2-aminopurine in vitro. High concentrations of ATP overcame the inhibition. Kinetic studies indicated that 2-aminopurine is a competitive inhibitor with respect to ATP, suggesting that these two molecules bind the same site on the kinase. Treatment of HeLa cells with poly(I):poly(C) stimulated PKR autophosphorylation in vivo. The stimulated activity was inhibited by 10 mM 2-aminopurine to approximately the same extent as the in vitro inhibition.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 2-Aminopurine / pharmacology*
  • Adenosine Triphosphate / pharmacology
  • Enzyme Activation
  • HeLa Cells
  • Humans
  • In Vitro Techniques
  • Phosphorylation
  • Protein Serine-Threonine Kinases / antagonists & inhibitors*
  • eIF-2 Kinase


  • 2-Aminopurine
  • Adenosine Triphosphate
  • Protein Serine-Threonine Kinases
  • eIF-2 Kinase