title: 2-Aminopurine inhibits the double-stranded RNA-dependent protein kinase both in vitro and in vivo.
abstract: 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.
authors.affiliation: Department of Biochemistry, University of Iowa, Iowa City 52242.
authors.forename: Y
authors.initials: Y
authors.lastname: Hu
authors.forename: T W
authors.initials: TW
authors.lastname: Conway
mesh_terms: D015075:2-Aminopurine / Q000494:pharmacology*; D000255:Adenosine Triphosphate / Q000494:pharmacology; D004789:Enzyme Activation; D006367:HeLa Cells; D006801:Humans; D066298:In Vitro Techniques; D010766:Phosphorylation; D017346:Protein Serine-Threonine Kinases / Q000037:antagonists & inhibitors*; D019892:eIF-2 Kinase
chemical_list: D015075:2-Aminopurine; D000255:Adenosine Triphosphate; D017346:Protein Serine-Threonine Kinases; D019892:eIF-2 Kinase