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J Interferon Res. 1993 Oct;13(5):323-8.

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

Author information

1
Department of Biochemistry, University of Iowa, Iowa City 52242.

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.

PMID:
7905506
DOI:
10.1089/jir.1993.13.323
[Indexed for MEDLINE]

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