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. 1979 Jul;76(7):3208–3212. doi: 10.1073/pnas.76.7.3208

Kinetics of the induction of three translation-regulatory enzymes by interferon.

A Kimchi, L Shulman, A Schmidt, Y Chernajovsky, A Fradin, M Revel
PMCID: PMC383793  PMID: 226962

Abstract

Three enzymes that cause inhibition of mRNA translation, eukaryotic initiation factor 2 protein kinase PK-i, oligoisoadenylate synthetase E, and phosphodiesterase 2'-PDi, have been recently isolated from interferon-treated cells. We show that the rise in these three enzyme activities may be used to study the response of uninfected cells to interferon. For each enzyme, a specific microassay that can be carried out on extracts from 2-5 x 10(4) monolayer cells from mouse, monkey, or man was developed. With these assays, the kinetics of induction of the three enzymes in mouse L cells are compared. The dose dependence for protein kinase PK-i induction is shown to be similar to that for the development of the antiviral state. Actinomycin D and anti-interferon serum block enzyme induction if added to the cells early after interferon treatment. The quantitative measurements of the intracellular level of these enzymes provide a new and convenient model to study the cell's response to interferon.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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