Kinetics of the induction of three translation-regulatory enzymes by interferon.
Proc Natl Acad Sci U S A, 1979/7;76(7):3208-12.
Kimchi A, Shulman L, Schmidt A, Chernajovsky Y, Fradin A, Revel M
PMID: 226962
Impact factor: 12.779
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.
MeSH terms
Adenine Nucleotides; Animals; Enzyme Induction; Interferons; Kinetics; L Cells; Mice; Oligoribonucleotides; Phosphoric Diester Hydrolases; Polynucleotide Ligases; Protein Biosynthesis; Protein Kinases; RNA, Double-Stranded
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