Kinetics of the induction of three translation-regulatory enzymes by interferon.
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.
D000227:Adenine Nucleotides; D000818:Animals; D004790:Enzyme Induction / Q000187:drug effects; D007372:Interferons / Q000494:pharmacology*; D007700:Kinetics; D007739:L Cells / Q000378:metabolism; D051379:Mice; D009843:Oligoribonucleotides; D010727:Phosphoric Diester Hydrolases / Q000096:biosynthesis*; D011118:Polynucleotide Ligases / Q000096:biosynthesis*; D014176:Protein Biosynthesis / Q000187:drug effects*; D011494:Protein Kinases / Q000096:biosynthesis*; D012330:RNA, Double-Stranded / Q000378:metabolism
D000227:Adenine Nucleotides; D009843:Oligoribonucleotides; D012330:RNA, Double-Stranded; D007372:Interferons; D011494:Protein Kinases; D010727:Phosphoric Diester Hydrolases; D011118:Polynucleotide Ligases; C021907:oligoisoadenylate synthetase E