Dissociation of protein kinase activity and the induction of the antiviral state in a cell line responsive to the antiviral effects of interferon
| Autor: | Howard M. Johnson, Boyd Hardesty, Russell P. Saneto, Cynthia H. Robbins, Gisela Kramer |
|---|---|
| Rok vydání: | 1981 |
| Předmět: |
Reticulocytes
Biophysics Mitogen-activated protein kinase kinase Biology Virus Replication Biochemistry MAP2K7 Mice L Cells Peptide Elongation Factor 2 Interferon medicine Animals ASK1 Phosphorylation Protein kinase A Molecular Biology Cyclin-dependent kinase 2 Cell Biology Peptide Elongation Factors Protein kinase R Glutathione Cell biology Enzyme Activation Kinetics Enzyme Induction biology.protein Cyclin-dependent kinase 9 Interferons Protein Kinases Ribosomes medicine.drug |
| Zdroj: | Biochemical and biophysical research communications. 103(1) |
| ISSN: | 0006-291X |
| Popis: | Interferons or oxidized glutathione were found to induce double-stranded RNA-dependent protein kinase activity in mouse L cells that phosphorylates the α subunit of eukaryotic peptide initiation factor 2. A mixture of leukocyte/fibroblast interferons as well as immune interferon induced the protein kinase and also suppressed virus replication in the L cells. Oxidized glutathione was equally effective in inducing protein kinase activity, but it did not induce an antiviral state in these cells. The data suggest that a simple cause and effect relationship does not exist between protein kinase induction and the establishment of the antiviral state in a cell that is responsive to the antiviral effects of interferon. |
| Databáze: | OpenAIRE |
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