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• W4250404637 endingPage "2737" @default.
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• W4250404637 abstract "Interleukin-1 (IL-1) is known to synergize with phorbol esters in the induction of interleukin-2 (IL-2) expression in T-lymphoid leukemia cells and proliferation of mouse thymocytes. We used a plasmid construct containing the bacterial gene for chloramphenicol acetyltransferase under the control of the human IL-2 promoter to study the nature of this synergism in the murine thymoma cell line EL4. Although IL-1 induction of the IL-2 promoter in these cells required costimulus with phorbol myristate acetate, the signal induced by IL-1 was qualitatively different. We provide evidence to support the hypothesis that the phorbol ester signal is mediated by protein kinase C, and we show that the IL-1 signal is not. That IL-1 and phorbol myristate acetate represent different stimuli was shown by their response to protein kinase C inhibitors, capacity to synergize with increased intracellular free calcium, and requirement for protein synthesis. In addition we show that pretreatment with IL-1 can prime EL4 cells to subsequent activation by concentrations of phorbol esters not normally sufficient to induce IL-2 expression. Pretreated cells remained primed for at least 40 h after removal of the IL-1. Neither phorbol myristate acetate nor a calcium ionophore was capable of preactivating EL4 cells." @default.
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• W4250404637 date "1990-06-01" @default.
• W4250404637 modified "2023-09-25" @default.
• W4250404637 title "A Role for Protein Kinase C Activity in Interleukin-1 (IL-1) Induction of IL-2 Gene Expression but Not in IL-1 Signal Transduction" @default.
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• W4250404637 doi "https://doi.org/10.1128/mcb.10.6.2731-2737.1990" @default.
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