Inhibitors of p38 mitogen-activated protein kinase (p38) have been reported to block tumor necrosis factor ␣ (TNF-␣) and interleukin-1 (IL-1) production in monocytes at the level of mRNA translation. Yet, several studies document that p38 can phosphorylate and activate specific transcription factors. Thus, to understand better the role of p38 during monocyte activation, we sought to determine the extent to which p38 is required for lipopolysaccharide (
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