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*
Institut Pasteur, Laboratoire des Mycoplasmes, Paris; and
Hoechst-Marion-Roussel, Centre de Recherche Romainville, Romainville, France
Stimulation of monocytes and resident macrophages by mycoplasmas
induces production of numerous cytokines. We have previously reported
that membrane lipoproteins derived from Mycoplasma
fermentans are responsible for the induction of proinflammatory
cytokines by monocytic cells and that triggering protein tyrosine
kinase activation is an essential requirement for this biologic effect.
In the present study, we have investigated the effect of M.
fermentans-derived membrane lipoproteins (LAMPf) on
mitogen-activated protein kinase (MAPK) cascades in the murine
macrophage cell line RAW 264.7 and have analyzed the contribution of
these pathways to the cytokine induction mediated by this agent.
Treatment of murine macrophages with LAMPf resulted in significant
activation of MAPK family members extracellular signal-regulated kinase
1 and 2 (ERK1/2), c-Jun NH2-terminal kinase (JNK), and p38. Unlike LPS,
these effects were demonstrated to be independent of the presence of
serum. The activation of MAPKs paralleled the tyrosine kinase
activation and peaked at 30 min after stimulation. The specific p38
inhibitor SB203580 abrogated the mycoplasma-induced IL-6, IL-1ß, and
TNF-
synthesis. The selective MAPK/extracellular signal-regulated
kinase 1 (MEK-1) inhibitor PD-98059 blocked both IL-1ß and TNF-
but not IL-6 production by RAW 264.7 cells in response to LAMPf.
Additionally, transfection of murine macrophages with a JNK dominant
negative mutant significantly reduced only IL-6 production. These data
underscore the role of MAPKs as signal transduction molecules
controlling the expression of cytokines upon mycoplasma stimulation.
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