Eutigoside C inhibits the production of inflammatory mediators (NO, PGE2, IL‐6) by down‐regulating NF‐κB and MAP kinase activity in LPS‐stimulated RAW 264.7 cells

Eutigoside C, a compound isolated from the leaves of Eurya emarginata, is thought to be an active anti‐inflammatory compound which operates through an unknown mechanism. In the present study we investigated the molecular mechanisms of eutigoside C activity in lipopolysacchardide (LPS)‐stimulated murine macrophage RAW 264.7 cells. Treatment with eutigoside C inhibited LPS‐stimulated production of nitric oxide (NO), prostaglandin E2 (PGE2) and interleukin‐6 (IL‐6). To further elucidate the mechanism of this inhibitory effect of eutigoside C, we studied LPS‐induced nuclear factor (NF)‐κB activation and mitogen‐activated protein (MAP) kinase phosphorylation. Eutigoside C suppressed NF‐κB DNA binding activity, interfering with nuclear translocation of NF‐κB. Eutigoside C suppressed the phosphorylation of three MAP kinases (ERK1/2, JNK and p38). These results suggest that eutigoside C inhibits the production of inflammatory mediators (NO, PGE2 and interleukin‐6) by suppressing the activation and translocation of NF‐κB and the phosphorylation of MAP kinases (ERK1/2, JNK and p38) in LPS‐stimulated murine macrophage RAW 264.7 cells.

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