Abstract
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.
Original language | English (US) |
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Pages (from-to) | 917-924 |
Number of pages | 8 |
Journal | Journal of Pharmacy and Pharmacology |
Volume | 60 |
Issue number | 7 |
DOIs | |
State | Published - Jul 2008 |