Emodin inhibits TNF alpha- induced MMP-1 expression through suppression of activator protein-1 (AP-1).
Matrix metalloproteinases (MMPs) are the proteases involved in the degradation of the extracellular matrix. MMP-1 is thought to be one of the key enzymes acting in fibrolysis, a process closely related to tissue remodeling. In this study, we found that emodin, an anthraquinone which has been isolated from the rhizome of Rheum palmatum, significantly inhibited TNF alpha- induced MMP-1 gene expression in a concentration-dependent manner. Therefore, we have attempted to characterize the inhibitory mechanism of emodin in TNF alpha- induced MMP-1 expression. Emodin was determined to inhibit TNF alpha- induced activation of AP-1 promoter, an important nuclear transcription factor in MMP-1 expression. Additionally, we detected that emodin suppressed the TNF alpha-induced phosphorylation of two mitogen-activated protein kinases, extracellular signal-regulated protein kinase and c-Jun N-terminal kinase, but it did not suppress the TNF alpha- induced phosphorylation of p38 kinase. In a consistent result, the TNF alpha- induced MMP-1 expression was inhibited by PD98059 (MEK/ ERK inhibitor) and SP600125 (JNK inhibitor), but was not inhibited by SB203580, a p38 MAPK inhibitor. Taken together, these results show that emodin suppresses TNF alpha- induced MMP-1 expression through the inhibition of the AP-1 signaling pathway.[1]References
- Emodin inhibits TNF alpha-induced MMP-1 expression through suppression of activator protein-1 (AP-1). Lee, J., Jung, E., Lee, J., Huh, S., Hwang, C.H., Lee, H.Y., Kim, E.J., Cheon, J.M., Hyun, C.G., Kim, Y.S., Park, D. Life Sci. (2006) [Pubmed]
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