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• W2014233524 abstract "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 α-induced MMP-1 gene expression in a concentration-dependent manner. Therefore, we have attempted to characterize the inhibitory mechanism of emodin in TNF α-induced MMP-1 expression. Emodin was determined to inhibit TNF α-induced activation of AP-1 promoter, an important nuclear transcription factor in MMP-1 expression. Additionally, we detected that emodin suppressed the TNF α-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 α-induced phosphorylation of p38 kinase. In a consistent result, the TNF α-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 α-induced MMP-1 expression through the inhibition of the AP-1 signaling pathway." @default.
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• W2014233524 date "2006-11-01" @default.
• W2014233524 modified "2023-10-17" @default.
• W2014233524 title "Emodin inhibits TNF α-induced MMP-1 expression through suppression of activator protein-1 (AP-1)" @default.
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• W2014233524 doi "https://doi.org/10.1016/j.lfs.2006.08.008" @default.
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