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Emodin inhibits TNF alpha-induced MMP-1 expression through suppression of activator protein-1 (AP-1)
Jongsung Lee1, Eunsun Jung, Jiyoung Lee
1Biospectrum Life Science Institute, Gunpo City, Gyunggi Do, Republic of Korea.
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 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.
Insights
Emodin, derived from Rheum palmatum, inhibits tumor necrosis factor alpha-induced matrix metalloproteinase-1 (MMP-1) gene expression. This natural compound suppresses MMP-1 via the AP-1 signaling pathway, impacting tissue remodeling.
Area of Science:
- Biochemistry
- Molecular Biology
- Pharmacology
Background:
- Matrix metalloproteinases (MMPs) degrade the extracellular matrix.
- MMP-1 is crucial in fibrolysis and tissue remodeling.
- Tumor necrosis factor alpha (TNF-α) can induce MMP-1 expression.
Purpose of the Study:
- To investigate the inhibitory mechanism of emodin on TNF-α-induced MMP-1 expression.
- To characterize how emodin affects the signaling pathways regulating MMP-1.
Main Methods:
- Assessed emodin's effect on TNF-α-induced MMP-1 gene expression.
- Analyzed emodin's impact on AP-1 promoter activation.
- Measured the phosphorylation of mitogen-activated protein kinases (MAPKs) including ERK, JNK, and p38.
- Utilized specific MAPK inhibitors (PD98059, SP600125, SB203580).
Main Results:
- Emodin significantly inhibited TNF-α-induced MMP-1 gene expression in a dose-dependent manner.
- Emodin suppressed TNF-α-induced AP-1 promoter activation.
- Emodin inhibited the phosphorylation of ERK and JNK, but not p38 MAPK.
- Inhibitors of MEK/ERK and JNK mimicked emodin's inhibitory effect on MMP-1 expression.
Conclusions:
- Emodin suppresses TNF-α-induced MMP-1 expression.
- The mechanism involves the inhibition of the AP-1 signaling pathway.
- Emodin's effects are mediated through the suppression of ERK and JNK signaling.
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