Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.bcp.2004.03.032
Title: Inhibitory effect of emodin on tumor invasion through suppression of activator protein-1 and nuclear factor-κB
Authors: Huang, Q. 
Shen, H.-M. 
Ong, C.-N. 
Keywords: 12-O-tetradecanoylphorbol-13-acetate
activator protein-1
AP-1
dithiothreitol
DTT
MAPK
matrix metalloproteinase
MMP
NF-κB
nuclear factor kappaB
PAGE
polyacrylamide gel electropheresis
SDS
sodium dodecyl sulfate
TPA
Issue Date: 15-Jul-2004
Citation: Huang, Q., Shen, H.-M., Ong, C.-N. (2004-07-15). Inhibitory effect of emodin on tumor invasion through suppression of activator protein-1 and nuclear factor-κB. Biochemical Pharmacology 68 (2) : 361-371. ScholarBank@NUS Repository. https://doi.org/10.1016/j.bcp.2004.03.032
Abstract: 3-Methyl-1,6,8-trihydroxyanthraquinone (emodin) is an active component from the rhizome of Rheum palmatum, a widely used traditional Chinese herb. In this study, we found that emodin significantly inhibited 12-O-tetradecanoylphorbol- 13-acetate (TPA)-induced in vitro invasion of human cancer cells including HSC5 and MDA-MB-231 cells. Matrix metalloproteinases (MMPs) are known to be associated with cancer invasion. Zymographic analysis showed that emodin suppressed TPA-induced MMP-9 activity in a concentration-dependent manner. We further demonstrated that emodin reduced the transcriptional activity of activator protein-1 (AP-1) and nuclear factor kappaB (NF-κB), two important nuclear transcription factors involved in MMP-9 expression. Emodin suppressed the phosphorylation of two mitogen-activated protein kinases, extracellular signal-regulated protein kinase and c-Jun N-terminal kinase, but not p38 kinase, leading to reduced c-Jun phosphorylation and AP-1 DNA-binding. Moreover, emodin inhibited TPA-induced degradation of inhibitor of kappaBα, nuclear translocation of p65, and NF-κB DNA-binding activity. Taken together, these results suggest that emodin inhibits the invasiveness of human cancer cells by suppressing MMP-9 expression through inhibiting AP-1 and NF-κB signaling pathways. © 2004 Elsevier Inc. All rights reserved.
Source Title: Biochemical Pharmacology
URI: http://scholarbank.nus.edu.sg/handle/10635/113528
ISSN: 00062952
DOI: 10.1016/j.bcp.2004.03.032
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