Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.bcp.2004.03.032
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dc.titleInhibitory effect of emodin on tumor invasion through suppression of activator protein-1 and nuclear factor-κB
dc.contributor.authorHuang, Q.
dc.contributor.authorShen, H.-M.
dc.contributor.authorOng, C.-N.
dc.date.accessioned2014-12-01T06:55:30Z
dc.date.available2014-12-01T06:55:30Z
dc.date.issued2004-07-15
dc.identifier.citationHuang, 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
dc.identifier.issn00062952
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/113528
dc.description.abstract3-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.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/j.bcp.2004.03.032
dc.sourceScopus
dc.subject12-O-tetradecanoylphorbol-13-acetate
dc.subjectactivator protein-1
dc.subjectAP-1
dc.subjectdithiothreitol
dc.subjectDTT
dc.subjectMAPK
dc.subjectmatrix metalloproteinase
dc.subjectMMP
dc.subjectNF-κB
dc.subjectnuclear factor kappaB
dc.subjectPAGE
dc.subjectpolyacrylamide gel electropheresis
dc.subjectSDS
dc.subjectsodium dodecyl sulfate
dc.subjectTPA
dc.typeArticle
dc.contributor.departmentCOMMUNITY,OCCUPATIONAL & FAMILY MEDICINE
dc.description.doi10.1016/j.bcp.2004.03.032
dc.description.sourcetitleBiochemical Pharmacology
dc.description.volume68
dc.description.issue2
dc.description.page361-371
dc.description.codenBCPCA
dc.identifier.isiut000222308200017
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