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dc.contributor.authorPark, Jun Yeon-
dc.contributor.authorPark, Do Hwi-
dc.contributor.authorJeon, Youngsic-
dc.contributor.authorKim, Young-Joo-
dc.contributor.authorLee, Jaemin-
dc.contributor.authorShin, Myoung-Sook-
dc.contributor.authorKang, Ki Sung-
dc.contributor.authorHwang, Gwi Seo-
dc.contributor.authorKim, Hyun Young-
dc.contributor.authorYamabe, Noriko-
dc.date.accessioned2024-01-19T21:32:48Z-
dc.date.available2024-01-19T21:32:48Z-
dc.date.created2021-09-05-
dc.date.issued2018-10-15-
dc.identifier.issn0960-894X-
dc.identifier.urihttps://pubs.kist.re.kr/handle/201004/120784-
dc.description.abstractMetastasis is responsible for the great majority of deaths in cancer patients. Matrix metalloproteinases (MMPs) have critical functions in cancer metastasis. Especially, MMP-2 and MMP-9 play a major role in tumor-cell migration and invasion. Therefore, to first find out the inhibitory effect of eupatilin on expression of MMPs in SNU182 cells, we used quantitative real-rime PCR to measure MMP-2 and MMP-9 mRNA levels. Eupatilin suppressed transcription of MMP-2 in SNU182 cells more than did the corresponding controls. Also, eupatilin significantly blocked tube formation when treated with a concentration of 3.125 or 6.25 mu g/mL on human umbilical vein vascular endothelial cells (HUVECs). Eupatilin induced significant anti-angiogenic potential associated with down-regulation of hypoxia-inducible factor 1-alpha (HIF-1 alpha), vascular endothelial growth factor (VEGF), and phosphorylated Akt expression. Thus, tube-formation inhibition and MMP-2-mediated migration are likely to be important therapeutic targets of eupatilin in hepatocellular carcinoma metastasis.-
dc.languageEnglish-
dc.publisherPergamon Press Ltd.-
dc.subjectNITRIC-OXIDE SYNTHASE-
dc.subjectMATRIX METALLOPROTEINASES-
dc.subjectEXPRESSION-
dc.subjectCARCINOMA-
dc.subjectPATHOGENESIS-
dc.subjectCOLLAGENASE-
dc.subjectMIGRATION-
dc.subjectEXTRACT-
dc.subjectCELLS-
dc.subjectACID-
dc.titleEupatilin inhibits angiogenesis-mediated human hepatocellular metastasis by reducing MMP-2 and VEGF signaling-
dc.typeArticle-
dc.identifier.doi10.1016/j.bmcl.2018.08.034-
dc.description.journalClass1-
dc.identifier.bibliographicCitationBioorganic & Medicinal Chemistry Letters, v.28, no.19, pp.3150 - 3154-
dc.citation.titleBioorganic & Medicinal Chemistry Letters-
dc.citation.volume28-
dc.citation.number19-
dc.citation.startPage3150-
dc.citation.endPage3154-
dc.description.journalRegisteredClassscie-
dc.description.journalRegisteredClassscopus-
dc.identifier.wosid000446034100003-
dc.identifier.scopusid2-s2.0-85054083552-
dc.relation.journalWebOfScienceCategoryChemistry, Medicinal-
dc.relation.journalWebOfScienceCategoryChemistry, Organic-
dc.relation.journalResearchAreaPharmacology & Pharmacy-
dc.relation.journalResearchAreaChemistry-
dc.type.docTypeArticle-
dc.subject.keywordPlusNITRIC-OXIDE SYNTHASE-
dc.subject.keywordPlusMATRIX METALLOPROTEINASES-
dc.subject.keywordPlusEXPRESSION-
dc.subject.keywordPlusCARCINOMA-
dc.subject.keywordPlusPATHOGENESIS-
dc.subject.keywordPlusCOLLAGENASE-
dc.subject.keywordPlusMIGRATION-
dc.subject.keywordPlusEXTRACT-
dc.subject.keywordPlusCELLS-
dc.subject.keywordPlusACID-
dc.subject.keywordAuthorEupatilin-
dc.subject.keywordAuthorMetastasis-
dc.subject.keywordAuthorHUVEC-
dc.subject.keywordAuthorMMPs-
dc.subject.keywordAuthorVEGF-
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KIST Article > 2018
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