Please use this identifier to cite or link to this item: https://ir.swu.ac.th/jspui/handle/123456789/17298
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dc.contributor.authorKittiwattanokhun A.
dc.contributor.authorSamosorn S.
dc.contributor.authorInnajak S.
dc.contributor.authorWatanapokasin R.
dc.date.accessioned2022-03-10T13:16:46Z-
dc.date.available2022-03-10T13:16:46Z-
dc.date.issued2021
dc.identifier.issn7533322
dc.identifier.other2-s2.0-85100802120
dc.identifier.urihttps://ir.swu.ac.th/jspui/handle/123456789/17298-
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85100802120&doi=10.1016%2fj.biopha.2021.111337&partnerID=40&md5=e3dc675fe7142598e0efdf425d535fe8
dc.description.abstractBackground: Senna alata L. Roxb or candle bush is a traditional medicinal plant with a wide range of biological activities including anti-inflammatory, antimicrobial and antifungal. Leaf extract of S. alata showed the anti-tumor activity in various cancer cell lines. In this study, we focused on the inhibitory mechanism of S. alata extract (SAE) on cancer metastasis including cell migration, cell invasion and signaling pathways in chondrosarcoma SW1353 cells. Purpose: This study aimed to evaluate the anti-metastatic mechanisms of Senna alata extract on chondrosarcoma SW1353 cells. Methods: Screening for phytochemicals in biologically active fraction of SAE was analysed by 1H NMR spectroscopy. Cell viability and cytoxicity were determined by using MTT assay. Cell migration was observed by scratch wound healing and transwell migration assay. Cell invasion and cell adhesion assay were examined by Matrigel coated transwell chambers or plates. The expression of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs), MAPKs and PI3K/Akt signaling pathways and NF-κB were detected by Western blot analysis. Results: The SAE treatment at the sub-cytoxic and non-cytotoxic concentrations significantly inhibited cell migration, cell invasion and cell adhesion of SW1353 cells in a dose-dependent manner. The results from Western blot analysis showed decreased MMP-2 and MMP-9 expression, while increased TIMP-1 and TIMP-2 expression in SAE treated cells. Moreover, SAE suppressed phosphorylation of ERK1/2, p38 and Akt but decreased NF-κB transcription factor expression in SW1353 cells. Conclusion: These results revealed that SAE could reduce MMP-2 and MMP-9 expression by downregulation of NF-κB which is downstream of MAPKs and PI3K/Akt signaling pathway in SW1353 cells resulting in reduced cancer cell migration and invasion. Therefore, SAE may have the potential use as an alternative treatment of chondrosarcoma metastasis. © 2021
dc.languageen
dc.subjectantineoplastic agent
dc.subjectchloroform
dc.subjectgelatinase A
dc.subjectgelatinase B
dc.subjectimmunoglobulin enhancer binding protein
dc.subjectmitogen activated protein kinase 1
dc.subjectmitogen activated protein kinase 3
dc.subjectplant extract
dc.subjectSenna alata extract
dc.subjecttissue inhibitor of metalloproteinase 1
dc.subjecttissue inhibitor of metalloproteinase 2
dc.subjectunclassified drug
dc.subjectgelatinase A
dc.subjectgelatinase B
dc.subjectimmunoglobulin enhancer binding protein
dc.subjectmitogen activated protein kinase
dc.subjectMMP2 protein, human
dc.subjectMMP9 protein, human
dc.subjectoncoprotein
dc.subjectphosphatidylinositol 3 kinase
dc.subjectSenna extract
dc.subjectTIMP1 protein, human
dc.subjectTIMP2 protein, human
dc.subjecttissue inhibitor of metalloproteinase 1
dc.subjecttissue inhibitor of metalloproteinase 2
dc.subjectArticle
dc.subjectcell adhesion assay
dc.subjectcell invasion
dc.subjectcell migration
dc.subjectcell proliferation
dc.subjectcell viability
dc.subjectchondrosarcoma
dc.subjectcontrolled study
dc.subjectdown regulation
dc.subjectdrug mechanism
dc.subjectdrug screening
dc.subjecthuman
dc.subjecthuman cell
dc.subjectin vitro study
dc.subjectmetastasis
dc.subjectmetastasis inhibition
dc.subjectMTT assay
dc.subjectPi3K/Akt signaling
dc.subjectplant leaf
dc.subjectpriority journal
dc.subjectprotein expression
dc.subjectproton nuclear magnetic resonance
dc.subjectSW1353 cell line
dc.subjectthin layer chromatography
dc.subjecttranswell assay
dc.subjecttumor microenvironment
dc.subjectWestern blotting
dc.subjectwound closure
dc.subjectwound healing assay
dc.subjectcell adhesion
dc.subjectcell motion
dc.subjectcell survival
dc.subjectchemistry
dc.subjectchondrosarcoma
dc.subjectdrug effect
dc.subjectmetabolism
dc.subjectmetastasis
dc.subjectsignal transduction
dc.subjecttumor cell line
dc.subjectCell Adhesion
dc.subjectCell Line, Tumor
dc.subjectCell Movement
dc.subjectCell Proliferation
dc.subjectCell Survival
dc.subjectChondrosarcoma
dc.subjectHumans
dc.subjectMatrix Metalloproteinase 2
dc.subjectMatrix Metalloproteinase 9
dc.subjectMitogen-Activated Protein Kinases
dc.subjectNeoplasm Metastasis
dc.subjectNF-kappa B
dc.subjectOncogene Protein v-akt
dc.subjectPhosphatidylinositol 3-Kinase
dc.subjectSenna Extract
dc.subjectSignal Transduction
dc.subjectTissue Inhibitor of Metalloproteinase-1
dc.subjectTissue Inhibitor of Metalloproteinase-2
dc.titleInhibitory effects on chondrosarcoma cell metastasis by Senna alata extract
dc.typeArticle
dc.rights.holderScopus
dc.identifier.bibliograpycitationBiomedicine and Pharmacotherapy. Vol 137, No. (2021)
dc.identifier.doi10.1016/j.biopha.2021.111337
Appears in Collections:Scopus 1983-2021

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