Cucurbitacin B suppresses the transactivation activity of RelA/p65

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dc.contributor.authorH R Jin-
dc.contributor.authorX Jin-
dc.contributor.authorN T Dat-
dc.contributor.authorJung Joon Lee-
dc.date.accessioned2017-04-19T09:22:55Z-
dc.date.available2017-04-19T09:22:55Z-
dc.date.issued2011-
dc.identifier.issn0730-2312-
dc.identifier.uri10.1002/jcb.23078ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/10117-
dc.description.abstractCucurbitacin B, a natural triterpenoid is well-known for its strong anticancer activity, and recent studies showed that the compound inhibits JAK/STAT3 pathway. In this study, we demonstrate for the first time that cucurbitacin B is also a potent inhibitor of NF-κB activation. Our results showed that cucurbitacin B inhibited TNF-α-induced expression of NF-κB reporter gene and NF-κB target genes in a dose-dependent manner, however, it did not prevent either stimuli-induced degradation of IκBα or nuclear translocation and DNA-binding activity of NF-κB. On the other hand, cucurbitacin B dose-dependently suppressed not only NF-κB activation induced by overexpression of RelA/p65 but also transactivation activity of RelA/p65 subunit of NF-κB. Consistently, treatment of HeLa cells with the compound significantly suppressed TNF-α-induced activation of Akt and phosphorylation of Ser536 in RelA/p65, which is required for transactivation activity. Consequently, cucurbitacin B inhibited TNF-α-induced expression of NF-κB-dependent anti-apoptotic proteins such as c-IAP1, c-IAP2, XIAP, TRAF1, and TRAF2 and sensitized TNF-α-induced cell death. Taken together, our results demonstrated that cucurbitacin B could be served as a valuable candidate for the intervention of NF-κB-dependent pathological condition such as cancer.-
dc.publisherWiley-
dc.titleCucurbitacin B suppresses the transactivation activity of RelA/p65-
dc.title.alternativeCucurbitacin B suppresses the transactivation activity of RelA/p65-
dc.typeArticle-
dc.citation.titleJournal of Cellular Biochemistry-
dc.citation.number6-
dc.citation.endPage1650-
dc.citation.startPage1643-
dc.citation.volume112-
dc.contributor.affiliatedAuthorJung Joon Lee-
dc.contributor.alternativeNameJin-
dc.contributor.alternativeNameJin-
dc.contributor.alternativeNameDat-
dc.contributor.alternativeName이정준-
dc.identifier.bibliographicCitationJournal of Cellular Biochemistry, vol. 112, no. 6, pp. 1643-1650-
dc.identifier.doi10.1002/jcb.23078-
dc.subject.keywordAKT-
dc.subject.keywordanti-apoptosis-
dc.subject.keywordcucurbitacin B-
dc.subject.keywordNF-κB-
dc.subject.keywordRELA/p65-
dc.subject.keywordtransactivation-
dc.subject.localAKT-
dc.subject.localAkt-
dc.subject.localanti-apoptosis-
dc.subject.localantiapoptosis-
dc.subject.localAnti-apoptosis-
dc.subject.localcucurbitacin B-
dc.subject.localNuclear factor-kappa B-
dc.subject.localnuclear factor κB-
dc.subject.localNf-κb-
dc.subject.localNF-kB-
dc.subject.localnuclear factor kappa B-
dc.subject.localNF-κB (nuclear factor kappa-B)-
dc.subject.localNF-kappaB-
dc.subject.localNuclear factor-κb-
dc.subject.localNF-κ B-
dc.subject.localNF-κB-
dc.subject.localNF-kappa B-
dc.subject.localNuclear factor κB (NF-κB)-
dc.subject.localNuclear factor κB-
dc.subject.localNFκB-
dc.subject.localNf-κB-
dc.subject.localNuclear factor-κB-
dc.subject.localnuclear factorκB-
dc.subject.localNuclear factor (NF)-κB-
dc.subject.localNuclear factor kappa B-
dc.subject.localnuclear factor-κB-
dc.subject.localNF-ΚB-
dc.subject.localNuclear factor-kappa B (NF-κB)-
dc.subject.localNuclear factor-kappaB-
dc.subject.localnuclear factor-kappaB-
dc.subject.localnuclear factor-kappaB (NF-κB)-
dc.subject.localNFkappaB-
dc.subject.localNuclear factor kappaB-
dc.subject.localRELA/p65-
dc.subject.localRelA/p65-
dc.subject.localTransactivation-
dc.subject.localtransactivation-
dc.description.journalClassY-
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