S100A6 (calcyclin) enhances the sensitivity to apoptosis via the upregulation of caspase-3 activity in Hep3B cells

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dc.contributor.authorJ H Joo-
dc.contributor.authorS Y Yoon-
dc.contributor.authorJ H Kim-
dc.contributor.authorS G Paik-
dc.contributor.authorSung Ran Min-
dc.contributor.authorJ S Lim-
dc.contributor.authorIn Seong Choe-
dc.contributor.authorIn Pyo Choi-
dc.contributor.authorJae Wha Kim-
dc.date.accessioned2017-04-19T09:09:43Z-
dc.date.available2017-04-19T09:09:43Z-
dc.date.issued2008-
dc.identifier.issn0730-2312-
dc.identifier.uri10.1002/jcb.21496ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/8348-
dc.description.abstractS100A6 (calcyclin) is a small calcium-binding protein which has been implicated in several cellular processes such as cell cycle progression, cytoskeleton rearrangement, and exocytosis. Also the upregulation of S100A6 has been reported in a variety of tumors and linked to metastasis. However, exact intracellular roles of S100A6 related with apoptosis have not been clarified yet. Here we demonstrated that the upregulation of S100A6 enhances the cell death rate compared to the control under the apoptotic conditions. In exogenously S100A6 induced Hep3B cells, cell viability was significantly decreased compared with mock and S100A6-knockdown cells under calcium ionophore A23187 treatment. The exogenously introduced S100A6 significantly affected the caspase-3-like activity in programmed cell death through the enhanced caspase-3 expression, which was verified by promoter assay in wild or mutant S100A6-transfected Hep3B cells. Next, the promoter activity of caspase-3 was increased by 2.5-folds in wild-type S100A6-transfected cells compared to mutant 2 (E67K, mutant of EF-hand motif) or control. Our results suggest that S100A6 might be involved in the processing of apoptosis by modulating the transcriptional regulation of caspase-3.-
dc.publisherWiley-
dc.titleS100A6 (calcyclin) enhances the sensitivity to apoptosis via the upregulation of caspase-3 activity in Hep3B cells-
dc.title.alternativeS100A6 (calcyclin) enhances the sensitivity to apoptosis via the upregulation of caspase-3 activity in Hep3B cells-
dc.typeArticle-
dc.citation.titleJournal of Cellular Biochemistry-
dc.citation.number4-
dc.citation.endPage1197-
dc.citation.startPage1183-
dc.citation.volume103-
dc.contributor.affiliatedAuthorSung Ran Min-
dc.contributor.affiliatedAuthorIn Seong Choe-
dc.contributor.affiliatedAuthorIn Pyo Choi-
dc.contributor.affiliatedAuthorJae Wha Kim-
dc.contributor.alternativeName주종혁-
dc.contributor.alternativeName윤선영-
dc.contributor.alternativeName김주헌-
dc.contributor.alternativeName백상기-
dc.contributor.alternativeName민성란-
dc.contributor.alternativeName임종석-
dc.contributor.alternativeName최인성-
dc.contributor.alternativeName최인표-
dc.contributor.alternativeName김재화-
dc.identifier.bibliographicCitationJournal of Cellular Biochemistry, vol. 103, no. 4, pp. 1183-1197-
dc.identifier.doi10.1002/jcb.21496-
dc.subject.keywordA23187-
dc.subject.keywordapoptosis-
dc.subject.keywordcaspase-3-
dc.subject.keywordEF-hand-
dc.subject.keywordHep3B-
dc.subject.keywordS100A6-
dc.subject.localA23187-
dc.subject.localApoptosis-
dc.subject.localapoptosis-
dc.subject.localCaspase 3-
dc.subject.localCaspase-3-
dc.subject.localcaspase-3-
dc.subject.localEF-hand-
dc.subject.localHep3B-
dc.subject.localS100A6-
dc.description.journalClassY-
Appears in Collections:
Division of Research on National Challenges > Plant Systems Engineering Research > 1. Journal Articles
Division of Biomedical Research > Immunotherapy Research Center > 1. Journal Articles
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