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Article: Histone deacetylase inhibitor-induced cellular apoptosis involves stanniocalcin-1 activation

TitleHistone deacetylase inhibitor-induced cellular apoptosis involves stanniocalcin-1 activation
Authors
Issue Date2008
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yexcr
Citation
Experimental Cell Research, 2008, v. 314 n. 16, p. 2975-2984 How to Cite?
AbstractOur previous studies have demonstrated the involvement of HIF-1 and p53 in the regulation of stanniocalcin-1 (STC1) gene transcription in human cancer cells. In this study, we reported that the treatment of human colon adenoma HT29 cells with a histone deacetylase (HDAC) inhibitor (i.e. trichostatin A, TSA) induced both cellular apoptosis and STC1 expression. The activation of STC1 expression was also observed in other TSA-treated human cancer cells (i.e. SKOV3, CaCo-2, Jurkat and CNE-2 cells). STC1 mRNA was rapidly induced within 4 h in TSA-treated HT29 cells, and was found to be transcriptionally regulated and was independent of new protein synthesis as revealed by ActD and CHX treatment respectively. The induction was correlated with increased cellular levels of acetyl histone H3 and H4 and acetyl NFκB. Chromatin immunoprecipitation (ChIP) assay showed the increased binding of acetyl histone H3 and H4 to STC1 promoter in the TSA-treated cells. A cotreatment of HT29 cells with a NFκB inhibitor (parthenolide) significantly inhibited the TSA-induced cellular levels of acetyl NFκB p65 and abolished the stimulation of STC1 gene expression. ChIP assay also demonstrated that TSA treatment increased while TSA/parthenolide cotreatment decreased NFκB p65 binding to STC1 gene promoter. In the STC1-luciferase promoter construct (1 kb) study, the data implied that the promoter can be activated by TSA treatment. Interestingly, the promoter region contains 2 putative NFκB binding sites. Consistent with the STC1mRNA expression data, TSA/parthenolide cotreatment also significantly inhibited the TSA-induced STC1 promoter-driven luciferase activity. Importantly, TSA-induced apoptotic process was found to be significantly reduced by the silencing of STC1 expression. This is the first study to show that histone hyper-acetylation and the recruitment of activated NFκB stimulated STC1 gene expression. In addition, our results support the notion that STC1 is a pro-apoptotic factor. © 2008 Elsevier Inc. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/183397
ISSN
2015 Impact Factor: 3.378
2015 SCImago Journal Rankings: 1.900
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLaw, AYSen_US
dc.contributor.authorLai, KPen_US
dc.contributor.authorLui, WCen_US
dc.contributor.authorWan, HTen_US
dc.contributor.authorWong, CKCen_US
dc.date.accessioned2013-05-27T07:12:33Z-
dc.date.available2013-05-27T07:12:33Z-
dc.date.issued2008en_US
dc.identifier.citationExperimental Cell Research, 2008, v. 314 n. 16, p. 2975-2984en_US
dc.identifier.issn0014-4827en_US
dc.identifier.urihttp://hdl.handle.net/10722/183397-
dc.description.abstractOur previous studies have demonstrated the involvement of HIF-1 and p53 in the regulation of stanniocalcin-1 (STC1) gene transcription in human cancer cells. In this study, we reported that the treatment of human colon adenoma HT29 cells with a histone deacetylase (HDAC) inhibitor (i.e. trichostatin A, TSA) induced both cellular apoptosis and STC1 expression. The activation of STC1 expression was also observed in other TSA-treated human cancer cells (i.e. SKOV3, CaCo-2, Jurkat and CNE-2 cells). STC1 mRNA was rapidly induced within 4 h in TSA-treated HT29 cells, and was found to be transcriptionally regulated and was independent of new protein synthesis as revealed by ActD and CHX treatment respectively. The induction was correlated with increased cellular levels of acetyl histone H3 and H4 and acetyl NFκB. Chromatin immunoprecipitation (ChIP) assay showed the increased binding of acetyl histone H3 and H4 to STC1 promoter in the TSA-treated cells. A cotreatment of HT29 cells with a NFκB inhibitor (parthenolide) significantly inhibited the TSA-induced cellular levels of acetyl NFκB p65 and abolished the stimulation of STC1 gene expression. ChIP assay also demonstrated that TSA treatment increased while TSA/parthenolide cotreatment decreased NFκB p65 binding to STC1 gene promoter. In the STC1-luciferase promoter construct (1 kb) study, the data implied that the promoter can be activated by TSA treatment. Interestingly, the promoter region contains 2 putative NFκB binding sites. Consistent with the STC1mRNA expression data, TSA/parthenolide cotreatment also significantly inhibited the TSA-induced STC1 promoter-driven luciferase activity. Importantly, TSA-induced apoptotic process was found to be significantly reduced by the silencing of STC1 expression. This is the first study to show that histone hyper-acetylation and the recruitment of activated NFκB stimulated STC1 gene expression. In addition, our results support the notion that STC1 is a pro-apoptotic factor. © 2008 Elsevier Inc. All rights reserved.en_US
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yexcren_US
dc.relation.ispartofExperimental Cell Researchen_US
dc.subject.meshAcetylationen_US
dc.subject.meshApoptosis - Drug Effectsen_US
dc.subject.meshCell Line, Tumoren_US
dc.subject.meshEnzyme Inhibitors - Metabolism - Pharmacologyen_US
dc.subject.meshGene Expression Regulation - Drug Effectsen_US
dc.subject.meshGenes, Reporteren_US
dc.subject.meshGlycoproteins - Genetics - Metabolismen_US
dc.subject.meshHistone Deacetylase Inhibitorsen_US
dc.subject.meshHistone Deacetylases - Metabolismen_US
dc.subject.meshHistones - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshHydroxamic Acids - Metabolism - Pharmacologyen_US
dc.subject.meshRna Interferenceen_US
dc.subject.meshTranscription Factor Rela - Antagonists & Inhibitors - Genetics - Metabolismen_US
dc.subject.meshTranscription, Geneticen_US
dc.titleHistone deacetylase inhibitor-induced cellular apoptosis involves stanniocalcin-1 activationen_US
dc.typeArticleen_US
dc.identifier.emailLai, KP: ballllai@hotmail.comen_US
dc.identifier.authorityLai, KP=rp01753en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/j.yexcr.2008.07.002en_US
dc.identifier.pmid18652825-
dc.identifier.scopuseid_2-s2.0-51649119512en_US
dc.identifier.hkuros223781-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-51649119512&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume314en_US
dc.identifier.issue16en_US
dc.identifier.spage2975en_US
dc.identifier.epage2984en_US
dc.identifier.isiWOS:000259802600007-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLaw, AYS=16175363700en_US
dc.identifier.scopusauthoridLai, KP=7402135707en_US
dc.identifier.scopusauthoridLui, WC=24483760200en_US
dc.identifier.scopusauthoridWan, HT=24483853000en_US
dc.identifier.scopusauthoridWong, CKC=35276549400en_US

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