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dc.contributor.authorÇoker Gürkan, Ajda
dc.contributor.authorArısan, Elif Damla
dc.contributor.authorObakan Yerlikaya, Pınar
dc.contributor.authorAkalın, Kübra
dc.contributor.authorÖzbey, Utku
dc.contributor.authorPalavan Ünsal, Zeynep Narçın
dc.date.accessioned2018-07-13T09:03:06Z
dc.date.available2018-07-13T09:03:06Z
dc.date.issued2015-06
dc.identifier.issn1021-335X
dc.identifier.other1791-2431
dc.identifier.urihttps://doi.org/10.3892/or.2015.3918
dc.identifier.urihttps://hdl.handle.net/11413/2074
dc.description.abstractPurvalanol, a novel cyclin-dependent kinase inhibitor, is referred to as a strong apoptotic inducer which causes cell cycle arrest in various cancer cells such as prostate, breast and colon cancer cell lines. Various physiological and pathological conditions such as glucose starvation, inhibition of protein glycosylation and oxidative stress may cause an accumulation of unfolded proteins in the endoplasmic reticulum (ER), leading to the unfolded protein response (UPR) and autophagy. Lacking proteosomal function on aggregates of unfolded proteins, ER stress may induce autophagic machinery. Autophagy, an evolutionarily conserved process, is characterized by massive degradation of cytosolic contents. In the present study, our aim was to determine the time-dependent, ER-mediated apoptotic and autophagy induction of purvalanol in HCT 116 colon cancer cells. Fifteen micromoles of purvalanol induced a reduction in cell viability by 20 and 35% within 24 and 48 h, respectively. HCT 116 colon cancer cells were exposed to purvalanol, which activated ER stress via upregulation of PERK, IREl alpha gene expression, eIF-2 alpha phosphorylation and ATF-6 cleavage at early time-points in the HCT 116 colon cancer cells. Moreover, we determined that during purvalanol-mediated ER stress, autophagic machinery was also activated prior to apoptotic cell death finalization. Beclin-1 and Atg-5 expression levels were upregulated and LC3 was cleaved after a 6 h purvalanol treatment. Purvalanol induced mitochondrial membrane potential loss, caspase-7 and caspase-3 activation and PARP cleavage following a 48 h treatment. Thus, we conclude that the anticancer effect of purvalanol in HCT 116 cells was due to ER stress-mediated apoptosis; however, purvalanol triggered autophagy, which functions as a cell survival mechanism at early time-points.tr_TR
dc.language.isoen_UStr_TR
dc.publisherSpandidos Publ Ltd, Pob 18179, Athens, 116 10, Greecetr_TR
dc.relationOncology Reportstr_TR
dc.subjectPurvalanoltr_TR
dc.subject Endoplasmic Reticulum stress; tr_TR
dc.subjectAutophagytr_TR
dc.subjectApoptosistr_TR
dc.subjectColon Cancertr_TR
dc.subjectUnfolded protein responsetr_TR
dc.subjectPolyamine catabolic pathwaytr_TR
dc.subjectTranscription factorstr_TR
dc.subjectCarcinoma cellstr_TR
dc.subjectEr stresstr_TR
dc.subjectInhibitorstr_TR
dc.subjectInductiontr_TR
dc.subjectKinasestr_TR
dc.subjectChoptr_TR
dc.subjectCalreticulintr_TR
dc.titlePurvalanol induces endoplasmic reticulum stress-mediated apoptosis and autophagy in a time-dependent manner in HCT116 colon cancer cellstr_TR
dc.typeArticletr_TR
dc.contributor.authorID125860tr_TR
dc.contributor.authorID113920tr_TR
dc.contributor.authorID156421tr_TR
dc.contributor.authorID6125tr_TR
dc.identifier.wos355058700014
dc.identifier.wos355058700014en
dc.identifier.scopus2-s2.0-84928886629
dc.identifier.scopus2-s2.0-84928886629en
dc.identifier.pubmed25901510
dc.identifier.pubmed25901510en


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