Involvement of protein phosphatase 2A in interferon-?-2b-induced apoptosis in K562 human chronic myelogenous leukaemia cells

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dc.contributor.authorSaydam, G..
dc.contributor.authorAydin H.H.
dc.contributor.authorSahin F.
dc.contributor.authorSelvi N.
dc.contributor.authorOktem G.
dc.contributor.authorTerzioglu E.
dc.contributor.authorBuyukkececi F.
dc.contributor.authorOmay S.B.
dc.date.accessioned2019-10-27T08:59:39Z
dc.date.available2019-10-27T08:59:39Z
dc.date.issued2003
dc.departmentEge Üniversitesien_US
dc.description.abstractInterferon-alpha (IFN-?)-2b is known to have antiproliferative effects on hematological malignant cells, especially chronic myelogenous leukaemia (CML). However, it can induce cytogenetical remissions in a very small percentage of the patients. Also during interferon therapy, resistance can emerge in the CML clones. K562 is an in vitro model cell line transformed from a Ph positive CML patient. It can be induced to differentiate to granulocytic and/or monocytic lineages with certain molecules. IFN-?-2b generally exerts its effects on CML cells by Janus family kinases (Jak/Stat) pathway, mostly through tyrosine kinase system. However, there is almost no data on the relevance of serine/threonine (Ser/Thr) protein phosphatase (PP) system in the interferon induced signal transduction pathways. In this study, we investigated serine/threonine protein phosphatases in the IFN-?-2b induced K562 cytotoxicity. Trypan blue dye exclusion test and MTT assay were utilised for determining cytotoxicity. IC50 of IFN-?-2b on K562 cells was found to be 600IU/ml. However, no differentiation was determined by analysis of cell surface antigen expressions. Serine/threonine protein phosphatase inhibitors calyculin A (Cal A) and okadaic acid (OKA) augmented the IFN-?-2b induced cytotoxicity. Apoptosis assay by the mono-oligonucleosome detection and acridine orange/propidium iodide dye revealed marked apoptosis underlying cytotoxicity. Phosphatase enzyme assay revealed a gradual increase in protein phosphatase 2A (PP2A) activity during interferon induced cytotoxicity. Conversely, immunoblots showed no change in the expression of PP2A catalytic and regulatory subunits. In conclusion, PP2A plays a role in IFN-?-2b induced apoptosis of K562 cells and should be investigated as a new window furthermore. © 2003 Elsevier Science Ltd. All rights reserved.en_US
dc.identifier.doi10.1016/S0145-2126(02)00347-8en_US
dc.identifier.endpage717en_US
dc.identifier.issn0145-2126
dc.identifier.issue8en_US
dc.identifier.pmid12801529en_US
dc.identifier.scopusqualityN/Aen_US
dc.identifier.startpage709en_US
dc.identifier.urihttps://doi.org/10.1016/S0145-2126(02)00347-8
dc.identifier.urihttps://hdl.handle.net/11454/27870
dc.identifier.volume27en_US
dc.indekslendigikaynakScopusen_US
dc.indekslendigikaynakPubMeden_US
dc.language.isoenen_US
dc.publisherElsevier Ltden_US
dc.relation.ispartofLeukemia Researchen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/closedAccessen_US
dc.subjectApoptosisen_US
dc.subjectInterferon-?-2ben_US
dc.subjectK562 cellsen_US
dc.subjectPP2Aen_US
dc.titleInvolvement of protein phosphatase 2A in interferon-?-2b-induced apoptosis in K562 human chronic myelogenous leukaemia cellsen_US
dc.typeArticleen_US

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