Proteomic signature of neuroblastoma cells UKF-NB-4 reveals key role of lysosomal sequestration and the proteasome complex in acquiring chemoresistance to cisplatin

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dc.contributor.authorMerlos Rodrigo, Miguel Ángelcs
dc.contributor.authorMichálková, Hanacs
dc.contributor.authorDe los Rios, Viviancs
dc.contributor.authorCasal Álvarez, José Ignaciocs
dc.contributor.authorEckschlager, Tomášcs
dc.contributor.authorHraběta, Jancs
dc.contributor.authorBelhajová, Mariecs
dc.contributor.authorHeger, Zbyněkcs
dc.contributor.authorAdam, Vojtěchcs
dc.coverage.issue3cs
dc.coverage.volume18cs
dc.date.issued2019-03-25cs
dc.description.abstractCisplatin (CDDP) is a widely used agent in the treatment of neuroblastoma. Unfortunately, the development of acquired chemoresistance limits its clinical use. To gain a detailed understanding of the mechanisms underlying the development of such chemoresistance, we comparatively analyzed established cisplatin-resistant neuroblastoma cell line (UKF-NB-4(CDDP)) and its sensitive counterpart (UKF-NB-4). First, using viability screenings, we confirmed the decreased sensitivity of tested cells to cisplatin and identified a cross-resistance to carboplatin and oxaliplatin. Then, the proteomic signatures were analyzed using nano liquid chromatography with tandem mass spectrometry. Among the proteins responsible for UKF-NB-4(CDDP) chemoresistance, ion channels transport family proteins, ATP-binding cassette superfamily proteins (ATP = adenosine triphosphate), solute carrier-mediated trans-membrane transporters, proteasome complex subunits, and V-ATPases were identified. Moreover, we detected markedly higher proteasome activity in UKF-NB-4(CDDP) cells and a remarkable lysosomal enrichment that can be inhibited by bafilomycin A to sensitize UKF-NB-4(CDDP) to CDDP. Our results indicate that lysosomal sequestration and proteasome activity may be one of the key mechanisms responsible for intrinsic chemoresistance of neuroblastoma to CDDP.en
dc.formattextcs
dc.format.extent1255-1263cs
dc.format.mimetypeapplication/pdfcs
dc.identifier.citationJOURNAL OF PROTEOME RESEARCH. 2019, vol. 18, issue 3, p. 1255-1263.en
dc.identifier.doi10.1021/acs.jproteome.8b00867cs
dc.identifier.issn1535-3893cs
dc.identifier.orcid0000-0002-3915-7270cs
dc.identifier.orcid0000-0002-8527-286Xcs
dc.identifier.other156373cs
dc.identifier.researcheridD-1973-2013cs
dc.identifier.researcheridD-7686-2012cs
dc.identifier.urihttp://hdl.handle.net/11012/195620
dc.language.isoencs
dc.publisherAmerican Chemical Societycs
dc.relation.ispartofJOURNAL OF PROTEOME RESEARCHcs
dc.relation.urihttps://pubs.acs.org/doi/10.1021/acs.jproteome.8b00867cs
dc.rights(C) American Chemical Societycs
dc.rights.accessopenAccesscs
dc.rights.sherpahttp://www.sherpa.ac.uk/romeo/issn/1535-3893/cs
dc.subjectneuroblastomaen
dc.subjectchemoresistanceen
dc.subjectcisplatinen
dc.subjectlysosomesen
dc.subjectproteomicsen
dc.subjectV-ATPasesen
dc.titleProteomic signature of neuroblastoma cells UKF-NB-4 reveals key role of lysosomal sequestration and the proteasome complex in acquiring chemoresistance to cisplatinen
dc.type.driverarticleen
dc.type.statusPeer-revieweden
dc.type.versionacceptedVersionen
sync.item.dbidVAV-156373en
sync.item.dbtypeVAVen
sync.item.insts2025.02.03 15:50:00en
sync.item.modts2025.01.17 16:51:27en
thesis.grantorVysoké učení technické v Brně. Středoevropský technologický institut VUT. Chytré nanonástrojecs
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