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dc.contributor.authorCrul, Tim
dc.contributor.authorCsoboz, Balint
dc.contributor.authorGombos, Imre
dc.contributor.authorMarton, Annamaria
dc.contributor.authorPeter, Maria
dc.contributor.authorBalogh, Gabor
dc.contributor.authorVizler, Csaba
dc.contributor.authorSzente, Lajos
dc.contributor.authorVigh, Laszlo
dc.date.accessioned2021-01-07T14:19:02Z
dc.date.available2021-01-07T14:19:02Z
dc.date.issued2020-04-12
dc.description.abstractThe heat shock response (HSR) regulates induction of stress/heat shock proteins (HSPs) to preserve proteostasis during cellular stress. Earlier, our group established that the plasma membrane (PM) acts as a sensor and regulator of HSR through changes in its microdomain organization. PM microdomains such as lipid rafts, dynamic nanoscale assemblies enriched in cholesterol and sphingomyelin, and caveolae, cholesterol-rich PM invaginations, constitute clustering platforms for proteins functional in signaling cascades. Here, we aimed to compare the effect of cyclodextrin (MβCD)- and nystatin-induced cholesterol modulations on stress-activated expression of the representative HSPs, HSP70, and HSP25 in mouse B16-F10 melanoma cells. Depletion of cholesterol levels with MβCD impaired the heat-inducibility of both HSP70 and HSP25. Sequestration of cholesterol with nystatin impaired the heat-inducibility of HSP25 but not of HSP70. Imaging fluorescent correlation spectroscopy marked a modulated lateral diffusion constant of fluorescently labelled cholesterol in PM during cholesterol deprived conditions. Lipidomics analysis upon MβCD treatment revealed, next to cholesterol reductions, decreased lysophosphatidylcholine and phosphatidic acid levels. These data not only highlight the involvement of PM integrity in HSR but also suggest that altered dynamics of specific cholesterol pools could represent a mechanism to fine tune HSP expression.en_US
dc.identifier.citationCrul, Csoboz, Gombos, Marton, Peter, Balogh, Vizler, Szente, Vigh. Modulation of Plasma Membrane Composition and Microdomain Organization Impairs Heat Shock Protein Expression in B16-F10 Mouse Melanoma Cells. Cells. 2020;9(4):1-14en_US
dc.identifier.cristinIDFRIDAID 1858302
dc.identifier.doi10.3390/cells9040951
dc.identifier.issn2073-4409
dc.identifier.urihttps://hdl.handle.net/10037/20200
dc.language.isoengen_US
dc.publisherMDPIen_US
dc.relation.journalCells
dc.rights.accessRightsopenAccessen_US
dc.rights.holderCopyright 2020 The Author(s)en_US
dc.subjectVDP::Medical disciplines: 700::Basic medical, dental and veterinary science disciplines: 710en_US
dc.subjectVDP::Medisinske Fag: 700::Basale medisinske, odontologiske og veterinærmedisinske fag: 710en_US
dc.titleModulation of Plasma Membrane Composition and Microdomain Organization Impairs Heat Shock Protein Expression in B16-F10 Mouse Melanoma Cellsen_US
dc.type.versionpublishedVersionen_US
dc.typeJournal articleen_US
dc.typeTidsskriftartikkelen_US
dc.typePeer revieweden_US


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