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SILAC-based quantitative proteomics and microscopy analysis of cancer cells treated with the N-glycolyl GM3-specific anti-tumor antibody 14F7

dc.contributor.authorBousquet P.A
dc.contributor.authorManna D
dc.contributor.authorSandvik J.A
dc.contributor.authorArntzen M.Ø
dc.contributor.authorMoreno E
dc.contributor.authorSandvig K
dc.contributor.authorKrengel U.
dc.date.accessioned2023-10-24T19:26:05Z
dc.date.available2023-10-24T19:26:05Z
dc.date.created2022
dc.identifier.issn16643224
dc.identifier.urihttp://hdl.handle.net/11407/8116
dc.description.abstractCancer immunotherapy represents a promising approach to specifically target and treat cancer. The most common mechanisms by which monoclonal antibodies kill cells include antibody-dependent cell-mediated cytotoxicity, complement-dependent cytotoxicity and apoptosis, but also other mechanisms have been described. 14F7 is an antibody raised against the tumor-associated antigen NeuGc GM3, which was previously reported to kill cancer cells without inducing apoptotic pathways. The antibody was reported to induce giant membrane lesions in tumor cells, with apparent changes in the cytoskeleton. Here, we investigated the effect of humanized 14F7 on HeLa cells using stable isotope labeling with amino acids in cell culture (SILAC) in combination with LC-MS and live cell imaging. 14F7 did not kill the HeLa cells, however, it caused altered protein expression (MS data are available via ProteomeXchange with identifier PXD024320). Several cytoskeletal and nucleic-acid binding proteins were found to be strongly down-regulated in response to antibody treatment, suggesting how 14F7 may induce membrane lesions in cells that contain higher amounts of NeuGc GM3. The altered expression profile identified in this study thus contributes to an improved understanding of the unusual killing mechanism of 14F7. Copyright © 2022 Bousquet, Manna, Sandvik, Arntzen, Moreno, Sandvig and Krengel.eng
dc.language.isoeng
dc.publisherFrontiers Media S.A.
dc.relation.isversionofhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85142428827&doi=10.3389%2ffimmu.2022.994790&partnerID=40&md5=d7e5844dbe6a67c6bd234f87bb3c00bf
dc.sourceFront. Immunol.
dc.sourceFrontiers in Immunologyeng
dc.subject14F7eng
dc.subjectcytoskeletoneng
dc.subjectGangliosideeng
dc.subjectGlycosphingolipideng
dc.subjectImmunotherapyeng
dc.subjectNeuGc GM3/Neu5Gc GM3eng
dc.subjectSILACeng
dc.subjectTranscription factorseng
dc.titleSILAC-based quantitative proteomics and microscopy analysis of cancer cells treated with the N-glycolyl GM3-specific anti-tumor antibody 14F7eng
dc.typeArticle
dc.rights.accessrightsinfo:eu-repo/semantics/restrictedAccess
dc.publisher.programCiencias Básicasspa
dc.type.spaArtículo
dc.identifier.doi10.3389/fimmu.2022.994790
dc.relation.citationvolume13
dc.publisher.facultyFacultad de Ciencias Básicasspa
dc.affiliationBousquet, P.A., Department of Chemistry, University of Oslo, Oslo, Norway
dc.affiliationManna, D., Department of Chemistry, University of Oslo, Oslo, Norway
dc.affiliationSandvik, J.A., Department of Physics, University of Oslo, Oslo, Norway
dc.affiliationArntzen, M.Ø., Department of Biosciences, University of Oslo, Oslo, Norway
dc.affiliationMoreno, E., Facultad de Ciencias Básicas, Universidad de Medellín, Medellín, Colombia
dc.affiliationSandvig, K., Department of Biosciences, University of Oslo, Oslo, Norway, Department of Molecular Cell Biology, Institute for Cancer Research, The Norwegian Radium Hospital, Oslo, Norway, Centre for Cancer Cell Reprogramming, Faculty of Medicine, University of Oslo, Oslo, Norway
dc.affiliationKrengel, U., Department of Chemistry, University of Oslo, Oslo, Norway
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