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Proteomic identification of heat shock induced danger signals in a melanoma cell lysate used in dendritic cell based cancer immunotherapy

Authordc.contributor.authorGonzález, Fermin E. 
Authordc.contributor.authorChernobrovkin, Alexey 
Authordc.contributor.authorPereda, Cristián 
Authordc.contributor.authorGarcía Salum, Tamara 
Authordc.contributor.authorLópez, Mercedes N. 
Authordc.contributor.authorSalazar Onfray, Flavio 
Authordc.contributor.authorZubarev, Roman A. 
Authordc.contributor.authorTittarelli, Andrés 
Admission datedc.date.accessioned2018-07-24T14:23:32Z
Available datedc.date.available2018-07-24T14:23:32Z
Publication datedc.date.issued2018
Cita de ítemdc.identifier.citationJournal of Immunology Research Vol 2018, Article ID 3982942, 15 pageses_ES
Identifierdc.identifier.other10.1155/2018/3982942
Identifierdc.identifier.urihttp://repositorio.uchile.cl/handle/2250/150199
Abstractdc.description.abstractAutologous dendritic cells (DCs) loaded with cancer cell-derived lysates have become a promising tool in cancer immunotherapy. During the last decade, we demonstrated that vaccination of advanced melanoma patients with autologous tumor antigen presenting cells (TAPCells) loaded with an allogeneic heat shock- (HS-) conditioned melanoma cell-derived lysate (called TRIMEL) is able to induce an antitumor immune response associated with a prolonged patient survival. TRIMEL provides not only a broad spectrum of potential melanoma-associated antigens but also danger signals that are crucial in the induction of a committed mature DC phenotype. However, potential changes induced by heat conditioning on the proteome of TRIMEL are still unknown. The identification of newly or differentially expressed proteins under defined stress conditions is relevant for understanding the lysate immunogenicity. Here, we characterized the proteomic profile of TRIMEL in response to HS treatment. A quantitative label-free proteome analysis of over 2800 proteins was performed, with 91 proteins that were found to be regulated by HS treatment: 18 proteins were overexpressed and 73 underexpressed. Additionally, 32 proteins were only identified in the HS-treated TRIMEL and 26 in non HS-conditioned samples. One protein from the overexpressed group and two proteins from the HS-exclusive group were previously described as potential damage-associated molecular patterns (DAMPs). Some of the HS-induced proteins, such as haptoglobin, could be also considered as DAMPs and candidates for further immunological analysis in the establishment of new putative danger signals with immunostimulatory functions.es_ES
Patrocinadordc.description.sponsorshipChilean National Fund for Scientific and Technological Development FONDECYT 11130607 FONDEF ID16I10148 FONDECYT 1171213es_ES
Lenguagedc.language.isoenes_ES
Publisherdc.publisherHindawi Ltda.es_ES
Type of licensedc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile*
Link to Licensedc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/*
Sourcedc.sourceJournal of Immunology Researches_ES
Títulodc.titleProteomic identification of heat shock induced danger signals in a melanoma cell lysate used in dendritic cell based cancer immunotherapyes_ES
Document typedc.typeArtículo de revistaes_ES
Catalogueruchile.catalogadortjnes_ES
Indexationuchile.indexArtículo de publicación ISIes_ES


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Attribution-NonCommercial-NoDerivs 3.0 Chile
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 3.0 Chile