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dc.contributor.authorAcebo País, Paloma-
dc.contributor.authorGiner-Sánchez, Daniel-
dc.contributor.authorCalvo, Piedad-
dc.contributor.authorBlanco-Rivero, Amaya-
dc.contributor.authorOrtega, Álvaro D.-
dc.contributor.authorFernández, Pedro L.-
dc.contributor.authorRoncador, Giovanna-
dc.contributor.authorFernández-Malavé, Edgar-
dc.contributor.authorChamorro, Margarita-
dc.contributor.authorCuezva, José M.-
dc.date.accessioned2011-07-13T18:07:44Z-
dc.date.available2011-07-13T18:07:44Z-
dc.date.issued2009-
dc.identifier.citationTranslational Oncology 2 (3): 138–145 (2009)es_ES
dc.identifier.issn1936-5233-
dc.identifier.urihttp://hdl.handle.net/10261/37745-
dc.description.abstractNowadays, cellular bioenergetics has become a central issue of investigation in cancer biology. Recently, the metabolic activity of the cancer cell has been shown to correlate with a proteomic index that informs of the relative mitochondrial activity of the cell. Within this new field of investigation, we report herein the production and characterization of high-affinity monoclonal antibodies against proteins of the “bioenergetic signature” of the cell. The use of recombinant proteins and antibodies against the mitochondrial β-F1-ATPase and Hsp60 proteins and the enzymes of the glycolytic pathway glyceraldehyde-3-phosphate dehydrogenase and pyruvate kinase M2 in quantitative assays provide, for the first time, the actual amount of these proteins in normal and tumor surgical specimens of breast, lung, and esophagus. The application of this methodology affords a straightforward proteomic signature that quantifies the variable energetic demand of human tissues. Furthermore, the results show an unanticipated finding: tumors from different tissues and/or histological types have the same proteomic signature of energetic metabolism. Therefore, the results indicate that cancer abolishes the tissue-specific differences in the bioenergetic phenotype of mitochondria. Overall, the results support that energetic metabolism represents an additional hallmark of the phenotype of the cancer cell and a promising target for the treatment of diverse neoplasias.es_ES
dc.description.sponsorshipNowadays, cellular bioenergetics has become a central issue of investigation in cancer biology. Recently, the metabolic activity of the cancer cell has been shown to correlate with a proteomic index that informs of the relative mitochondrial activity of the cell. Within this new field of investigation, we report herein the production and characterization of high-affinity monoclonal antibodies against proteins of the “bioenergetic signature” of the cell. The use of recombinant proteins and antibodies against the mitochondrial β-F1-ATPase and Hsp60 proteins and the enzymes of the glycolytic pathway glyceraldehyde-3-phosphate dehydrogenase and pyruvate kinase M2 in quantitative assays provide, for the first time, the actual amount of these proteins in normal and tumor surgical specimens of breast, lung, and esophagus. The application of this methodology affords a straightforward proteomic signature that quantifies the variable energetic demand of human tissues. Furthermore, the results show an unanticipated finding: tumors from different tissues and/or histological types have the same proteomic signature of energetic metabolism. Therefore, the results indicate that cancer abolishes the tissue-specific differences in the bioenergetic phenotype of mitochondria. Overall, the results support that energetic metabolism represents an additional hallmark of the phenotype of the cancer cell and a promising target for the treatment of diverse neoplasias.es_ES
dc.language.isoenges_ES
dc.publisherElsevieres_ES
dc.rightsopenAccesses_ES
dc.subjectTumorses_ES
dc.subjectGlycolytic pathwayes_ES
dc.subjectβ-F1-ATPasees_ES
dc.subjecthallmarkes_ES
dc.titleCancer Abolishes the Tissue Type–Specific Differences in the Phenotype of Energetic Metabolismes_ES
dc.typeartículoes_ES
dc.identifier.doi10.1593/tlo.09106-
dc.description.peerreviewedPeer reviewedes_ES
dc.relation.publisherversionhttp://dx.doi.org/10.1593/tlo.09106es_ES
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