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dc.contributor.authorMedina Villaamil, Vanessa
dc.contributor.authorAparicio Gallego, Guadalupe
dc.contributor.authorValladares-Ayerbes, Manuel
dc.contributor.authorSantamarina, Isabel
dc.contributor.authorAntón-Aparicio, Luis M.
dc.date.accessioned2017-09-29T08:01:03Z
dc.date.available2017-09-29T08:01:03Z
dc.date.issued2012-09-01
dc.identifier.citationMedina Villaamil V, Aparicio Gallego G, Valladares-Ayerbes M, Santamarina Caínzos I, Antón Aparicio LM. Multiple biomarker tissue arrays: a computational approach to identifying protein-protein interactions in the EGFR/ERK signalling pathway. J Mol Signal [Internet]. 2012 Sep 1 [acceso 2017 Sep 29];7:14. Disponible en: https://jmolecularsignaling.biomedcentral.com/articles/10.1186/1750-2187-7-14es_ES
dc.identifier.issn1750-2187
dc.identifier.urihttp://hdl.handle.net/2183/19548
dc.description.abstract[Abstract] Background. Many studies have demonstrated genetic and environmental factors that lead to renal cell carcinoma (RCC) and that occur during a protracted period of tumourigenesis. It appears suitable to identify and characterise potential molecular markers that appear during tumourigenesis and that might provide rapid and effective possibilities for the early detection of RCC. EGFR activation induces cell cycle progression, inhibition of apoptosis and angiogenesis, promotion of invasion/metastasis, and other tumour promoting activities. Over-expression of EGFR is thought to play an important role in tumour initiation and progression of RCC because up-regulation of EGFR has been associated with high grade cancers and a worse prognosis. Methods. Characterisation of the protein profile interacting with EGFR was performed using the following: an immunohistochemical (IHC) study of EGFR, a comprehensive computational study of EGFR protein-protein interactions, an analysis correlating the expression levels of EGFR with other significant markers in the tumourigenicity of RCC, and finally, an analysis of the utility of EGFR for prognosis in a cohort of patients with renal cell carcinoma. Results. The cases that showed a higher level of this protein fell within the clear cell histological subtype (p = 0.001). The EGFR significance statistic was found with respect to a worse prognosis. In vivo significant correlations were found with PDGFR-β, Flk-1, Hif1-α, proteins related to differentiation (such as DLL3 and DLL4 ligands), and certain metabolic proteins such as Glut5. In silico significant associations gave us a panel of 32 EGFR-interacting proteins (EIP) using the APID and STRING databases. Conclusions. This work summarises the multifaceted role of EGFR in the pathology of RCC, and it identifies EIPs that could help to provide mechanistic explanations for the different behaviours observed in tumours.es_ES
dc.language.isoenges_ES
dc.publisherBioMed Centrales_ES
dc.relation.urihttp://dx.doi.org/10.1186/1750-2187-7-14es_ES
dc.rightsAtribución 3.0 Españaes_ES
dc.rights.urihttp://creativecommons.org/licenses/by/3.0/es/*
dc.subjectEGFRes_ES
dc.subjectInteracting proteinses_ES
dc.subjectRenal cell carcinomaes_ES
dc.subjectTissue arrayes_ES
dc.titleMultiple biomarker tissue arrays: a computational approach to identifying protein-protein interactions in the EGFR/ERK signalling pathwayes_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
dc.rights.accessinfo:eu-repo/semantics/openAccesses_ES
UDC.journalTitleJournal of Molecular Signalinges_ES
UDC.volume7es_ES


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