2024-03-29T14:27:27Zhttp://repisalud.isciii.es/oai/requestoai:repisalud.isciii.es:20.500.12105/82052022-09-20T07:24:31Zcom_20.500.12105_2174com_20.500.12105_2051com_20.500.12105_2173col_20.500.12105_2175
Repisalud
author
Marrugal, Ángela
author
Ferrer, Irene
author
Pastor, Maria Dolores
author
Ojeda, Laura
author
Quintanal-Villalonga, Alvaro
author
Carnero, Amancio
author
Molina-Pinelo, Sonia
author
Paz Ares, Luis Gonzaga
funder
Comunidad de Madrid
funder
European Regional Development Fund
funder
Fundación Mutua Madrileña
funder
Instituto de Salud Carlos III
funder
Ministerio de Ciencia e Innovación (España)
2019-08-12T09:38:41Z
2019-08-12T09:38:41Z
2019-07-31
Cells. 2019;8(8).
2073-4409
http://hdl.handle.net/20.500.12105/8205
31370342
10.3390/cells8080806
2073-4409
Cells
Heat shock protein 90 (HSP90) is an important chaperone in lung adenocarcinoma, with relevant protein drivers such as EGFR (epidermal growth factor receptor) and EML4-ALK (echinoderm microtubule-associated protein-like protein4 fused to anaplastic lymphoma kinase) depending on it for their correct function, therefore HSP90 inhibitors show promise as potential treatments for lung adenocarcinoma. To study responses to its inhibition, HSP90 was pharmacologically interrupted by geldanamycin and resorcinol derivatives or with combined inhibition of HSP90 plus HSP70 in lung adenocarcinoma cell lines. Two-dimensional electrophoresis was performed to identify proteomic profiles associated with inhibition which will help to understand the biological basis for the responses. HSP90 inhibition resulted in altered protein profiles that differed according the treatment condition studied. Results revealed 254 differentially expressed proteins after treatments, among which, eukaryotic translation initiation factor3 subunit I (eIF3i) and citrate synthase demonstrated their potential role as response biomarkers. The differentially expressed proteins also enabled signalling pathways involved in responses to be identified; these included apoptosis, serine-glycine biosynthesis and tricarboxylic acid cycle. The proteomic profiles identified here contribute to an improved understanding of HSP90 inhibition and open possibilities for the detection of potential response biomarkers which will be essential to maximize treatment efficacy in lung adenocarcinoma.
eng
HSP90 inhibitors
Chaperones
Lung cancer
Proteomic
Impact of Heat Shock Protein 90 Inhibition on the Proteomic Profile of Lung Adenocarcinoma as Measured by Two-Dimensional Electrophoresis Coupled with Mass Spectrometry
journal article
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URL
https://repisalud.isciii.es/bitstream/20.500.12105/8205/1/ImpactofHeatShockProtein_2019.pdf
File
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ImpactofHeatShockProtein_2019.pdf
URL
https://repisalud.isciii.es/bitstream/20.500.12105/8205/7/ImpactofHeatShockProtein_2019.pdf.txt
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MD5
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ImpactofHeatShockProtein_2019.pdf.txt