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Rapid proteomic analysis for solid tumors reveals LSD1 as a drug target in an end‐stage cancer patient

Recent advances in mass spectrometry (MS)‐based technologies are now set to transform translational cancer proteomics from an idea to a practice. Here, we present a robust proteomic workflow for the analysis of clinically relevant human cancer tissues that allows quantitation of thousands of tumor p...

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Detalles Bibliográficos
Autores principales: Doll, Sophia, Kriegmair, Maximilian C., Santos, Alberto, Wierer, Michael, Coscia, Fabian, Neil, Helen Michele, Porubsky, Stefan, Geyer, Philipp E., Mund, Andreas, Nuhn, Philipp, Mann, Matthias
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6068348/
https://www.ncbi.nlm.nih.gov/pubmed/29901861
http://dx.doi.org/10.1002/1878-0261.12326
Descripción
Sumario:Recent advances in mass spectrometry (MS)‐based technologies are now set to transform translational cancer proteomics from an idea to a practice. Here, we present a robust proteomic workflow for the analysis of clinically relevant human cancer tissues that allows quantitation of thousands of tumor proteins in several hours of measuring time and a total turnaround of a few days. We applied it to a chemorefractory metastatic case of the extremely rare urachal carcinoma. Quantitative comparison of lung metastases and surrounding tissue revealed several significantly upregulated proteins, among them lysine‐specific histone demethylase 1 (LSD1/KDM1A). LSD1 is an epigenetic regulator and the target of active development efforts in oncology. Thus, clinical cancer proteomics can rapidly and efficiently identify actionable therapeutic options. While currently described for a single case study, we envision that it can be applied broadly to other patients in a similar condition.