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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| Hauptverfasser: | , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
14 June 2018
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| In: |
Molecular oncology
Year: 2018, Jahrgang: 12, Heft: 8, Pages: 1296-1307 |
| ISSN: | 1878-0261 |
| DOI: | 10.1002/1878-0261.12326 |
| Online-Zugang: | Verlag, Volltext: https://doi.org/10.1002/1878-0261.12326 Verlag, Volltext: https://febs.onlinelibrary.wiley.com/doi/abs/10.1002/1878-0261.12326 
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| Verfasserangaben: | Sophia Doll, Maximilian C. Kriegmair, Alberto Santos, Michael Wierer, Fabian Coscia, Helen Michele Neil, Stefan Porubsky, Philipp E. Geyer, Andreas Mund, Philipp Nuhn and Matthias Mann |
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| 520 | |a 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. | ||
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