Rapid proteomic analysis for solid tumors reveals LSD1 as a drug target in an end-stage cancer patient
Autor/innen
- S. Doll
- M.C. Kriegmair
- A. Santos
- M. Wierer
- F. Coscia
- H.M. Neil
- S. Porubsky
- P.E. Geyer
- A. Mund
- P. Nuhn
- M. Mann
Journal
- Molecular Oncology
Quellenangabe
- Mol Oncol 12 (8): 1296-1307
Zusammenfassung
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.