Abstract
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.
Original language | English |
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Journal | Molecular Oncology |
Volume | 12 |
Issue number | 8 |
Pages (from-to) | 1296-1307 |
Number of pages | 12 |
ISSN | 1574-7891 |
DOIs | |
Publication status | Published - 2018 |
Keywords
- case study
- clinical proteomics
- epigenetics
- mass spectrometry
- urachal carcinoma