Open AccessRapid proteomic analysis for solid tumors reveals LSD 1 as a drug target in an end‐stage cancer patient
Author(s) -
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
Publication year - 2018
Publication title -
molecular oncology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.332
H-Index - 88
eISSN - 1878-0261
pISSN - 1574-7891
DOI - 10.1002/1878-0261.12326
Subject(s) - proteomics , cancer , demethylase , cancer research , quantitative proteomics , regulator , computational biology , epigenetics , biology , bioinformatics , medicine , biochemistry , gene
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 ( LSD 1/ KDM 1A). LSD 1 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.