Rapid proteomic analysis for solid tumors reveals LSD1 as a drug target in an end-stage cancer patient
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Rapid proteomic analysis for solid tumors reveals LSD1 as a drug target in an end-stage cancer patient. / 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.
In: Molecular Oncology, Vol. 12, No. 8, 2018, p. 1296-1307.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Rapid proteomic analysis for solid tumors reveals LSD1 as a drug target in an end-stage cancer patient
AU - Doll, Sophia
AU - Kriegmair, Maximilian C.
AU - Santos, Alberto
AU - Wierer, Michael
AU - Coscia, Fabian
AU - Neil, Helen Michele
AU - Porubsky, Stefan
AU - Geyer, Philipp E.
AU - Mund, Andreas
AU - Nuhn, Philipp
AU - Mann, Matthias
N1 - © 2018 The Authors. Published by FEBS Press and John Wiley & Sons Ltd.
PY - 2018
Y1 - 2018
N2 - 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.
AB - 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.
KW - case study
KW - clinical proteomics
KW - epigenetics
KW - mass spectrometry
KW - urachal carcinoma
U2 - 10.1002/1878-0261.12326
DO - 10.1002/1878-0261.12326
M3 - Journal article
C2 - 29901861
VL - 12
SP - 1296
EP - 1307
JO - Molecular Oncology
JF - Molecular Oncology
SN - 1574-7891
IS - 8
ER -
ID: 198265634