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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...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6068348/ https://www.ncbi.nlm.nih.gov/pubmed/29901861 http://dx.doi.org/10.1002/1878-0261.12326 |
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author | 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 |
author_facet | 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 |
author_sort | Doll, Sophia |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-6068348 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-60683482018-08-03 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 Mol Oncol Research Articles 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. John Wiley and Sons Inc. 2018-06-14 2018-08 /pmc/articles/PMC6068348/ /pubmed/29901861 http://dx.doi.org/10.1002/1878-0261.12326 Text en © 2018 The Authors. Published by FEBS Press and John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Articles 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 Rapid proteomic analysis for solid tumors reveals LSD1 as a drug target in an end‐stage cancer patient |
title | Rapid proteomic analysis for solid tumors reveals LSD1 as a drug target in an end‐stage cancer patient |
title_full | Rapid proteomic analysis for solid tumors reveals LSD1 as a drug target in an end‐stage cancer patient |
title_fullStr | Rapid proteomic analysis for solid tumors reveals LSD1 as a drug target in an end‐stage cancer patient |
title_full_unstemmed | Rapid proteomic analysis for solid tumors reveals LSD1 as a drug target in an end‐stage cancer patient |
title_short | Rapid proteomic analysis for solid tumors reveals LSD1 as a drug target in an end‐stage cancer patient |
title_sort | rapid proteomic analysis for solid tumors reveals lsd1 as a drug target in an end‐stage cancer patient |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6068348/ https://www.ncbi.nlm.nih.gov/pubmed/29901861 http://dx.doi.org/10.1002/1878-0261.12326 |
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