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Mass spectrometry‐based characterization of histones in clinical samples: applications, progress, and challenges
In the last 15 years, increasing evidence linking epigenetics to various aspects of cancer biology has prompted the investigation of histone post‐translational modifications (PTMs) and histone variants in the context of clinical samples. The studies performed so far demonstrated the potential of thi...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9291046/ https://www.ncbi.nlm.nih.gov/pubmed/33415821 http://dx.doi.org/10.1111/febs.15707 |
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author | Noberini, Roberta Robusti, Giulia Bonaldi, Tiziana |
author_facet | Noberini, Roberta Robusti, Giulia Bonaldi, Tiziana |
author_sort | Noberini, Roberta |
collection | PubMed |
description | In the last 15 years, increasing evidence linking epigenetics to various aspects of cancer biology has prompted the investigation of histone post‐translational modifications (PTMs) and histone variants in the context of clinical samples. The studies performed so far demonstrated the potential of this type of investigations for the discovery of both potential epigenetic biomarkers for patient stratification and novel epigenetic mechanisms potentially targetable for cancer therapy. Although traditionally the analysis of histones in clinical samples was performed through antibody‐based methods, mass spectrometry (MS) has emerged as a more powerful tool for the unbiased, comprehensive, and quantitative investigation of histone PTMs and variants. MS has been extensively used for the analysis of epigenetic marks in cell lines and animal tissue and, thanks to recent technological advances, is now ready to be applied also to clinical samples. In this review, we will provide an overview on the quantitative MS‐based analysis of histones, their PTMs and their variants in cancer clinical samples, highlighting current achievements and future perspectives for this novel field of research. Among the different MS‐based approaches currently available for histone PTM profiling, we will focus on the ‘bottom‐up’ strategy, namely the analysis of short proteolytic peptides, as it has been already successfully employed for the analysis of clinical samples. |
format | Online Article Text |
id | pubmed-9291046 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-92910462022-07-20 Mass spectrometry‐based characterization of histones in clinical samples: applications, progress, and challenges Noberini, Roberta Robusti, Giulia Bonaldi, Tiziana FEBS J State‐of‐the‐Art Review In the last 15 years, increasing evidence linking epigenetics to various aspects of cancer biology has prompted the investigation of histone post‐translational modifications (PTMs) and histone variants in the context of clinical samples. The studies performed so far demonstrated the potential of this type of investigations for the discovery of both potential epigenetic biomarkers for patient stratification and novel epigenetic mechanisms potentially targetable for cancer therapy. Although traditionally the analysis of histones in clinical samples was performed through antibody‐based methods, mass spectrometry (MS) has emerged as a more powerful tool for the unbiased, comprehensive, and quantitative investigation of histone PTMs and variants. MS has been extensively used for the analysis of epigenetic marks in cell lines and animal tissue and, thanks to recent technological advances, is now ready to be applied also to clinical samples. In this review, we will provide an overview on the quantitative MS‐based analysis of histones, their PTMs and their variants in cancer clinical samples, highlighting current achievements and future perspectives for this novel field of research. Among the different MS‐based approaches currently available for histone PTM profiling, we will focus on the ‘bottom‐up’ strategy, namely the analysis of short proteolytic peptides, as it has been already successfully employed for the analysis of clinical samples. John Wiley and Sons Inc. 2021-01-23 2022-03 /pmc/articles/PMC9291046/ /pubmed/33415821 http://dx.doi.org/10.1111/febs.15707 Text en © 2021 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ (https://creativecommons.org/licenses/by-nc-nd/4.0/) License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made. |
spellingShingle | State‐of‐the‐Art Review Noberini, Roberta Robusti, Giulia Bonaldi, Tiziana Mass spectrometry‐based characterization of histones in clinical samples: applications, progress, and challenges |
title | Mass spectrometry‐based characterization of histones in clinical samples: applications, progress, and challenges |
title_full | Mass spectrometry‐based characterization of histones in clinical samples: applications, progress, and challenges |
title_fullStr | Mass spectrometry‐based characterization of histones in clinical samples: applications, progress, and challenges |
title_full_unstemmed | Mass spectrometry‐based characterization of histones in clinical samples: applications, progress, and challenges |
title_short | Mass spectrometry‐based characterization of histones in clinical samples: applications, progress, and challenges |
title_sort | mass spectrometry‐based characterization of histones in clinical samples: applications, progress, and challenges |
topic | State‐of‐the‐Art Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9291046/ https://www.ncbi.nlm.nih.gov/pubmed/33415821 http://dx.doi.org/10.1111/febs.15707 |
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