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Clinicopathologic significance of protein lysine methyltransferases in cancer
Protein lysine methyltransferases (PKMTs) constitute a large family of approximately 50 chromatin modifiers that mono-, di- and/or tri-methylate lysine residues on histone and non-histone substrates. With the advent of The Cancer Genome Atlas, it became apparent that this family of chromatin modifie...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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BioMed Central
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7557092/ https://www.ncbi.nlm.nih.gov/pubmed/33050946 http://dx.doi.org/10.1186/s13148-020-00897-3 |
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author | Vougiouklakis, Theodore Bernard, Benjamin J. Nigam, Nupur Burkitt, Kyunghee Nakamura, Yusuke Saloura, Vassiliki |
author_facet | Vougiouklakis, Theodore Bernard, Benjamin J. Nigam, Nupur Burkitt, Kyunghee Nakamura, Yusuke Saloura, Vassiliki |
author_sort | Vougiouklakis, Theodore |
collection | PubMed |
description | Protein lysine methyltransferases (PKMTs) constitute a large family of approximately 50 chromatin modifiers that mono-, di- and/or tri-methylate lysine residues on histone and non-histone substrates. With the advent of The Cancer Genome Atlas, it became apparent that this family of chromatin modifiers harbors frequent genetic and expression alterations in multiple types of cancer. In this regard, past and ongoing preclinical studies have provided insight into the mechanisms of action of some of these enzymes, laying the ground for the ongoing development of PKMT inhibitors as novel anticancer therapeutics. The purpose of this review is to summarize existing data obtained by different research groups through immunohistochemical analysis of the protein expression levels of PKMTs, and their respective clinicopathologic associations. We focused on studies that used immunohistochemistry to associate protein expression levels of specific PKMTs, as well as several established histone methylation marks, with clinicopathologic features and survival outcomes in various cancer types. We also review ongoing clinical trials of PKMT inhibitors in cancer treatment. This review underscores the clinical relevance and potential of targeting the family of PKMT enzymes as the next generation of cancer therapy. |
format | Online Article Text |
id | pubmed-7557092 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-75570922020-10-15 Clinicopathologic significance of protein lysine methyltransferases in cancer Vougiouklakis, Theodore Bernard, Benjamin J. Nigam, Nupur Burkitt, Kyunghee Nakamura, Yusuke Saloura, Vassiliki Clin Epigenetics Review Protein lysine methyltransferases (PKMTs) constitute a large family of approximately 50 chromatin modifiers that mono-, di- and/or tri-methylate lysine residues on histone and non-histone substrates. With the advent of The Cancer Genome Atlas, it became apparent that this family of chromatin modifiers harbors frequent genetic and expression alterations in multiple types of cancer. In this regard, past and ongoing preclinical studies have provided insight into the mechanisms of action of some of these enzymes, laying the ground for the ongoing development of PKMT inhibitors as novel anticancer therapeutics. The purpose of this review is to summarize existing data obtained by different research groups through immunohistochemical analysis of the protein expression levels of PKMTs, and their respective clinicopathologic associations. We focused on studies that used immunohistochemistry to associate protein expression levels of specific PKMTs, as well as several established histone methylation marks, with clinicopathologic features and survival outcomes in various cancer types. We also review ongoing clinical trials of PKMT inhibitors in cancer treatment. This review underscores the clinical relevance and potential of targeting the family of PKMT enzymes as the next generation of cancer therapy. BioMed Central 2020-10-13 /pmc/articles/PMC7557092/ /pubmed/33050946 http://dx.doi.org/10.1186/s13148-020-00897-3 Text en © The Author(s) 2020 Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data. |
spellingShingle | Review Vougiouklakis, Theodore Bernard, Benjamin J. Nigam, Nupur Burkitt, Kyunghee Nakamura, Yusuke Saloura, Vassiliki Clinicopathologic significance of protein lysine methyltransferases in cancer |
title | Clinicopathologic significance of protein lysine methyltransferases in cancer |
title_full | Clinicopathologic significance of protein lysine methyltransferases in cancer |
title_fullStr | Clinicopathologic significance of protein lysine methyltransferases in cancer |
title_full_unstemmed | Clinicopathologic significance of protein lysine methyltransferases in cancer |
title_short | Clinicopathologic significance of protein lysine methyltransferases in cancer |
title_sort | clinicopathologic significance of protein lysine methyltransferases in cancer |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7557092/ https://www.ncbi.nlm.nih.gov/pubmed/33050946 http://dx.doi.org/10.1186/s13148-020-00897-3 |
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