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Histone citrullination: a new target for tumors
As the main protein components of chromatin, histones play central roles in gene regulation as spools of winding DNA. Histones are subject to various modifications, including phosphorylation, acetylation, glycosylation, methylation, ubiquitination and citrullination, which affect gene transcription....
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8192683/ https://www.ncbi.nlm.nih.gov/pubmed/34116679 http://dx.doi.org/10.1186/s12943-021-01373-z |
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author | Zhu, Dongwei Zhang, Yue Wang, Shengjun |
author_facet | Zhu, Dongwei Zhang, Yue Wang, Shengjun |
author_sort | Zhu, Dongwei |
collection | PubMed |
description | As the main protein components of chromatin, histones play central roles in gene regulation as spools of winding DNA. Histones are subject to various modifications, including phosphorylation, acetylation, glycosylation, methylation, ubiquitination and citrullination, which affect gene transcription. Histone citrullination, a posttranscriptional modification catalyzed by peptidyl arginine deiminase (PAD) enzymes, is involved in human carcinogenesis. In this study, we highlighted the functions of histone citrullination in physiological regulation and tumors. Additionally, because histone citrullination involves forming neutrophil extracellular traps (NETs), the relationship between NETs and tumors was illustrated. Finally, the clinical application of histone citrullination and PAD inhibitors was discussed. |
format | Online Article Text |
id | pubmed-8192683 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-81926832021-06-11 Histone citrullination: a new target for tumors Zhu, Dongwei Zhang, Yue Wang, Shengjun Mol Cancer Review As the main protein components of chromatin, histones play central roles in gene regulation as spools of winding DNA. Histones are subject to various modifications, including phosphorylation, acetylation, glycosylation, methylation, ubiquitination and citrullination, which affect gene transcription. Histone citrullination, a posttranscriptional modification catalyzed by peptidyl arginine deiminase (PAD) enzymes, is involved in human carcinogenesis. In this study, we highlighted the functions of histone citrullination in physiological regulation and tumors. Additionally, because histone citrullination involves forming neutrophil extracellular traps (NETs), the relationship between NETs and tumors was illustrated. Finally, the clinical application of histone citrullination and PAD inhibitors was discussed. BioMed Central 2021-06-11 /pmc/articles/PMC8192683/ /pubmed/34116679 http://dx.doi.org/10.1186/s12943-021-01373-z Text en © The Author(s) 2021 https://creativecommons.org/licenses/by/4.0/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/ (https://creativecommons.org/licenses/by/4.0/) . The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/ (https://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 Zhu, Dongwei Zhang, Yue Wang, Shengjun Histone citrullination: a new target for tumors |
title | Histone citrullination: a new target for tumors |
title_full | Histone citrullination: a new target for tumors |
title_fullStr | Histone citrullination: a new target for tumors |
title_full_unstemmed | Histone citrullination: a new target for tumors |
title_short | Histone citrullination: a new target for tumors |
title_sort | histone citrullination: a new target for tumors |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8192683/ https://www.ncbi.nlm.nih.gov/pubmed/34116679 http://dx.doi.org/10.1186/s12943-021-01373-z |
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