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Wild-type and mutated IDH1/2 enzymes and therapy responses
Isocitrate dehydrogenase 1 and 2 (IDH1/2) are key enzymes in cellular metabolism, epigenetic regulation, redox states, and DNA repair. IDH1/2 mutations are causal in the development and/or progression of various types of cancer due to supraphysiological production of d-2-hydroxyglutarate. In various...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5895605/ https://www.ncbi.nlm.nih.gov/pubmed/29367755 http://dx.doi.org/10.1038/s41388-017-0077-z |
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author | Molenaar, Remco J. Maciejewski, Jaroslaw P. Wilmink, Johanna W. van Noorden, Cornelis J. F. |
author_facet | Molenaar, Remco J. Maciejewski, Jaroslaw P. Wilmink, Johanna W. van Noorden, Cornelis J. F. |
author_sort | Molenaar, Remco J. |
collection | PubMed |
description | Isocitrate dehydrogenase 1 and 2 (IDH1/2) are key enzymes in cellular metabolism, epigenetic regulation, redox states, and DNA repair. IDH1/2 mutations are causal in the development and/or progression of various types of cancer due to supraphysiological production of d-2-hydroxyglutarate. In various tumor types, IDH1/2-mutated cancers predict for improved responses to treatment with irradiation or chemotherapy. The present review discusses the molecular basis of the sensitivity of IDH1/2-mutated cancers with respect to the function of mutated IDH1/2 in cellular processes and their interactions with novel IDH1/2-mutant inhibitors. Finally, lessons learned from IDH1/2 mutations for future clinical applications in IDH1/2 wild-type cancers are discussed. |
format | Online Article Text |
id | pubmed-5895605 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-58956052018-04-13 Wild-type and mutated IDH1/2 enzymes and therapy responses Molenaar, Remco J. Maciejewski, Jaroslaw P. Wilmink, Johanna W. van Noorden, Cornelis J. F. Oncogene Review Article Isocitrate dehydrogenase 1 and 2 (IDH1/2) are key enzymes in cellular metabolism, epigenetic regulation, redox states, and DNA repair. IDH1/2 mutations are causal in the development and/or progression of various types of cancer due to supraphysiological production of d-2-hydroxyglutarate. In various tumor types, IDH1/2-mutated cancers predict for improved responses to treatment with irradiation or chemotherapy. The present review discusses the molecular basis of the sensitivity of IDH1/2-mutated cancers with respect to the function of mutated IDH1/2 in cellular processes and their interactions with novel IDH1/2-mutant inhibitors. Finally, lessons learned from IDH1/2 mutations for future clinical applications in IDH1/2 wild-type cancers are discussed. Nature Publishing Group UK 2018-01-25 2018 /pmc/articles/PMC5895605/ /pubmed/29367755 http://dx.doi.org/10.1038/s41388-017-0077-z Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License, which permits any non-commercial 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 license, and indicate if changes were made. If you remix, transform, or build upon this article or a part thereof, you must distribute your contributions under the same license as the original. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license 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 license, visit http://creativecommons.org/licenses/by-nc-sa/4.0/. |
spellingShingle | Review Article Molenaar, Remco J. Maciejewski, Jaroslaw P. Wilmink, Johanna W. van Noorden, Cornelis J. F. Wild-type and mutated IDH1/2 enzymes and therapy responses |
title | Wild-type and mutated IDH1/2 enzymes and therapy responses |
title_full | Wild-type and mutated IDH1/2 enzymes and therapy responses |
title_fullStr | Wild-type and mutated IDH1/2 enzymes and therapy responses |
title_full_unstemmed | Wild-type and mutated IDH1/2 enzymes and therapy responses |
title_short | Wild-type and mutated IDH1/2 enzymes and therapy responses |
title_sort | wild-type and mutated idh1/2 enzymes and therapy responses |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5895605/ https://www.ncbi.nlm.nih.gov/pubmed/29367755 http://dx.doi.org/10.1038/s41388-017-0077-z |
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