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KDM4A regulates HIF-1 levels through H3K9me3
Regions of hypoxia (low oxygen) occur in most solid tumours and cells in these areas are the most aggressive and therapy resistant. In response to decreased oxygen, extensive changes in gene expression mediated by Hypoxia-Inducible Factors (HIFs) contribute significantly to the aggressive hypoxic tu...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5593970/ https://www.ncbi.nlm.nih.gov/pubmed/28894274 http://dx.doi.org/10.1038/s41598-017-11658-3 |
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author | Dobrynin, Grzegorz McAllister, Tom E. Leszczynska, Katarzyna B. Ramachandran, Shaliny Krieg, Adam J. Kawamura, Akane Hammond, Ester M. |
author_facet | Dobrynin, Grzegorz McAllister, Tom E. Leszczynska, Katarzyna B. Ramachandran, Shaliny Krieg, Adam J. Kawamura, Akane Hammond, Ester M. |
author_sort | Dobrynin, Grzegorz |
collection | PubMed |
description | Regions of hypoxia (low oxygen) occur in most solid tumours and cells in these areas are the most aggressive and therapy resistant. In response to decreased oxygen, extensive changes in gene expression mediated by Hypoxia-Inducible Factors (HIFs) contribute significantly to the aggressive hypoxic tumour phenotype. In addition to HIFs, multiple histone demethylases are altered in their expression and activity, providing a secondary mechanism to extend the hypoxic signalling response. In this study, we demonstrate that the levels of HIF-1α are directly controlled by the repressive chromatin mark, H3K9me3. In conditions where the histone demethylase KDM4A is depleted or inactive, H3K9me3 accumulates at the HIF-1α locus, leading to a decrease in HIF-1α mRNA and a reduction in HIF-1α stabilisation. Loss of KDM4A in hypoxic conditions leads to a decreased HIF-1α mediated transcriptional response and correlates with a reduction in the characteristics associated with tumour aggressiveness, including invasion, migration, and oxygen consumption. The contribution of KDM4A to the regulation of HIF-1α is most robust in conditions of mild hypoxia. This suggests that KDM4A can enhance the function of HIF-1α by increasing the total available protein to counteract any residual activity of prolyl hydroxylases. |
format | Online Article Text |
id | pubmed-5593970 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-55939702017-09-13 KDM4A regulates HIF-1 levels through H3K9me3 Dobrynin, Grzegorz McAllister, Tom E. Leszczynska, Katarzyna B. Ramachandran, Shaliny Krieg, Adam J. Kawamura, Akane Hammond, Ester M. Sci Rep Article Regions of hypoxia (low oxygen) occur in most solid tumours and cells in these areas are the most aggressive and therapy resistant. In response to decreased oxygen, extensive changes in gene expression mediated by Hypoxia-Inducible Factors (HIFs) contribute significantly to the aggressive hypoxic tumour phenotype. In addition to HIFs, multiple histone demethylases are altered in their expression and activity, providing a secondary mechanism to extend the hypoxic signalling response. In this study, we demonstrate that the levels of HIF-1α are directly controlled by the repressive chromatin mark, H3K9me3. In conditions where the histone demethylase KDM4A is depleted or inactive, H3K9me3 accumulates at the HIF-1α locus, leading to a decrease in HIF-1α mRNA and a reduction in HIF-1α stabilisation. Loss of KDM4A in hypoxic conditions leads to a decreased HIF-1α mediated transcriptional response and correlates with a reduction in the characteristics associated with tumour aggressiveness, including invasion, migration, and oxygen consumption. The contribution of KDM4A to the regulation of HIF-1α is most robust in conditions of mild hypoxia. This suggests that KDM4A can enhance the function of HIF-1α by increasing the total available protein to counteract any residual activity of prolyl hydroxylases. Nature Publishing Group UK 2017-09-11 /pmc/articles/PMC5593970/ /pubmed/28894274 http://dx.doi.org/10.1038/s41598-017-11658-3 Text en © The Author(s) 2017 Open Access This 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 license, and indicate if changes were made. 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/4.0/. |
spellingShingle | Article Dobrynin, Grzegorz McAllister, Tom E. Leszczynska, Katarzyna B. Ramachandran, Shaliny Krieg, Adam J. Kawamura, Akane Hammond, Ester M. KDM4A regulates HIF-1 levels through H3K9me3 |
title | KDM4A regulates HIF-1 levels through H3K9me3 |
title_full | KDM4A regulates HIF-1 levels through H3K9me3 |
title_fullStr | KDM4A regulates HIF-1 levels through H3K9me3 |
title_full_unstemmed | KDM4A regulates HIF-1 levels through H3K9me3 |
title_short | KDM4A regulates HIF-1 levels through H3K9me3 |
title_sort | kdm4a regulates hif-1 levels through h3k9me3 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5593970/ https://www.ncbi.nlm.nih.gov/pubmed/28894274 http://dx.doi.org/10.1038/s41598-017-11658-3 |
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