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HDAC6 and Ovarian Cancer

The special class IIb histone deacetylase, HDAC6, plays a prominent role in many cellular processes related to cancer, including oncogenesis, the cell stress response, motility, and myriad signaling pathways. Many of the lessons learned from other cancers can be applied to ovarian cancer as well. HD...

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Detalles Bibliográficos
Autores principales: Haakenson, Joshua, Zhang, Xiaohong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3676797/
https://www.ncbi.nlm.nih.gov/pubmed/23644884
http://dx.doi.org/10.3390/ijms14059514
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author Haakenson, Joshua
Zhang, Xiaohong
author_facet Haakenson, Joshua
Zhang, Xiaohong
author_sort Haakenson, Joshua
collection PubMed
description The special class IIb histone deacetylase, HDAC6, plays a prominent role in many cellular processes related to cancer, including oncogenesis, the cell stress response, motility, and myriad signaling pathways. Many of the lessons learned from other cancers can be applied to ovarian cancer as well. HDAC6 interacts with diverse proteins such as HSP90, cortactin, tubulin, dynein, p300, Bax, and GRK2 in both the nucleus and cytoplasm to carry out these cancerous functions. Not all pro-cancer interactions of HDAC6 involve deacetylation. The idea of using HDAC6 as a target for cancer treatment continues to expand in recent years, and more potent and specific HDAC6 inhibitors are required to effectively down-regulate the tumor-prone cell signaling pathways responsible for ovarian cancer.
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spelling pubmed-36767972013-07-02 HDAC6 and Ovarian Cancer Haakenson, Joshua Zhang, Xiaohong Int J Mol Sci Review The special class IIb histone deacetylase, HDAC6, plays a prominent role in many cellular processes related to cancer, including oncogenesis, the cell stress response, motility, and myriad signaling pathways. Many of the lessons learned from other cancers can be applied to ovarian cancer as well. HDAC6 interacts with diverse proteins such as HSP90, cortactin, tubulin, dynein, p300, Bax, and GRK2 in both the nucleus and cytoplasm to carry out these cancerous functions. Not all pro-cancer interactions of HDAC6 involve deacetylation. The idea of using HDAC6 as a target for cancer treatment continues to expand in recent years, and more potent and specific HDAC6 inhibitors are required to effectively down-regulate the tumor-prone cell signaling pathways responsible for ovarian cancer. Molecular Diversity Preservation International (MDPI) 2013-05-02 /pmc/articles/PMC3676797/ /pubmed/23644884 http://dx.doi.org/10.3390/ijms14059514 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland http://creativecommons.org/licenses/by/3.0 This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Haakenson, Joshua
Zhang, Xiaohong
HDAC6 and Ovarian Cancer
title HDAC6 and Ovarian Cancer
title_full HDAC6 and Ovarian Cancer
title_fullStr HDAC6 and Ovarian Cancer
title_full_unstemmed HDAC6 and Ovarian Cancer
title_short HDAC6 and Ovarian Cancer
title_sort hdac6 and ovarian cancer
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3676797/
https://www.ncbi.nlm.nih.gov/pubmed/23644884
http://dx.doi.org/10.3390/ijms14059514
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