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Trichostatin A enhances acetylation as well as protein stability of ERα through induction of p300 protein
DC Field | Value | Language |
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dc.contributor.author | Kim, Sung-Hye | - |
dc.contributor.author | Kang, Hyun-Jin | - |
dc.contributor.author | Na, Hyelin | - |
dc.contributor.author | Lee, Mi-Ock | - |
dc.date.accessioned | 2017-02-03T02:28:22Z | - |
dc.date.available | 2017-02-03T02:28:22Z | - |
dc.date.issued | 2010-04-13 | - |
dc.identifier.citation | Breast Cancer Research, 12(2):R22 | ko_KR |
dc.identifier.uri | https://hdl.handle.net/10371/100407 | - |
dc.description | This is an open access article distributed under the terms of the Creative Commons Attribution
License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. | ko_KR |
dc.description.abstract | Abstract
Introduction Trichostatin A (TSA) is a well-characterized histone deacetylase (HDAC) inhibitor. TSA modifies the balance between HDAC and histone acetyltransferase activities that is important in chromatin remodeling and gene expression. Although several previous studies have demonstrated the role of TSA in regulation of estrogen receptor alpha (ERα), the precise mechanism by which TSA affects ERα activity remains unclear. Methods Transient transfection was performed using the Welfect-EX™Plus procedure. The mRNA expression was determined using RT-PCR. Protein expression and interaction were determined by western blotting and immunoprecipitation. The transfection of siRNAs was performed using the Oligofectamine™ reagent procedure. Results TSA treatment increased acetylation of ERα in a dose-dependent manner. The TSA-induced acetylation of ERα was accompanied by an increased stability of ERα protein. Interestingly, TSA also increased the acetylation and the stability of p300 protein. Overexpression of p300 induced acetylation and stability of ERα by blocking ubiquitination. Knockdown of p300 by RNA interference decreased acetylation as well as the protein level of ERα, indicating that p300 mediated the TSA-induced stabilization of ERα. Conclusions We report that TSA enhanced acetylation as well as the stability of the ERα protein by modulating stability of p300. These results may provide the molecular basis for pharmacological functions of HDAC inhibitors in the treatment of human breast cancer. | ko_KR |
dc.language.iso | en | ko_KR |
dc.publisher | BioMed Central | ko_KR |
dc.title | Trichostatin A enhances acetylation as well as protein stability of ERα through induction of p300 protein | ko_KR |
dc.type | Article | ko_KR |
dc.contributor.AlternativeAuthor | 김성혜 | - |
dc.contributor.AlternativeAuthor | 강현진 | - |
dc.contributor.AlternativeAuthor | 나혜린 | - |
dc.contributor.AlternativeAuthor | 이미옥 | - |
dc.identifier.doi | 10.1186/bcr2562 | - |
dc.language.rfc3066 | en | - |
dc.rights.holder | Kim et al.; licensee BioMed Central Ltd. | - |
dc.date.updated | 2017-01-29T03:04:31Z | - |
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