摘要
原文 | 英語 |
---|---|
頁(從 - 到) | 74-80 |
頁數 | 7 |
期刊 | Redox Biology |
卷 | 19 |
DOIs | |
出版狀態 | 已發佈 - 十月 1 2018 |
指紋
ASJC Scopus subject areas
- Organic Chemistry
- Clinical Biochemistry
引用此文
Upregulation of Znf179 acetylation by SAHA protects cells against oxidative stress. / Wu, Chung Che; Lee, Pin Tse; Kao, Tzu Jen; Chou, Szu Yi; Su, Ruei Yuan; Lee, Yi Chao; Yeh, Shiu Hwa; Liou, Jing Ping; Hsu, Tsung I.; Su, Tsung Ping; Chuang, Cheng Keng; Chang, Wen Chang; Chuang, Jian Ying.
於: Redox Biology, 卷 19, 01.10.2018, p. 74-80.研究成果: 雜誌貢獻 › 文章
}
TY - JOUR
T1 - Upregulation of Znf179 acetylation by SAHA protects cells against oxidative stress
AU - Wu, Chung Che
AU - Lee, Pin Tse
AU - Kao, Tzu Jen
AU - Chou, Szu Yi
AU - Su, Ruei Yuan
AU - Lee, Yi Chao
AU - Yeh, Shiu Hwa
AU - Liou, Jing Ping
AU - Hsu, Tsung I.
AU - Su, Tsung Ping
AU - Chuang, Cheng Keng
AU - Chang, Wen Chang
AU - Chuang, Jian Ying
N1 - Copyright © 2018 The Authors. Published by Elsevier B.V. All rights reserved.
PY - 2018/10/1
Y1 - 2018/10/1
N2 - The accumulation of reactive oxygen species (ROS) commonly occurs during normal aging and during some acute/chronic progressive disorders. In order to avoid oxidative damage, scavenging of these radicals is important. Previously, we identified zinc finger protein 179 (Znf179) as a neuroprotector that increases antioxidant enzymes against superoxide radicals. However, the molecular mechanisms involved in the activation and regulation of Znf179 remain unresolved. Here, by performing sequence alignment, bioinformatics analysis, immunoprecipitation using two specific acetyl-lysine antibodies, and treatment with the histone deacetylase (HDAC) inhibitor SAHA, we determined the lysine-specific acetylation of Znf179. Furthermore, we investigated Znf179 interaction with HDACs and revealed that peroxide insult induced a dissociation of Znf179-HDAC1/HDAC6, causing an increase in Znf179 acetylation. Importantly, HDAC inhibition by SAHA further prompted Znf179 hyperacetylation, which promoted Znf179 to form a transcriptional complex with Sp1 and increased antioxidant gene expression against oxidative attack. In summary, the results obtained in this study showed that Znf179 was regulated by HDACs and that Znf179 acetylation was a critical mechanism in the induction of antioxidant defense systems. Additionally, HDAC inhibitors may have therapeutic potential for induction of Znf179 acetylation, strengthening the Znf179 protective functions against neurodegenerative processes.
AB - The accumulation of reactive oxygen species (ROS) commonly occurs during normal aging and during some acute/chronic progressive disorders. In order to avoid oxidative damage, scavenging of these radicals is important. Previously, we identified zinc finger protein 179 (Znf179) as a neuroprotector that increases antioxidant enzymes against superoxide radicals. However, the molecular mechanisms involved in the activation and regulation of Znf179 remain unresolved. Here, by performing sequence alignment, bioinformatics analysis, immunoprecipitation using two specific acetyl-lysine antibodies, and treatment with the histone deacetylase (HDAC) inhibitor SAHA, we determined the lysine-specific acetylation of Znf179. Furthermore, we investigated Znf179 interaction with HDACs and revealed that peroxide insult induced a dissociation of Znf179-HDAC1/HDAC6, causing an increase in Znf179 acetylation. Importantly, HDAC inhibition by SAHA further prompted Znf179 hyperacetylation, which promoted Znf179 to form a transcriptional complex with Sp1 and increased antioxidant gene expression against oxidative attack. In summary, the results obtained in this study showed that Znf179 was regulated by HDACs and that Znf179 acetylation was a critical mechanism in the induction of antioxidant defense systems. Additionally, HDAC inhibitors may have therapeutic potential for induction of Znf179 acetylation, strengthening the Znf179 protective functions against neurodegenerative processes.
KW - Antioxidants
KW - HDACs
KW - Oxidative stress
KW - SAHA
KW - Znf179
UR - http://www.scopus.com/inward/record.url?scp=85051474924&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85051474924&partnerID=8YFLogxK
U2 - 10.1016/j.redox.2018.08.001
DO - 10.1016/j.redox.2018.08.001
M3 - Article
AN - SCOPUS:85051474924
VL - 19
SP - 74
EP - 80
JO - Redox Biology
JF - Redox Biology
SN - 2213-2317
ER -