SIRT5 inhibits peroxisomal ACOX1 to prevent oxidative damage and is downregulated in liver cancer

Peroxisomes account for ~35% of total H 2 O 2 generation in mammalian tissues. Peroxisomal ACOX1 (acyl‐CoA oxidase 1) is the first and rate‐limiting enzyme in fatty acid β‐oxidation and a major producer of H 2 O 2 . ACOX1 dysfunction is linked to peroxisomal disorders and hepatocarcinogenesis. Here,...

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Published inEMBO reports Vol. 19; no. 5
Main Authors Chen, Xiu‐Fei, Tian, Meng‐Xin, Sun, Ren‐Qiang, Zhang, Meng‐Li, Zhou, Li‐Sha, Jin, Lei, Chen, Lei‐Lei, Zhou, Wen‐Jie, Duan, Kun‐Long, Chen, Yu‐Jia, Gao, Chao, Cheng, Zhou‐Li, Wang, Fang, Zhang, Jin‐Ye, Sun, Yi‐Ping, Yu, Hong‐Xiu, Zhao, Yu‐Zheng, Yang, Yi, Liu, Wei‐Ren, Shi, Ying‐Hong, Xiong, Yue, Guan, Kun‐Liang, Ye, Dan
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 01.05.2018
Springer Nature B.V
John Wiley and Sons Inc
Subjects
ACOX1
Acyl-CoA Oxidase - antagonists & inhibitors
Acyl-CoA Oxidase - genetics
Acyl-CoA Oxidase - metabolism
Animals
Carcinoma, Hepatocellular - metabolism
Clonal deletion
Damage prevention
Deoxyribonucleic acid
Dimers
DNA
DNA Damage
Down-Regulation
EMBO03
EMBO29
EMBO31
Female
Gene Knockdown Techniques
HEK293 Cells
HeLa Cells
Hep G2 Cells
Hepatocellular carcinoma
Homeostasis
Humans
Hydrogen Peroxide
Liver
Liver cancer
Liver Neoplasms - metabolism
Male
Metabolism
Mice
Mice, Knockout
Middle Aged
Oxidation
Oxidation-Reduction
Oxidative Stress
Peroxisomes
Peroxisomes - chemistry
Prognosis
Reactive oxygen species
SIRT5
Sirtuins - genetics
Sirtuins - metabolism
succinylation
SIRT5
liver cancer
succinylation
ACOX1
oxidative stress
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Abstract Peroxisomes account for ~35% of total H 2 O 2 generation in mammalian tissues. Peroxisomal ACOX1 (acyl‐CoA oxidase 1) is the first and rate‐limiting enzyme in fatty acid β‐oxidation and a major producer of H 2 O 2 . ACOX1 dysfunction is linked to peroxisomal disorders and hepatocarcinogenesis. Here, we show that the deacetylase sirtuin 5 (SIRT5) is present in peroxisomes and that ACOX1 is a physiological substrate of SIRT5. Mechanistically, SIRT5‐mediated desuccinylation inhibits ACOX1 activity by suppressing its active dimer formation in both cultured cells and mouse livers. Deletion of SIRT5 increases H 2 O 2 production and oxidative DNA damage, which can be alleviated by ACOX1 knockdown. We show that SIRT5 downregulation is associated with increased succinylation and activity of ACOX1 and oxidative DNA damage response in hepatocellular carcinoma (HCC). Our study reveals a novel role of SIRT5 in inhibiting peroxisome‐induced oxidative stress, in liver protection, and in suppressing HCC development. Synopsis This study reveals a role for SIRT5 in regulating peroxisomal H 2 O 2 and ROS homeostasis and indicates its potential function in liver protection and hepatocellular carcinoma suppression. SIRT5 is localized in peroxisomes where it controls H 2 O 2 metabolism. SIRT5‐mediated desuccinylation inhibits ACOX1 activity by suppressing its active dimer formation. SIRT5 downregulation increases ACOX1 activity and oxidative DNA damage response in HCC. Graphical Abstract This study reveals a role for SIRT5 in regulating peroxisomal H 2 O 2 and ROS homeostasis and indicates its potential function in liver protection and hepatocellular carcinoma suppression.
AbstractList Peroxisomes account for ~35% of total H2O2 generation in mammalian tissues. Peroxisomal ACOX1 (acyl‐CoA oxidase 1) is the first and rate‐limiting enzyme in fatty acid β‐oxidation and a major producer of H2O2. ACOX1 dysfunction is linked to peroxisomal disorders and hepatocarcinogenesis. Here, we show that the deacetylase sirtuin 5 (SIRT5) is present in peroxisomes and that ACOX1 is a physiological substrate of SIRT5. Mechanistically, SIRT5‐mediated desuccinylation inhibits ACOX1 activity by suppressing its active dimer formation in both cultured cells and mouse livers. Deletion of SIRT5 increases H2O2 production and oxidative DNA damage, which can be alleviated by ACOX1 knockdown. We show that SIRT5 downregulation is associated with increased succinylation and activity of ACOX1 and oxidative DNA damage response in hepatocellular carcinoma (HCC). Our study reveals a novel role of SIRT5 in inhibiting peroxisome‐induced oxidative stress, in liver protection, and in suppressing HCC development.
Peroxisomes account for ~35% of total H 2 O 2 generation in mammalian tissues. Peroxisomal ACOX 1 (acyl‐CoA oxidase 1) is the first and rate‐limiting enzyme in fatty acid β‐oxidation and a major producer of H 2 O 2 . ACOX 1 dysfunction is linked to peroxisomal disorders and hepatocarcinogenesis. Here, we show that the deacetylase sirtuin 5 ( SIRT 5) is present in peroxisomes and that ACOX 1 is a physiological substrate of SIRT 5. Mechanistically, SIRT 5‐mediated desuccinylation inhibits ACOX 1 activity by suppressing its active dimer formation in both cultured cells and mouse livers. Deletion of SIRT 5 increases H 2 O 2 production and oxidative DNA damage, which can be alleviated by ACOX 1 knockdown. We show that SIRT 5 downregulation is associated with increased succinylation and activity of ACOX 1 and oxidative DNA damage response in hepatocellular carcinoma ( HCC ). Our study reveals a novel role of SIRT 5 in inhibiting peroxisome‐induced oxidative stress, in liver protection, and in suppressing HCC development.
Peroxisomes account for ~35% of total H2O2 generation in mammalian tissues. Peroxisomal ACOX1 (acyl-CoA oxidase 1) is the first and rate-limiting enzyme in fatty acid β-oxidation and a major producer of H2O2 ACOX1 dysfunction is linked to peroxisomal disorders and hepatocarcinogenesis. Here, we show that the deacetylase sirtuin 5 (SIRT5) is present in peroxisomes and that ACOX1 is a physiological substrate of SIRT5. Mechanistically, SIRT5-mediated desuccinylation inhibits ACOX1 activity by suppressing its active dimer formation in both cultured cells and mouse livers. Deletion of SIRT5 increases H2O2 production and oxidative DNA damage, which can be alleviated by ACOX1 knockdown. We show that SIRT5 downregulation is associated with increased succinylation and activity of ACOX1 and oxidative DNA damage response in hepatocellular carcinoma (HCC). Our study reveals a novel role of SIRT5 in inhibiting peroxisome-induced oxidative stress, in liver protection, and in suppressing HCC development.Peroxisomes account for ~35% of total H2O2 generation in mammalian tissues. Peroxisomal ACOX1 (acyl-CoA oxidase 1) is the first and rate-limiting enzyme in fatty acid β-oxidation and a major producer of H2O2 ACOX1 dysfunction is linked to peroxisomal disorders and hepatocarcinogenesis. Here, we show that the deacetylase sirtuin 5 (SIRT5) is present in peroxisomes and that ACOX1 is a physiological substrate of SIRT5. Mechanistically, SIRT5-mediated desuccinylation inhibits ACOX1 activity by suppressing its active dimer formation in both cultured cells and mouse livers. Deletion of SIRT5 increases H2O2 production and oxidative DNA damage, which can be alleviated by ACOX1 knockdown. We show that SIRT5 downregulation is associated with increased succinylation and activity of ACOX1 and oxidative DNA damage response in hepatocellular carcinoma (HCC). Our study reveals a novel role of SIRT5 in inhibiting peroxisome-induced oxidative stress, in liver protection, and in suppressing HCC development.
Peroxisomes account for ~35% of total H2O2 generation in mammalian tissues. Peroxisomal ACOX1 (acyl‐CoA oxidase 1) is the first and rate‐limiting enzyme in fatty acid β‐oxidation and a major producer of H2O2. ACOX1 dysfunction is linked to peroxisomal disorders and hepatocarcinogenesis. Here, we show that the deacetylase sirtuin 5 (SIRT5) is present in peroxisomes and that ACOX1 is a physiological substrate of SIRT5. Mechanistically, SIRT5‐mediated desuccinylation inhibits ACOX1 activity by suppressing its active dimer formation in both cultured cells and mouse livers. Deletion of SIRT5 increases H2O2 production and oxidative DNA damage, which can be alleviated by ACOX1 knockdown. We show that SIRT5 downregulation is associated with increased succinylation and activity of ACOX1 and oxidative DNA damage response in hepatocellular carcinoma (HCC). Our study reveals a novel role of SIRT5 in inhibiting peroxisome‐induced oxidative stress, in liver protection, and in suppressing HCC development. Synopsis This study reveals a role for SIRT5 in regulating peroxisomal H2O2 and ROS homeostasis and indicates its potential function in liver protection and hepatocellular carcinoma suppression. SIRT5 is localized in peroxisomes where it controls H2O2 metabolism. SIRT5‐mediated desuccinylation inhibits ACOX1 activity by suppressing its active dimer formation. SIRT5 downregulation increases ACOX1 activity and oxidative DNA damage response in HCC. This study reveals a role for SIRT5 in regulating peroxisomal H2O2 and ROS homeostasis and indicates its potential function in liver protection and hepatocellular carcinoma suppression.
Peroxisomes account for ~35% of total H 2 O 2 generation in mammalian tissues. Peroxisomal ACOX1 (acyl‐CoA oxidase 1) is the first and rate‐limiting enzyme in fatty acid β‐oxidation and a major producer of H 2 O 2 . ACOX1 dysfunction is linked to peroxisomal disorders and hepatocarcinogenesis. Here, we show that the deacetylase sirtuin 5 (SIRT5) is present in peroxisomes and that ACOX1 is a physiological substrate of SIRT5. Mechanistically, SIRT5‐mediated desuccinylation inhibits ACOX1 activity by suppressing its active dimer formation in both cultured cells and mouse livers. Deletion of SIRT5 increases H 2 O 2 production and oxidative DNA damage, which can be alleviated by ACOX1 knockdown. We show that SIRT5 downregulation is associated with increased succinylation and activity of ACOX1 and oxidative DNA damage response in hepatocellular carcinoma (HCC). Our study reveals a novel role of SIRT5 in inhibiting peroxisome‐induced oxidative stress, in liver protection, and in suppressing HCC development. Synopsis This study reveals a role for SIRT5 in regulating peroxisomal H 2 O 2 and ROS homeostasis and indicates its potential function in liver protection and hepatocellular carcinoma suppression. SIRT5 is localized in peroxisomes where it controls H 2 O 2 metabolism. SIRT5‐mediated desuccinylation inhibits ACOX1 activity by suppressing its active dimer formation. SIRT5 downregulation increases ACOX1 activity and oxidative DNA damage response in HCC. Graphical Abstract This study reveals a role for SIRT5 in regulating peroxisomal H 2 O 2 and ROS homeostasis and indicates its potential function in liver protection and hepatocellular carcinoma suppression.
Peroxisomes account for ~35% of total H O generation in mammalian tissues. Peroxisomal ACOX1 (acyl-CoA oxidase 1) is the first and rate-limiting enzyme in fatty acid β-oxidation and a major producer of H O ACOX1 dysfunction is linked to peroxisomal disorders and hepatocarcinogenesis. Here, we show that the deacetylase sirtuin 5 (SIRT5) is present in peroxisomes and that ACOX1 is a physiological substrate of SIRT5. Mechanistically, SIRT5-mediated desuccinylation inhibits ACOX1 activity by suppressing its active dimer formation in both cultured cells and mouse livers. Deletion of SIRT5 increases H O production and oxidative DNA damage, which can be alleviated by knockdown. We show that SIRT5 downregulation is associated with increased succinylation and activity of ACOX1 and oxidative DNA damage response in hepatocellular carcinoma (HCC). Our study reveals a novel role of SIRT5 in inhibiting peroxisome-induced oxidative stress, in liver protection, and in suppressing HCC development.
Author Chen, Xiu‐Fei
Xiong, Yue
Zhou, Li‐Sha
Zhang, Jin‐Ye
Gao, Chao
Cheng, Zhou‐Li
Wang, Fang
Liu, Wei‐Ren
Zhao, Yu‐Zheng
Ye, Dan
Duan, Kun‐Long
Zhou, Wen‐Jie
Sun, Yi‐Ping
Yu, Hong‐Xiu
Guan, Kun‐Liang
Zhang, Meng‐Li
Chen, Yu‐Jia
Chen, Lei‐Lei
Shi, Ying‐Hong
Sun, Ren‐Qiang
Jin, Lei
Tian, Meng‐Xin
Yang, Yi
AuthorAffiliation 2 Key Laboratory of Metabolism and Molecular Medicine, Ministry of Education Department of Biochemistry and Molecular Biology School of Basic Medical Sciences Fudan University Shanghai China
7 Lineberger Comprehensive Cancer Center Department of Biochemistry and Biophysics University of North Carolina at Chapel Hill Chapel Hill NC USA
3 State Key Laboratory of Genetic Engineering Collaborative Innovation Center of Genetics and Development School of Life Sciences Fudan University Shanghai China
8 Department of Pharmacology and Moores Cancer Center University of California San Diego La Jolla CA USA
6 School of Pharmacy East China University of Science and Technology Shanghai China
4 Department of Liver Surgery Liver Cancer Institute Zhongshan Hospital Fudan University Shanghai China
5 Key Laboratory of Carcinogenesis and Cancer Invasion of Ministry of Education Shanghai China
1 Molecular and Cell Biology Lab Institute of Biomedical Sciences Shanghai Medical College Shanghai China
9 Department of
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Fri Jul 11 15:09:53 EDT 2025
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Issue 5
Keywords SIRT5
liver cancer
succinylation
ACOX1
oxidative stress
Language English
License 2018 The Authors.
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Snippet Peroxisomes account for ~35% of total H 2 O 2 generation in mammalian tissues. Peroxisomal ACOX1 (acyl‐CoA oxidase 1) is the first and rate‐limiting enzyme in...
Peroxisomes account for ~35% of total H2O2 generation in mammalian tissues. Peroxisomal ACOX1 (acyl‐CoA oxidase 1) is the first and rate‐limiting enzyme in...
Peroxisomes account for ~35% of total H O generation in mammalian tissues. Peroxisomal ACOX1 (acyl-CoA oxidase 1) is the first and rate-limiting enzyme in...
Peroxisomes account for ~35% of total H2O2 generation in mammalian tissues. Peroxisomal ACOX1 (acyl-CoA oxidase 1) is the first and rate-limiting enzyme in...
Peroxisomes account for ~35% of total H 2 O 2 generation in mammalian tissues. Peroxisomal ACOX 1 (acyl‐CoA oxidase 1) is the first and rate‐limiting enzyme in...
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proquest
pubmed
wiley
springer
SourceType Open Access Repository
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Index Database
Publisher
SubjectTerms ACOX1
Acyl-CoA Oxidase - antagonists & inhibitors
Acyl-CoA Oxidase - genetics
Acyl-CoA Oxidase - metabolism
Animals
Carcinoma, Hepatocellular - metabolism
Clonal deletion
Damage prevention
Deoxyribonucleic acid
Dimers
DNA
DNA Damage
Down-Regulation
EMBO03
EMBO29
EMBO31
Female
Gene Knockdown Techniques
HEK293 Cells
HeLa Cells
Hep G2 Cells
Hepatocellular carcinoma
Homeostasis
Humans
Hydrogen Peroxide
Liver
Liver cancer
Liver Neoplasms - metabolism
Male
Metabolism
Mice
Mice, Knockout
Middle Aged
Oxidation
Oxidation-Reduction
Oxidative Stress
Peroxisomes
Peroxisomes - chemistry
Prognosis
Reactive oxygen species
SIRT5
Sirtuins - genetics
Sirtuins - metabolism
succinylation
Title SIRT5 inhibits peroxisomal ACOX1 to prevent oxidative damage and is downregulated in liver cancer
URI https://link.springer.com/article/10.15252/embr.201745124
https://onlinelibrary.wiley.com/doi/abs/10.15252%2Fembr.201745124
https://www.ncbi.nlm.nih.gov/pubmed/29491006
https://www.proquest.com/docview/2034202054
https://www.proquest.com/docview/2009568062
https://pubmed.ncbi.nlm.nih.gov/PMC5934778
Volume 19
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