Cited by 123Sirtuins and Resveratrol in MedicineBiochemical and Molecular ResearchAmino Acid Enzymes and Metabolism

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Overexpression of SIRT5 confirms its involvement in deacetylation and activation of carbamoyl phosphate synthetase 1

Ogura, Masahito, Nakamura, Yasuhiko, Tanaka, Daisuke, Zhuang, Xiaotong, Fujita, Yoshihito, Obara, Akio, Hamasaki, Akihiro, Hosokawa, Masaya, Inagaki, Nobuya·2010·Biochemical and Biophysical Research Communications

DOI 10.1016/j.bbrc.2010.01.081

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Abstract

SIR2 protein, an NAD-dependent deacetylase, is localized to nucleus and is involved in life span extension by calorie restriction in yeast. In mammals, among the seven SIR2 homologues (SIRT1-7), SIRT3, 4, and 5 are localized to mitochondria. As SIRT5 mRNA levels in liver are increased by fasting, the physiological role of SIRT5 was investigated in liver of SIRT5-overexpressing transgenic (SIRT5 Tg) mice. We identified carbamoyl phosphate synthetase 1 (CPS1), a key enzyme of the urea cycle that catalyzes condensation of ammonia with bicarbonate to form carbamoyl phosphate, as a target of SIRT5 by two-dimensional electrophoresis comparing mitochondrial proteins in livers of SIRT5 Tg and wild-type mice. CPS1 protein was more deacetylated and activated in liver of SIRT5 Tg mice than in wild-type. In addition, urea production was upregulated in hepatocytes of SIRT5 Tg mice. These results agree with those of a previous study using SIRT5 knockout (KO) mice. Because ammonia generated during fasting is toxic, SIRT5 protein might play a protective role by converting ammonia to non-toxic urea through deacetylation and activation of CPS1.

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Authors: Ogura, M., Nakamura, Y., Tanaka, D., Zhuang, X., Fujita, Y., Obara, A., Hamasaki, A., Hosokawa, M., & Inagaki, N.
Affiliations: Kyoto University (JP)
Corresponding author: Inagaki, Nobuya
ORCID: Ogura, Masahito
Nakamura, Yasuhiko
Tanaka, Daisuke
Fujita, Yoshihito
Hamasaki, Akihiro
Hosokawa, Masaya
Inagaki, Nobuya
Venue: Biochemical and Biophysical Research Communications
Publisher: Elsevier BV
Published: 2010-02
Volume: 393
Issue: 1
Pages: 73-78
ISSN: 0006-291X (ISSN-L)
DOI: 10.1016/j.bbrc.2010.01.081
OpenAlex: W2076186906
Cited by: 121
References: 28
Citations by year: 2026: 5 · 2025: 5 · 2024: 5 · 2023: 9 · 2022: 11 · 2021: 8 · 2020: 3 · 2019: 3 · 2018: 6 · 2017: 8 · 2016: 11 · 2015: 10 · 2014: 7 · 2013: 9 · 2012: 9
FWCI: 3.96
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
Locations: Biochemical and Biophysical Research Communications (publishedVersion)
PubMed (publishedVersion)
Funders: Kyoto University
Ministry of Education, Culture, Sports, Science and Technology
Ministry of Health, Labour and Welfare
Topics: Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Keywords: SIRT5, CPS1, protein deacetylation, enzyme activation, urea cycle, ammonia detoxification, liver, fasting, transgenic mice, mitochondrial proteins
MeSH terms: Acetylation, Amino Acid Sequence, Ammonia, Animals, Carbamoyl-Phosphate Synthase (Ammonia), Enzyme Activation, Fasting, Mice, Transgenic, Mitochondria, Liver, Molecular Sequence Data, Peptides, RNA, Messenger, Urea, Up-Regulation, Mice, Knockout, Hepatocytes, Sirtuins, Mice

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Overexpression of SIRT5 confirms its involvement in deacetylation and activation of carbamoyl phosphate synthetase 1

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