The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
Overexpression of SIRT5 confirms its involvement in deacetylation and activation of carbamoyl phosphate synthetase 1
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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“SIRT5 promotes urea cycle function via the regulation of carbamoyl phosphate synthase (CPS1) (Nakagawa et al., 2009; Ogura et al., 2010)”
From SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways (2013) · cites this paper as Ogura et al., 2010
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SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways
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Metadata
- 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
- Venue
- Biochemical and Biophysical Research Communications
- Publisher
- Elsevier BV
- Published
- 2010-02
- Volume
- 393
- Issue
- 1
- Pages
- 73-78
- ISSN
- 0006-291X (ISSN-L)
- 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
- 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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