Cited by 117Sirtuins and Resveratrol in MedicineFOXO transcription factor regulationNitric Oxide and Endothelin Effects

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SIRT3 interactions with FOXO3 acetylation, phosphorylation and ubiquitinylation mediate endothelial cell responses to hypoxia

Tseng, Anne H.-H., Wu, Li-Hong, Shieh, Shyan-Shu, Wang, Danny Ling·2014·Biochemical Journal

DOI 10.1042/bj20140213

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Abstract

The endothelial cells (ECs) that line the vascular lumen are exposed to a wide variety of environmental stresses, such as hypoxia. Maladaptation to stress in ECs is a key event in the development of cardiovascular disease. Sirtuin 3 (SIRT3) is an NAD+-dependent protein deacetylase that modulates various proteins to control mitochondrial function and metabolism. We found that hypoxia elicits an increase in SIRT3 mRNA and protein expression in ECs. Under the same hypoxic conditions, the forkhead box class O transcription factor FOXO3 is deacetylated by SIRT3. The SIRT3-mediated deacetylation of FOXO3 further reduces FOXO3 phosphorylation, ubiquitination and degradation, thereby stabilizing FOXO3 proteins. As a result, the level of FOXO3 protein is increased during hypoxia. Moreover, a set of FOXO3-dependent mitochondrial antioxidant enzymes, including manganese superoxide dismutase (MnSOD), peroxiredoxin 3 (Prx3), Prx5 and thioredoxin 2 (Trx2), are up-regulated in ECs to facilitate ROS detoxification in response to hypoxia. The SIRT3-mediated deacetylation of FOXO3 preserves mitochondrial bioenergetic function and increases cell survival under hypoxic conditions. These results indicate that SIRT3 stabilizes FOXO3 via deacetylation, which enhances the mitochondrial antioxidant defence system to increase the adaptive capacity of ECs during hypoxia. This finding provides a direction for ameliorating the development of cardiovascular diseases.

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Retraction Note: Sirt3 suppresses calcium oxalate-induced renal tubular epithelial cell injury via modification of FoxO3a-mediated autophagy
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Retracted
Sirtuin 3, a mitochondrial metabolic enzyme, links the mitochondrial function to neurophysiology in depression
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Authors: Tseng, A. H.-H., Wu, L.-H., Shieh, S.-S., & Wang, D. L.
Affiliations: Tzu Chi University (TW)
Institute of Medical Sciences, Tzu-Chi University, Hualien 97004, Taiwan
Institute of Biomedical Sciences, Academia Sinica (TW)
ORCID: Wang, Danny Ling
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 2014-10-23
Volume: 464
Issue: 1
Pages: 157-168
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj20140213
OpenAlex: W1978900120
Cited by: 114
References: 52
Citations by year: 2026: 3 · 2025: 7 · 2024: 9 · 2023: 19 · 2022: 9 · 2021: 12 · 2020: 11 · 2019: 11 · 2018: 7 · 2017: 6 · 2016: 8 · 2015: 11 · 2014: 1
FWCI: 4.41
Type: journal article
Language: en
Open access: closed
Locations: Biochemical Journal (publishedVersion)
PubMed (publishedVersion)
Funders: National Science Council
Academia Sinica
Topics: Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › FOXO transcription factor regulation
Health Sciences › Medicine › Physiology (medical) › Nitric Oxide and Endothelin Effects
Keywords: SIRT3, FOXO3, hypoxia, endothelial cells, protein deacetylation, protein stability, ubiquitination, phosphorylation, mitochondrial antioxidant defense, reactive oxygen species, manganese superoxide dismutase, peroxiredoxin, thioredoxin 2, mitochondrial bioenergetics, cardiovascular disease
MeSH terms: Forkhead Box Protein O3, Acetylation, Cell Survival, Humans, Phosphorylation, Protein Binding, Cell Hypoxia, Endothelial Cells, Forkhead Transcription Factors, Ubiquitination, Sirtuin 3, Human Umbilical Vein Endothelial Cells

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SIRT3 interactions with FOXO3 acetylation, phosphorylation and ubiquitinylation mediate endothelial cell responses to hypoxia

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