ArticleiScience2025
SIRT3 regulates PDHA1 acetylation in HUVECs to modulate inflammation and pyroptosis under clinorotation.
Article in iScience, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
3 citing papers in PubMed, 1 synthesis or guideline pooled it.
- SIRT3 in post-myocardial infarction macrophage reprogramming: linking mitochondrial fitness to inflammation resolution and repair.Frontiers in immunology · 2026Pooled it
- SIRT3 deficiency drives alveolar epithelial mitochondrial dysfunction in bronchopulmonary dysplasia via PDHA1 hyperacetylation.iScience · 2026Article
- Inflammasome-associated pyroptosis and tumor angiogenesis in prostate cancer.Iranian journal of basic medical sciences · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microgravity-induced endothelial inflammation contributes to cardiovascular dysfunction in astronauts, but the metabolic mechanisms involved are not fully defined. Sirtuin-3 (SIRT3), a mitochondrial deacetylase, regulates cellular metabolism and redox balance. The results demonstrate that two-dimensional clinorotation-induced simulated microgravity suppresses SIRT3 in human umbilical vein endothelial cells (HUVECs), resulting in mitochondrial dysfunction, NLRP3 inflammasome activation, and pyroptosis. SIRT3 overexpression mitigated these effects, while SIRT3 knockdown exacerbated them. Mechanistically, SIRT3 deletion promoted acetylation of pyruvate dehydrogenase E1α (PDHA1) at lysine 83, inhibiting pyruvate dehydrogenase complex (PDHC) activity and shifting metabolism toward higher levels of glycolysis. PDHA1 transfection suppressed NLRP3 inflammasome activation, pyroptosis, and glycolysis in HUVECs under simulated microgravity, while restoring mitochondrial membrane potential (ΔΨm) and oxidative phosphorylation. The PDHA1-K83R mutant provided stronger protection than wild-type PDHA1. These findings reveal that the SIRT3-PDHA1 axis links mitochondrial metabolism to endothelial inflammation under simulated microgravity, suggesting that targeting this pathway could help maintain vascular health during spaceflight.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.