Nutrient-driven histone acetylation underlies energy storage and mobilization
Chen L., Zhu L., Xiao H., Wang X., Xia F., Wang Z.
Animal Study, published in Mol Metab (2026) — summary generated from the PubMed abstract.
Evidence from laboratory and animal studies provides groundwork for understanding mechanisms and potential before human studies continue.
- Level A · Stronger Clinical Evidence
- Level B · Emerging clinical evidence with positive signals
- Level C · Early human research exploring benefits
- Level D · Scientific groundwork from lab and animal studies
- Emerging · Emerging topic under active research
This page is generated from the PubMed record. The Thai description is an automated summary of bibliographic fields and the abstract, not a full translation, and is not medical advice.
- Study type
- Animal Study
- Journal
- Mol Metab (2026)
- Reported sample size
- —
- Source database
- Europe PMC
- PMID
- 41786244
- PMCID
- PMC12997339
- DOI
- 10.1016/j.molmet.2026.102344
- Citations
- 1
Abstract (original English)
In natural settings, energy storage and mobilization maintain a dynamic balance in response to recurrent overfeeding and fasting. Imbalanced energy storage and mobilization lead to a variety of metabolic dysfunctions. However, whether the metabolic status directly couples with epigenetic modifications and transcriptional outputs remains unclear. Here, we aimed to investigate the epigenetic mechanism underlying this adaptive balance and observed that, in an overfeeding state, increased glucose availability is associated with enhanced histone acetylation coinciding with acetyl-CoA production in an acyl-CoA short-chain synthetase 2 (ACSS2)-dependent manner, contributing to energy storage (e.g., lipogenesis); in contrast, in the fasting state, elevated d-β-hydroxybutyrate levels are associated with altered histone acetylation distribution and transcriptional programs, supporting a metabolic shift from anabolism to catabolism, such as fatty acid oxidation. In both overfeeding and fasting states, acetylated lysines in the histone require BRD4 to recognize and initiate transcriptional regulation. Inhibition of BRD4 leads to context-dependent phenotypic effects: it ameliorates non-alcoholic fatty liver disease (NAFLD) pathology induced by a high-fat diet, while it exacerbates hepatic steatosis in fasted mice or mice fed a ketogenic diet. Thus, these findings highlights that epigenetic
What this study does not prove
- • This study does not prove SVF is an approved treatment or a replacement for standard care.
- • This is preclinical work; animal or laboratory results cannot be applied to humans.
Evidence level
Evidence from laboratory and animal studies provides groundwork for understanding mechanisms and potential before human studies continue.
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