ArticleCommunications biology2025
Lipolysis-derived fatty acids are needed for homeostatic control of sterol element-binding protein-1c driven hepatic lipogenesis.
Article in Communications biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Article
- Integrating WGCNA and machine learning to identify and validate key biomarkers in MASLD.BMC gastroenterology · 2026Article
- Chronic Alcohol Consumption Induces Irreversible and Heterogeneous Pancreatic Steatosis in Men: An MRI-Based Cross-Sectional Study.Journal of clinical medicine · 2026Article
- Regulatory effects of hawthorn on lipid metabolic homeostasis: mechanisms, evidences, and perspectives.Frontiers in nutrition · 2026Review
- Pregnancy and lactation exposure to bisphenol S induces ferroptosis via disrupted hepatic lipid metabolism in offspring mice.Frontiers in toxicology · 2026Article
- Bisphenol A Alters the Expression of Genes Involved in Lipogenesis, Inflammation, and Oxidative Stress in the Liver of Adult Zebrafish.Pharmaceuticals (Basel, Switzerland) · 2025Article
- PNPLA3 is a triglyceride lipase that mobilizes polyunsaturated fatty acids to facilitate hepatic secretion of large-sized very low-density lipoprotein.Nature communications · 2024Article
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Authors and funding
14 authors.
Funding
Abstract
Sterol Regulatory Element-Binding Protein-1c (SREBP-1c) is translated as an inactive precursor (P-SREBP-1c) postprandially. Low levels of unsaturated fatty acids (uFAs) and high insulin promote its proteolytic activation, yielding N-SREBP-1c that drives fatty acid (FA) biosynthesis. During fasting, however, lipogenesis is low, and adipose tissue lipolysis supplies the organism with FAs. Adipose Triglyceride Lipase (ATGL) is the rate-limiting enzyme for adipose tissue lipolysis, and it preferentially releases uFAs. Therefore, we hypothesized that adipose ATGL-derived uFAs suppress P-SREBP-1c activation in the liver. In this study, we show that (I) N-SREBP-1c is transiently higher in livers of fasted and refed adipose specific Atgl knockout mice than in control livers. (II) This effect is reversed by injection of uFAs. (III) uFAs inhibit endoplasmic reticulum to Golgi-apparatus transport of SREBP Cleavage-Activating Protein (SCAP) in hepatocytes, which is essential for SREBP activation. Our findings demonstrate that adipose tissue ATGL derived uFAs attenuate P-SREBP-1c activation in the liver mainly after refeeding. We propose that this ATGL/SREBP-1c axis adds an additional layer of coordination between lipogenesis and lipolysis.
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