Activation of AMP-Activated Protein Kinase and Stimulation of Energy Metabolism by Acetic Acid in L6 Myotube Cells.
Level 5 - mechanism / opinion, no new human data
In vitro cell culture experiment without human participants.
PubMed 27348124 · doi:10.1371/journal.pone.0158055
What was done
L6 rat myotube cells were treated with acetic acid in culture medium. Researchers measured cellular uptake of acetic acid, AMP-activated protein kinase (AMPK) phosphorylation, gene and protein expression of glucose transporter 4 (GLUT4), myoglobin, and myocyte enhancer factor 2A (MEF2A), as well as glucose uptake, fatty acid uptake, and intracellular triglyceride accumulation compared to untreated cells.
What was found
Acetic acid was rapidly taken up by L6 cells and triggered AMPK phosphorylation. Treated cells exhibited increased gene and protein expression of GLUT4, myoglobin, and MEF2A. Additionally, glucose uptake and fatty acid uptake were increased, whereas triglyceride accumulation was reduced compared with untreated controls. The abstract reported directional changes only and provided no specific numerical values or effect sizes.
Why it matters
The study identifies a plausible cellular pathway (AMPK activation and MEF2A upregulation) by which acetic acid modulates glucose and fatty acid handling in skeletal muscle cells.
Limits
This was an in vitro study conducted exclusively in a rat myotube cell line (L6 cells), meaning physiological relevance to intact human skeletal muscle, dosing kinetics, and clinical outcomes remain unverified. The abstract omits acetic acid concentrations, exposure durations, sample replicates, and quantitative statistical metrics.
Cited by
- supports Acetic acid reduces hepatic gluconeogenesis and stimulates GLUT4 translocation in muscle cells via AMPK activation.