AI Article Synopsis
- Ketone bodies are produced in the liver during low glucose availability and serve as an alternative energy source, particularly for the brain, heart, and muscles.
- β-hydroxybutyrate (BHB) is emerging as a signaling molecule that can modify proteins through a process called lysine β-hydroxybutyrylation (Kbhb), which is sensitive to BHB levels and occurs in various cellular locations.
- The use of a commonly employed antibody to study Kbhb on histones may misrepresent data because it can also detect other modifications, like acetylations, especially in experiments involving deacetylation inhibition.
Article Abstract
Ketone bodies are short chain fatty acids produced in the liver during periods of limited glucose availability that provide an alternative source of energy for the brain, heart, and skeletal muscle. Beyond this classical metabolic role, β-hydroxybutyrate (BHB), is gaining recognition as a pleiotropic signaling molecule. Lysine β-hydroxybutyrylation (Kbhb) is a newly discovered post-translational modification in which BHB is covalently attached to lysine ε-amino groups. This novel protein adduct is metabolically sensitive, dependent on BHB concentration, and found on proteins in multiple intracellular compartments, including the mitochondria and nucleus. Therefore, Kbhb is hypothesized to be an important component of ketone body-regulated physiology. Kbhb on histones is proposed to be an epigenetic regulator, which links metabolic alterations to gene expression. However, we found that the widely used antibody against the β-hydroxybutyrylated lysine 9 on histone H3 (H3K9bhb) also recognizes other modification(s), which are increased by deacetylation inhibition and include likely acetylations. Therefore, caution must be used when interpreting gene regulation data acquired with the H3K9bhb antibody.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10120668 | PMC |
| http://dx.doi.org/10.1101/2023.04.12.536655 | DOI Listing |
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Ketone bodies are short-chain fatty acids produced in the liver during periods of limited glucose availability that provide an alternative energy source for the brain, heart, and skeletal muscle. Beyond this metabolic role, β-hydroxybutyrate (BHB), is gaining recognition as a signaling molecule. Lysine β-hydroxybutyrylation (Kbhb) is a newly discovered post-translational modification in which BHB is covalently attached to lysine ε-amino groups.
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Article Synopsis
- Ketone bodies are produced in the liver during low glucose availability and serve as an alternative energy source, particularly for the brain, heart, and muscles.
- β-hydroxybutyrate (BHB) is emerging as a signaling molecule that can modify proteins through a process called lysine β-hydroxybutyrylation (Kbhb), which is sensitive to BHB levels and occurs in various cellular locations.
- The use of a commonly employed antibody to study Kbhb on histones may misrepresent data because it can also detect other modifications, like acetylations, especially in experiments involving deacetylation inhibition.
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