This publication suggests that acetate, derived from acetic acid, may assist the brain and other organs in reducing inflammation. That it does so specifically by acetylating DNA histones, explains the effectiveness of products such as organic apple cider vinegar in managing overmethylators.
Overmethylators, who may be identified by a histamine blood test, would benefit because acetyl-CoA competes with methyl compounds at the DNA histone. Whichever molecule binds to the histones determines if the cell turns to the slow mode or fast mode. In other words, histone and methylation control the activation of the cell and the product of their DNA transcription to produce proteins.
In summary, apple cider vinegar’s affect on histones could be very good for overmethylators. And consequently it may not be so good for undermethylators. Inadequately nourished or supplemented overmethylators have a tendency manifest symptoms of verbosity, paranoia, phobias and at the further end of the scale auditory and delusional schizophrenia. Dr William Walsh PhD believes that as many as 46% of persons with schizophrenia are overmethylators.
Acetate supplementation increases brain histone acetylation and inhibits histone deacetylase activity and expression.
Acetate supplementation increases brain, heart, and liver acetyl-CoA levels and reduces lipopolysaccharide-induced neuroinflammation. Because intracellular acetyl-CoA can be used to alter histone acetylation-state, using Western blot analysis, we measured the temporal effect that acetate supplementation had on brain and liver histone acetylation following a single oral dose of glyceryl triacetate (6 g/kg). In parallel experiments, we measured the effect that acetate supplementation had on histone deacetylase (HDAC) and histone acetyltransferase (HAT) enzymic activities and the expression levels of HDAC class I and II enzymes using Western blot analysis. We found that acetate supplementation increased the acetylation-state of brain histone H4 at lysine 8 at 2 and 4 h, histone H4 at lysine 16 at 4 and 24 h, and histone H3 at lysine 9 at 4 h following treatment. No changes in other forms of brain or liver H3 and H4 acetylation-state were found at any post-treatment times measured. Enzymic HAT and HDAC assays on brain extracts showed that acetate supplementation had no effect on HAT activity, but significantly inhibited by 2-fold HDAC activity at 2 and 4 h post-treatment. Western blot analysis demonstrated that HDAC 2 levels were decreased at 4 h following treatment. Based on these results, we conclude that acetyl-CoA derived from acetate supplementation increases brain histone acetylation-state by reducing HDAC activity and expression.