Removing legumes, whole grains, nuts, and seeds from the diet removes phytic acid, which may reduce its role in maintaining the integrity of the intestinal barrier.
Mechanism
Synthesis from 2 studies
Phytic acid from foods like beans and grains turns on a molecular switch in gut cells that stops enzymes from breaking down the seal between cells. Without this switch, the seal weakens and the gut becomes leaky. Adding phytic acid back fixes the seal.
Most probable mechanism
When phytic acid is present in the gut, it binds to a specific protein that turns on an enzyme called HDAC3. This enzyme then removes chemical tags from DNA that would otherwise turn on genes that break down the glue holding gut cells together. Without these genes active, the glue stays intact, keeping the gut lining sealed. If phytic acid is removed from the diet, the enzyme stays off, the genes turn on, the glue breaks down, and the gut becomes leaky.
Phytic acid is synthesized within intestinal epithelial cells through the enzymatic activity of IPMK, which converts inositol phosphates into phytic acid (InsP6)
Phytic acid binds directly to the DAD domain of the NCoR1/2 corepressor complex associated with HDAC3, inducing a conformational change that activates HDAC3's deacetylase function
Activated HDAC3 deacetylates histone H4 at lysine 16 at the promoter regions of matrix metalloproteinase (MMP) genes
Deacetylation of histone H4K16 represses transcription of MMP genes, including MMP1, MMP3, MMP10, and MMP13
Reduced expression of MMP proteases prevents degradation of tight junction proteins such as ZO-1 and occludin
Preservation of tight junction proteins maintains low paracellular permeability and structural integrity of the intestinal epithelial barrier
Evidence from Studies
Supporting (2)
Community contributions welcome
Phytic acid (InsP6) activates HDAC3 epigenetic axis to maintain intestinal barrier function
Phytic Acid (InsP6) Activates HDAC3 Epigenetic Axis to Maintain Intestinal Barrier Function
Contradicting (0)
Community contributions welcome
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