Phytic acid triggers a biochemical process that reduces the activity of enzymes called matrix metalloproteinases, which helps maintain the structural integrity of the intestinal lining.
Mechanism
Synthesis from 3 studies
A natural compound in plant foods binds to a molecular switch in gut cells that turns off enzymes that break down the gut's protective seal. When this switch is flipped, the seal stays intact, preventing harmful substances from leaking through the intestinal wall.
Most probable mechanism
A molecule found in plant foods binds to a protein in gut cells that turns off genes responsible for breaking down the protective lining of the intestine. This binding triggers a chain reaction that silences those genes, allowing the gut lining to stay tightly sealed and prevent leakage.
Phytic acid binds directly to the DAD domain of the NCoR1/2 corepressor complex associated with histone deacetylase 3 (HDAC3) on chromatin
This binding induces a conformational change that activates HDAC3's deacetylase enzyme activity
Activated HDAC3 removes acetyl groups from histone H4 at lysine 16 (H4K16) at the promoter regions of matrix metalloproteinase (MMP) genes
Deacetylation of H4K16 represses transcription of MMP genes, including MMP1, MMP3, MMP10, and MMP13
Reduced production of MMP enzymes 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 (3)
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
Phytic Acid (InsP6) Activates HDAC3 Epigenetic Axis to Maintain Intestinal Barrier Function
Contradicting (0)
Community contributions welcome
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