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The human liver and gut bacteria can alter molecules in food to influence signaling pathways that can activate or deactivate an array of genes, according to a new study led by researchers at Penn State.

The study, which involved both humans and mice, was published in the journal Communications Biology. When gut bacteria break down the dietary amino acid tryptophan—a protein building block found in common foods, including nuts, cheese and chicken—they produce a molecule, or metabolite, called indole-3-acetic acid (IAA).

The researchers found that gut bacteria and the liver can chemically attach glycine, an amino acid produced by the body and found in beans and meats, to IAA. Typically, this process, called conjugation, helps make the metabolite water-soluble so the body can safely eliminate it. IAA-glycine, however, may have special characteristics, the researchers said.

IAA can bind to and activate the aryl hydrocarbon (Ah) receptor, a protein that can activate or deactivate other genes. Previous research has shown that activation of the Ah receptor enhances gut immune function and intestinal barrier integrity, according to Gary H. Perdew, Thomas and Dorothy Willits Hallowell Emeritus Chair in Agricultural Sciences in the College of Agricultural Sciences and lead author of the paper.

"Surprisingly, we found that IAA-glycine also activates the Ah receptor, thereby contributing to its physiological activity," he said. "In contrast, previous work has demonstrated that conjugation reactions with some Ah receptor ligands can block receptor activation.

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