Abstract
The human gastrointestinal system has the capacity to metabolize dietary gluten. The capacity to degrade gliadin-derived peptide is present in humans from birth and increases during the first stages of life (up to 6–12 months of age). Fecal samples from 151 new-born and adult non-celiac disease (NCD) volunteers were collected, and glutenase and glianidase activities were evaluated. The capacity of total fecal proteins to metabolize 33-mer, 19-mer, and 13-mer gliadin peptides was also evaluated by high-performance liquid chromatography (HPLC). Feces from new-borns (meconium) showed glutenase and gliadinase activities, and peptidase activity against all three gliadin peptides. Maximal gluten degradative activity was observed in fecal samples from the youngest volunteers (0–12 months old). After the age of nine months, the gluten digestive capacity of gastrointestinal tract decreases and, from ±8 years old, individuals lose the ability to completely degrade toxic peptides. The gastrointestinal proteases involved in gluten digestion: elastase 2A, elastase 3B, and carboxipeptidase A1 are present from earlier stages of life. The human digestive tract contains the proteins capable of metabolizing gluten from birth, even before starting gluten intake. Humans are born with the ability to digest gluten and to completely degrade the potentially toxic gliadin-derived peptides (33-, 19-, and 13-mer).
Highlights
Gluten is considered to be the mass that remains when wheat dough is washed to remove starch granules and water-soluble constituents [1]
The Capacity to Metabolize Gluten Is Present in Humans from Birth
To investigate the capacity of the human GI tract to metabolize gluten from the first stages of life, we collected the earliest stool from 21 newborn children
Summary
Gluten is considered to be the mass that remains when wheat dough is washed to remove starch granules and water-soluble constituents [1]. Gluten includes proteins [1] (mainly gliadins and glutenins), and lipids (up to 10%) and some starches are present [2]. Pancreatic enzymes are firstly secreted as inactive precursors and are activated by the action of trypsin secreted by intestinal epithelial cells. Activated pancreatic enzymes convert proteins into free amino acids, which are absorbed by the cells of the intestinal wall [4]. Gluten proteins from wheat, barley, and rye cannot be completely hydrolyzed by human proteases due to the high proline content. Human gluten digestion generates large peptides (with 10 to >30 amino acid residues) that in celiac disease (CD) patients cross the small intestinal barrier and are deaminated by transglutaminase 2 [5]. In genetically-predisposed individuals expressing the human-leukocyte antigen (HLA)-DQ2.5 or DQ8, some of these peptides (such as the immunodominant 33-mer) trigger the inflammatory cascade of the autoimmune enteropathy known as celiac disease [6]
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