What is it about?
Gliadin is a protein present in wheat gluten that is not fully degraded during human digestion. The remaining large undigested peptides produce diverse diseases affecting around 5% of the general population. In general, the complicated relationship between food properties, behavior during digestion, and their contribution to human nutrition and health are not well understood. Here, we present the first evaluation of pepsin gliadin digest (p-gliadin) using a physicochemical approach combined with a screening panel of inflammatory biomarkers related to Celiac Disease (CeD) in the Caco-2 cell line. We found that the p-gliadin system behaves as a self-organized solution composed of oligomers and fibrils, which triggers the up-regulation of the mRNA of pro-apoptotic, chemoattractive, inflammatory, and permeability CeD related genes in the Caco-2 cell line.
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Why is it important?
Our findings led us to suggest that p-gliadin peptide supramolecular structures' interaction with the epithelial barrier could be responsible for the early tissue inflammatory response observed in CeD. In conclusion, it is revealed p-gliadin supramolecular structures' pathological role in the human epithelial cellular model, opening avenues to nutritional or therapeutic strategies to modulate the observed aggregation process.
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This page is a summary of: Pepsin Digest of Gliadin Forms Spontaneously Amyloid‐Like Nanostructures Influencing the Expression of Selected Pro‐Inflammatory, Chemoattractant, and Apoptotic Genes in Caco‐2 Cells: Implications for Gluten‐Related Disorders, Molecular Nutrition & Food Research, June 2021, Wiley, DOI: 10.1002/mnfr.202100200.
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