ArticleMolecular metabolism2017
The human digestive tract has proteases capable of gluten hydrolysis.
Article in Molecular metabolism, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 47 citations in OpenAlex.
- Psychiatric Symptoms Associated with Non-Celiac Gluten Sensitivity: A Focused Narrative Review.Nutrients · 2026Review
- 3D-Printable Sustainable Bioplastics from Gluten and Keratin.Gels (Basel, Switzerland) · 2024Article
- Acute Developmental Toxicity of Panax notoginseng in Zebrafish Larvae.Chinese journal of integrative medicine · 2023Article
- Biomarkers to Monitor Adherence to Gluten-Free Diet by Celiac Disease Patients: Gluten Immunogenic Peptides and Urinary miRNAs.Foods (Basel, Switzerland) · 2022Review
- Characterization ofFrontiers in cellular and infection microbiology · 2022Article
- Faecal proteome in clinically healthy dogs and cats: Findings in pooled faeces from 10 cats and 10 dogs.Veterinary record open · 2021Article
- Gliadin proteolytical resistant peptides: the interplay between structure and self-assembly in gluten-related disorders.Biophysical reviews · 2021Review
- Characterization ofFoods (Basel, Switzerland) · 2021Article
- New Insights into Non-Dietary Treatment in Celiac Disease: Emerging Therapeutic Options.Nutrients · 2021Review
- Probiotic Potential and Gluten Hydrolysis Activity of Lactobacillus brevis KT16-2.Probiotics and antimicrobial proteins · 2021Article
- Gluten-degrading bacteria: availability and applications.Applied microbiology and biotechnology · 2021Review
- The Human Digestive Tract Is Capable of Degrading Gluten from Birth.International journal of molecular sciences · 2020Article
- The Janus Face of Cereals: Wheat-Derived Prebiotics Counteract the Detrimental Effect of Gluten on Metabolic Homeostasis in Mice Fed a High-Fat/High-Sucrose Diet.Molecular nutrition & food research · 2019Article
- The Gut Microbiota in Celiac Disease and probiotics.Nutrients · 2019Review
- Article
- Cathepsins: Proteases that are vital for survival but can also be fatal.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2018Review
- S9A Serine Protease Engender Antigenic Gluten Catabolic Competence to the Human Gut Microbe.Indian journal of microbiology · 2018Article
- Gluten, Inflammation, and Neurodegeneration.American journal of lifestyle medicineArticle
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
objectiveTo identify, purify, and characterize the proteins responsible for glutenase activity in the feces of healthy subjects and patients with celiac disease (CD).
methodsSixteen subjects were included in this study; 8 were healthy with no known food intolerances, and 8 were treated CD patients on a gluten-free diet. Fecal samples were homogenized, and precipitated proteins were purified by chromatography. Glutenase activity was evaluated by bioassays, zymography, and high-performance liquid chromatography with immunogenic 33-mer, 19-mer, and 13-mer gliadin peptides.
resultsThe gastrointestinal elastase 3B (CEL3B), elastase 2A (CEL2A), and carboxypeptidase A1 (CBPA1) enzymes degraded human gluten. These proteins fully hydrolyzed 13-mer and 19-mer gliadin peptides that trigger immune-mediated enteropathy in individuals genetically predisposed to CD and partially digested a 33-mer. Feces from patients with CD showed more glutenase activity than feces from individuals without CD (171-466% higher). Peptidase activity against the gliadin peptides also increased in patients with CD.
conclusionThe digestive tracts of patients with CD and healthy subjects have enzymatic machinery needed for gluten degradation. Patients with CD showed more gluten hydrolysis than did healthy individuals, although, in both cases, a fraction of 33-mer peptide remained intact. Gliadin peptides derived from gastrointestinal digestion, especially the 33-mer, can potentially be used by commensal microbiota from both CD-positive and CD-negative individuals, and differences in bacterial hydrolysis can modify its immunogenic capacity.
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