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Mol Metab. 2017 May 22;6(7):693-702. doi: 10.1016/j.molmet.2017.05.008. eCollection 2017 Jul.

The human digestive tract has proteases capable of gluten hydrolysis.

Author information

1
Departamento de Biología Molecular, Área de Bioquímica y Biología Molecular, Universidad de León, Facultad de Veterinaria, 24071 León, Spain.
2
Instituto de Biología Molecular, Genómica y Proteómica (INBIOMIC), Universidad de León, Spain.
3
Departamento de Biología Molecular, Área de Microbiología, Universidad de León, Facultad de Ciencias Biológicas y Ambientales, 24071 León, Spain.
4
Departamento de Gastroenterología, Hospital Universitario de León, 24008 Léon, Spain.
5
Instituto de Biomedicina (IBIOMED), Universidad de León, Spain.

Abstract

OBJECTIVE:

To identify, purify, and characterize the proteins responsible for glutenase activity in the feces of healthy subjects and patients with celiac disease (CD).

METHODS:

Sixteen 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.

RESULTS:

The 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.

CONCLUSION:

The 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.

KEYWORDS:

ATIs, α-Amylase/trypsin inhibitors; CBPA1, human carboxypeptidase A1; CD, celiac disease; CEL2A, gastrointestinal elastase 2A; CEL3B, gastrointestinal elastase 3B; Celiac disease; Gliadin; Gliadinase activity; Gluten; Glutenase fecal activity; HLA-DQ, human leukocyte antigen; LPLC, low-performance liquid chromatography; NCD, non-celiac-disease

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