The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
Efficient degradation of gluten by a prolyl endoprotease in a gastrointestinal model: implications for coeliac disease
Abstract
BACKGROUND: Coeliac disease is caused by an immune response to gluten. As gluten proteins are proline rich they are resistant to enzymatic digestion in the gastrointestinal tract, a property that probably contributes to the immunogenic nature of gluten. AIMS: This study determined the efficiency of gluten degradation by a post-proline cutting enzyme, Aspergillus niger prolyl endoprotease (AN-PEP), in a dynamic system that closely mimics the human gastrointestinal tract (TIM system). METHODS: Two experiments were performed. In the first, a slice of bread was processed in the TIM system with and without co-administration of AN-PEP. In the second, a standard fast food menu was used. Samples of the digesting meals were taken from the stomach, duodenum, jejunum and ileum compartments at time zero until 4 hours after the start of the experiment. In these samples the levels of immunogenic peptides from gliadins and glutenins were assessed by monoclonal antibody-based competition assays, Western blot analysis and proliferation T-cell assays. RESULTS: AN-PEP accelerated the degradation of gluten in the stomach compartment to such an extent that hardly any gluten reached the duodenum compartment. CONCLUSION: AN-PEP is capable of accelerating the degradation of gluten in a gastrointestinal system that closely mimics in-vivo digestion. This implies that the co-administration of AN-PEP with a gluten-containing meal might eliminate gluten toxicity, thus offering patients the possibility of abandoning (occasionally) their strict gluten-free diet.
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Cites
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Structural Basis for Gluten Intolerance in Celiac Sprue
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Self-citationArentz-Hansen, H., Körner, R., Molberg, Ø., Quarsten, H., Vader, W., Kooy, Y. M. C., Lundin, K. E. A., Koning, F., Roepstorff, P., Sollid, L. M., et al. (2000) · The Journal of Experimental Medicine · doi:10.1084/jem.191.4.603 · Cited by 654
Self-citationAnderson, R. P., Degano, P., Godkin, A. J., Jewell, D. P., & Hill, A. V. S. (2000) · Nature Medicine · doi:10.1038/73200 · Cited by 578
Vader, W., Kooy, Y. M. C., van Veelen, P. A., de Ru, A., Harris, D. J., Benckhuijsen, W. E., Peña, A. S., Mearin, M. L., Drijfhout, J. W., & Koning, F. (2002) · Gastroenterology · doi:10.1053/gast.2002.33606 · Cited by 414
Self-citationIntestinal digestive resistance of immunodominant gliadin peptides
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Specificity of Tissue Transglutaminase Explains Cereal Toxicity in Celiac Disease
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Self-citationGLUTEN-INDUCED ENTEROPATHY THE EFFECT OF PARTIALLY DIGESTED GLUTEN
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Cited by
Ludvigsson, J. F., Bai, J. C., Biagi, F., Card, T. R., Ciacci, C., Ciclitira, P. J., Green, P. H. R., Hadjivassiliou, M., Holdoway, A., van Heel, D. A., et al. (2014) · Gut · doi:10.1136/gutjnl-2013-306578 · Cited by 1,116
Panel), E. P. O. G. M. O. (. (2010) · EFSA Journal · doi:10.2903/j.efsa.2010.1700 · Cited by 608
Celiac Disease: From Pathogenesis to Novel Therapies
Schuppan, D., Junker, Y., & Barisani, D. (2009) · Gastroenterology · doi:10.1053/j.gastro.2009.09.008 · Cited by 606
Di Sabatino, A., & Corazza, G. R. (2009) · The Lancet · doi:10.1016/s0140-6736(09)60254-3 · Cited by 555
New Clues in Celiac Disease Epidemiology, Pathogenesis, Clinical Manifestations, and Treatment
Lionetti, E., & Catassi, C. (2011) · International Reviews of Immunology · doi:10.3109/08830185.2011.602443 · Cited by 260
Metadata
- Authors
- Mitea, C., Havenaar, R., Drijfhout, J. W., Edens, L., Dekking, L., & Koning, F.
- Venue
- Gut
- Publisher
- BMJ
- Published
- 2007-05-14
- Volume
- 57
- Issue
- 1
- Pages
- 25-32
- ISSN
- 0017-5749 (ISSN-L)
- OpenAlex
- W2096941822
- Cited by
- 260
- References
- 32
- FWCI
- 13.09
- Type
- journal article
- Language
- en
- Open access
- closed
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