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Possible association between celiac disease and bacterial transglutaminase in food processing: a hypothesis
The incidence of celiac disease is increasing worldwide, and human tissue transglutaminase has long been considered the autoantigen of celiac disease. Concomitantly, the food industry has introduced ingredients such as microbial transglutaminase, which acts as a food glue, thereby revolutionizing fo...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4502714/ https://www.ncbi.nlm.nih.gov/pubmed/26084478 http://dx.doi.org/10.1093/nutrit/nuv011 |
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author | Lerner, Aaron Matthias, Torsten |
author_facet | Lerner, Aaron Matthias, Torsten |
author_sort | Lerner, Aaron |
collection | PubMed |
description | The incidence of celiac disease is increasing worldwide, and human tissue transglutaminase has long been considered the autoantigen of celiac disease. Concomitantly, the food industry has introduced ingredients such as microbial transglutaminase, which acts as a food glue, thereby revolutionizing food qualities. Several observations have led to the hypothesis that microbial transglutaminase is a new environmental enhancer of celiac disease. First, microbial transglutaminase deamidates/transamidates glutens such as the endogenous human tissue transglutaminase. It is capable of crosslinking proteins and other macromolecules, thereby changing their antigenicity and resulting in an increased antigenic load presented to the immune system. Second, it increases the stability of protein against proteinases, thus diminishing foreign protein elimination. Infections and the crosslinked nutritional constituent gluten and microbial transglutaminase increase the permeability of the intestine, where microbial transglutaminases are necessary for bacterial survival. The resulting intestinal leakage allows more immunogenic foreign molecules to induce celiac disease. The increased use of microbial transglutaminase in food processing may promote celiac pathogenesis ex vivo, where deamidation/transamidation starts, possibly explaining the surge in incidence of celiac disease. If future research substantiates this hypothesis, the findings will affect food product labeling, food additive policies of the food industry, and consumer health education. |
format | Online Article Text |
id | pubmed-4502714 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-45027142015-09-01 Possible association between celiac disease and bacterial transglutaminase in food processing: a hypothesis Lerner, Aaron Matthias, Torsten Nutr Rev Special Articles The incidence of celiac disease is increasing worldwide, and human tissue transglutaminase has long been considered the autoantigen of celiac disease. Concomitantly, the food industry has introduced ingredients such as microbial transglutaminase, which acts as a food glue, thereby revolutionizing food qualities. Several observations have led to the hypothesis that microbial transglutaminase is a new environmental enhancer of celiac disease. First, microbial transglutaminase deamidates/transamidates glutens such as the endogenous human tissue transglutaminase. It is capable of crosslinking proteins and other macromolecules, thereby changing their antigenicity and resulting in an increased antigenic load presented to the immune system. Second, it increases the stability of protein against proteinases, thus diminishing foreign protein elimination. Infections and the crosslinked nutritional constituent gluten and microbial transglutaminase increase the permeability of the intestine, where microbial transglutaminases are necessary for bacterial survival. The resulting intestinal leakage allows more immunogenic foreign molecules to induce celiac disease. The increased use of microbial transglutaminase in food processing may promote celiac pathogenesis ex vivo, where deamidation/transamidation starts, possibly explaining the surge in incidence of celiac disease. If future research substantiates this hypothesis, the findings will affect food product labeling, food additive policies of the food industry, and consumer health education. Oxford University Press 2015-08 2015-06-16 /pmc/articles/PMC4502714/ /pubmed/26084478 http://dx.doi.org/10.1093/nutrit/nuv011 Text en © The Author(s) 2015. Published by Oxford University Press on behalf of the International Life Sciences Institute. http://creativecommons.org/licenses/by-nc-nd/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs licence (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial reproduction and distribution of the work, in any medium, provided the original work is not altered or transformed in any way, and that the work is properly cited. For commercial re-use, please contact journals.permissions@oup.com |
spellingShingle | Special Articles Lerner, Aaron Matthias, Torsten Possible association between celiac disease and bacterial transglutaminase in food processing: a hypothesis |
title | Possible association between celiac disease and bacterial transglutaminase in food processing: a hypothesis |
title_full | Possible association between celiac disease and bacterial transglutaminase in food processing: a hypothesis |
title_fullStr | Possible association between celiac disease and bacterial transglutaminase in food processing: a hypothesis |
title_full_unstemmed | Possible association between celiac disease and bacterial transglutaminase in food processing: a hypothesis |
title_short | Possible association between celiac disease and bacterial transglutaminase in food processing: a hypothesis |
title_sort | possible association between celiac disease and bacterial transglutaminase in food processing: a hypothesis |
topic | Special Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4502714/ https://www.ncbi.nlm.nih.gov/pubmed/26084478 http://dx.doi.org/10.1093/nutrit/nuv011 |
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