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Processed Food Additive Microbial Transglutaminase and Its Cross-Linked Gliadin Complexes Are Potential Public Health Concerns in Celiac Disease
Open AccessArticle

Constitutive Differential Features of Type 2 Transglutaminase in Cells Derived from Celiac Patients and from Healthy Subjects

1
Department of Chemistry and Biology, University of Salerno, 84084 Fisciano, Italy
2
Department of Translational Medical Science, University Federico II, 80138 Naples, Italy
3
European Laboratory for the Investigation of Food-Induced Diseases (ELFID), University Federico II, 80138 Naples, Italy
*
Author to whom correspondence should be addressed.
These authors equally contributed to the work.
Int. J. Mol. Sci. 2020, 21(4), 1231; https://doi.org/10.3390/ijms21041231
Received: 17 January 2020 / Revised: 7 February 2020 / Accepted: 10 February 2020 / Published: 12 February 2020
Type 2 transglutaminase (TG2) is a ubiquitous enzyme able to modify gliadin peptides introduced into the organism through the diet. By means of its catalytic activity, TG2 seems to have an important pathogenetic role in celiac disease (CD), an inflammatory intestinal disease caused by the ingestion of gluten-containing cereals. A strong autoimmune response to TG2 characterizes CD development. Anti-TG2 antibodies specifically derange the uptake of the α-gliadin peptide 31–43 by control, but not by celiac dermal fibroblasts, underlying some different constitutive features regarding TG2 in healthy and celiac subjects. Our aim was to investigate whether these differences depended on a different TG2 subcellular distribution and whether peptide 31–43 differentially regulated TG2 expression and activity in cells of the two groups of subjects. We found that TG2 was more abundantly associated with membranes of celiac fibroblasts than of control cells, in particular with the early endosomal and autophagic compartments. We also found that peptide 31–43 differentially affected TG2 expression and activity in the two groups of cells, activating TG2 more in control than in celiac cells and inducing TG2 expression in celiac cells, but not in control ones. The different TG2 subcellular localization and the different way the peptide 31–43 modulates TG2 activity and availability into control and CD cells suggested that TG2 is involved in the definition of a constitutive CD cellular phenotype, thus having an important and still undefined role in CD pathogenesis. View Full-Text
Keywords: type 2 transglutaminase; celiac disease; gliadin peptide 31–43; celiac cellular phenotype; skin-derived fibroblasts type 2 transglutaminase; celiac disease; gliadin peptide 31–43; celiac cellular phenotype; skin-derived fibroblasts
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Paolella, G.; Nanayakkara, M.; Sposito, S.; Lepretti, M.; Auricchio, S.; Esposito, C.; Barone, M.V.; Martucciello, S.; Caputo, I. Constitutive Differential Features of Type 2 Transglutaminase in Cells Derived from Celiac Patients and from Healthy Subjects. Int. J. Mol. Sci. 2020, 21, 1231.

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