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Article

Tissue Transglutaminase but Not Microbial Transglutaminase Is Inhibited by Exogenous Oxidative Substances in Celiac Disease

1
Department of Pediatrics, Justus-Liebig-University Giessen, 35392 Giessen, Germany
2
Institute of Nutritional Science, Justus-Liebig-University Giessen, 35392 Giessen, Germany
*
Author to whom correspondence should be addressed.
Academic Editors: Maria Vittoria Barone and Salvatore Auricchio
Int. J. Mol. Sci. 2022, 23(4), 2248; https://doi.org/10.3390/ijms23042248
Received: 27 January 2022 / Revised: 14 February 2022 / Accepted: 15 February 2022 / Published: 17 February 2022
(This article belongs to the Special Issue Pro-inflammatory Nutrients: Focus on Gliadin and Celiac Disease 2.0)
Enzymatic modification of gliadin peptides by human transglutaminase 2 (TG2) is a central step in celiac disease (CD) pathogenesis. Microbial transglutaminase (mTG) mimics the enzymatic function of TG2 and might play a role in CD. TG2 is inhibited by endogenous oxidative endoplasmic reticulum-resident protein 57 (ERp57), but data about mTG are lacking. We investigated the localization of ERp57 in duodenal biopsies and examined inhibition of TG2, and mTG by competitive, and oxidative molecules. Localization of ERp57 was investigated in duodenal biopsies from CD, and control patients by electron microcopy. Inhibition of TG2 and mTG was analyzed on an in vitro level using a photometric assay. ERp57 was observed within the lamina propria and its abundance within the endoplasmic reticulum (ER) was reduced in CD patients. TG2 was oxidatively inhibited by up to 95% by PX12 (p < 0.001) and L-cystine (p < 0.001), whereas mTG remained unaffected. The reduced presence of ERp57 within the ER of CD biopsies suggests a regulatory function of this protein within CD pathogenesis. PX12 and L-cystine oxidatively inhibit TG2 and might serve as treatment options in CD. mTG is poorly regulated and could contribute to the accumulation of immunogenic peptides within the gut with potential pathogenic effects. View Full-Text
Keywords: celiac disease; transglutaminase 2; microbial transglutaminase; TG2 inhibitor; ERp57 celiac disease; transglutaminase 2; microbial transglutaminase; TG2 inhibitor; ERp57
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MDPI and ACS Style

Stricker, S.; Rudloff, S.; De Laffolie, J.; Zimmer, K.-P. Tissue Transglutaminase but Not Microbial Transglutaminase Is Inhibited by Exogenous Oxidative Substances in Celiac Disease. Int. J. Mol. Sci. 2022, 23, 2248. https://doi.org/10.3390/ijms23042248

AMA Style

Stricker S, Rudloff S, De Laffolie J, Zimmer K-P. Tissue Transglutaminase but Not Microbial Transglutaminase Is Inhibited by Exogenous Oxidative Substances in Celiac Disease. International Journal of Molecular Sciences. 2022; 23(4):2248. https://doi.org/10.3390/ijms23042248

Chicago/Turabian Style

Stricker, Sebastian, Silvia Rudloff, Jan De Laffolie, and Klaus-Peter Zimmer. 2022. "Tissue Transglutaminase but Not Microbial Transglutaminase Is Inhibited by Exogenous Oxidative Substances in Celiac Disease" International Journal of Molecular Sciences 23, no. 4: 2248. https://doi.org/10.3390/ijms23042248

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