Next Article in Journal
Synthesis, Properties, and Biodegradation of Sequential Poly(Ester Amide)s Containing γ-Aminobutyric Acid
Previous Article in Journal
Sonic Hedgehog and Triiodothyronine Pathway Interact in Mouse Embryonic Neural Stem Cells
Previous Article in Special Issue
Microbial Transglutaminase as a Tool to Improve the Features of Hydrocolloid-Based Bioplastics
Open AccessReview

Interplay between Type 2 Transglutaminase (TG2), Gliadin Peptide 31-43 and Anti-TG2 Antibodies in Celiac Disease

1
Department of Chemistry and Biology, University of Salerno, 84084 Fisciano (SA), Italy
2
European Laboratory for the Investigation of Food-Induced Diseases (ELFID), University of Salerno, 84084 Fisciano (SA), Italy
*
Author to whom correspondence should be addressed.
These authors contributed equally to the work.
Int. J. Mol. Sci. 2020, 21(10), 3673; https://doi.org/10.3390/ijms21103673 (registering DOI)
Received: 28 April 2020 / Revised: 20 May 2020 / Accepted: 20 May 2020 / Published: 23 May 2020
Celiac disease (CD) is a common intestinal inflammatory disease involving both a genetic background and environmental triggers. The ingestion of gluten, a proteic component of several cereals, represents the main hexogen factor implied in CD onset that involves concomitant innate and adaptive immune responses to gluten. Immunogenicity of some gluten sequences are strongly enhanced as the consequence of the deamidation of specific glutamine residues by type 2 transglutaminase (TG2), a ubiquitous enzyme whose expression is up-regulated in the intestine of CD patients. A short gluten sequence resistant to intestinal proteases, the α-gliadin peptide 31-43, seems to modulate TG2 function in the gut; on the other hand, the enzyme can affect the biological activity of this peptide. In addition, an intense auto-immune response towards TG2 is a hallmark of CD. Auto-antibodies exert a range of biological effects on several cells, effects that in part overlap with those induced by peptide 31-43. In this review, we delineate a scenario in which TG2, anti-TG2 antibodies and peptide 31-43 closely relate to each other, thus synergistically participating in CD starting and progression. View Full-Text
Keywords: type 2 transglutaminase; celiac disease; anti-TG2 antibodies; gliadin peptide31-43 type 2 transglutaminase; celiac disease; anti-TG2 antibodies; gliadin peptide31-43
Show Figures

Figure 1

MDPI and ACS Style

Martucciello, S.; Sposito, S.; Esposito, C.; Paolella, G.; Caputo, I. Interplay between Type 2 Transglutaminase (TG2), Gliadin Peptide 31-43 and Anti-TG2 Antibodies in Celiac Disease. Int. J. Mol. Sci. 2020, 21, 3673.

Show more citation formats Show less citations formats
Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Article Access Map by Country/Region

1
Search more from Scilit
 
Search
Back to TopTop