Interplay between Type 2 Transglutaminase (TG2), Gliadin Peptide 31-43 and Anti-TG2 Antibodies in Celiac Disease
<b> </b>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...
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doaj-49337f2d3be74047830b357a8aecfef92020-11-25T03:05:36ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672020-05-01213673367310.3390/ijms21103673Interplay between Type 2 Transglutaminase (TG2), Gliadin Peptide 31-43 and Anti-TG2 Antibodies in Celiac DiseaseStefania Martucciello0Silvia Sposito1Carla Esposito2Gaetana Paolella3Ivana Caputo4Department of Chemistry and Biology, University of Salerno, 84084 Fisciano, ItalyEuropean Laboratory for the Investigation of Food-Induced Diseases (ELFID), University of Salerno, 84084 Fisciano, ItalyDepartment of Chemistry and Biology, University of Salerno, 84084 Fisciano, ItalyDepartment of Chemistry and Biology, University of Salerno, 84084 Fisciano, ItalyDepartment of Chemistry and Biology, University of Salerno, 84084 Fisciano, Italy<b> </b>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.https://www.mdpi.com/1422-0067/21/10/3673type 2 transglutaminaseceliac diseaseanti-TG2 antibodiesgliadin peptide31-43 |
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DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Stefania Martucciello Silvia Sposito Carla Esposito Gaetana Paolella Ivana Caputo |
spellingShingle |
Stefania Martucciello Silvia Sposito Carla Esposito Gaetana Paolella Ivana Caputo Interplay between Type 2 Transglutaminase (TG2), Gliadin Peptide 31-43 and Anti-TG2 Antibodies in Celiac Disease International Journal of Molecular Sciences type 2 transglutaminase celiac disease anti-TG2 antibodies gliadin peptide31-43 |
author_facet |
Stefania Martucciello Silvia Sposito Carla Esposito Gaetana Paolella Ivana Caputo |
author_sort |
Stefania Martucciello |
title |
Interplay between Type 2 Transglutaminase (TG2), Gliadin Peptide 31-43 and Anti-TG2 Antibodies in Celiac Disease |
title_short |
Interplay between Type 2 Transglutaminase (TG2), Gliadin Peptide 31-43 and Anti-TG2 Antibodies in Celiac Disease |
title_full |
Interplay between Type 2 Transglutaminase (TG2), Gliadin Peptide 31-43 and Anti-TG2 Antibodies in Celiac Disease |
title_fullStr |
Interplay between Type 2 Transglutaminase (TG2), Gliadin Peptide 31-43 and Anti-TG2 Antibodies in Celiac Disease |
title_full_unstemmed |
Interplay between Type 2 Transglutaminase (TG2), Gliadin Peptide 31-43 and Anti-TG2 Antibodies in Celiac Disease |
title_sort |
interplay between type 2 transglutaminase (tg2), gliadin peptide 31-43 and anti-tg2 antibodies in celiac disease |
publisher |
MDPI AG |
series |
International Journal of Molecular Sciences |
issn |
1661-6596 1422-0067 |
publishDate |
2020-05-01 |
description |
<b> </b>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. |
topic |
type 2 transglutaminase celiac disease anti-TG2 antibodies gliadin peptide31-43 |
url |
https://www.mdpi.com/1422-0067/21/10/3673 |
work_keys_str_mv |
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