Abstract
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.
Highlights
The enzyme type 2 transglutaminase (TG2) plays a key role in the pathogenesis of celiac disease (CD), primarily for its enzymatic activity that transforms common food proteins, i.e., gluten proteins contained in cereals, in unhealthy molecules for genetic predisposed individuals [1]
Auto-antibodies against TG2, abundantly produced at an early stage of Celiac disease (CD) development, have themselves a biological activity when interacting with TG2 on the cell surface and in the extra-cellular matrix (ECM) [3]
We have examined known or potential relationships between TG2, peptide 31-43 of the α-gliadin (P31-43) and antibodies to TG2, trying to highlight the thin thread connecting them in the molecular mechanism of CD pathogenesis
Summary
The enzyme type 2 transglutaminase (TG2) plays a key role in the pathogenesis of celiac disease (CD), primarily for its enzymatic activity that transforms common food proteins, i.e., gluten proteins contained in cereals, in unhealthy molecules for genetic predisposed individuals [1]. It is able to modulate TG2 activity and expression; in turn, TG2 may regulate some effects induced by P31-43. Auto-antibodies against TG2, abundantly produced at an early stage of CD development, have themselves a biological activity when interacting with TG2 on the cell surface and in the extra-cellular matrix (ECM) [3]. In some cases, they are able to modulate effects produced by P31-43 stimulation [3]. We have examined known or potential relationships between TG2, P31-43 and antibodies to TG2, trying to highlight the thin thread connecting them in the molecular mechanism of CD pathogenesis
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