COMMENTARY

Inflammatory bowel disease

Transglutaminases: new target molecules for inflammatory bowel disease?

B Siegmund, M Zeitz

Charité Universitätsmedizin Berlin, Campus Benjamin Franklin, Medizinische Klinik I, Berlin, Germany

Correspondence to:
Correspondence to:
Dr B Siegmund
Charité Universitätsmedizin Berlin, Campus Benjamin Franklin, Medizinische Klinik I, Hindenburgdamm 30, 12200 Berlin, Germany; britta.siegmund@charite.de

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Transglutaminases may be involved in intestinal inflammation and may even represent therapeutic targets for ulcerative colitis

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Keywords: transglutaminases; colon; keratinocyte; ulcerative colitis; intestinal inflammation; inflammatory bowel disease

The first 150 words of the full text of this article appear below.

The family of transglutaminases (TG) includes the plasma form factor XIIIa as well as the tissue transglutaminase (tTG) and keratinocyte transglutaminase (TGk). In particular, tTG reminds every gastroenterologist primarily of coeliac disease where tTG represents the key autoantigen.¹ Disease induction is confined to tTG, a ubiquitous enzyme which is released from fibroblasts, endothelial, and inflammatory cells during mechanical irritation or inflammation. At acidic pH, which occurs with inflammation, tTG can, apart from its physiological function described in more detail below, also simply deamidate some of the glutamine residues of the gluten peptides. In coeliac disease, deamidation introduces a negative charge into the gluten peptides which can increase the binding affinity to HLA-DQ2 or HLA-DQ8, the primary HLA association in coeliac disease. Binding of gluten peptide to either HLA-DQ2 or HLA-DQ8 results in an increase in their capacity to stimulate T cells, thus inducing intestinal inflammation.^2,3

As indicated . . . [Full text of this article]

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