Open AccessThe analysis of the fine specificity of celiac disease antibodies using tissue transglutaminase fragments
Author(s) -
Sblattero Daniele,
Florian Fiorella,
Azzoni Elisabetta,
Zyla Trevin,
Park Min,
Baldas Valentina,
Not Tarcisio,
Ventura Alessandro,
Bradbury Andrew,
Marzari Roberto
Publication year - 2002
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1033.2002.03215.x
Subject(s) - tissue transglutaminase , antibody , malabsorption , enzyme , biology , disease , microbiology and biotechnology , immunology , biochemistry , medicine , pathology , endocrinology
Celiac disease is an intestinal malabsorption characterized by an intolerance to cereal proteins accompanied by immunological responses to dietary gliadins and an autoantigen located in the endomysium. The latter has been identified as the enzyme tissue transglutaminase which belongs to a family of enzymes that catalyze protein cross‐linking reactions and is constitutively expressed in many tissues as well as being activated during apoptosis. In a recent paper, we described the selection and characterization of anti‐transglutaminase Igs from phage antibody libraries created from intestinal lymphocytes from celiac disease patients. In this work, using transglutaminase gene fragments, we identify a region of tissue transglutaminase recognized by these antibodies as being conformational and located in the core domain of the enzyme. This is identical to the region recognized by anti‐transglutaminase Igs found in the serum of celiac disease patients.