| Literature DB >> 12392549 |
Daniele Sblattero1, Fiorella Florian, Elisabetta Azzoni, Trevin Zyla, Min Park, Valentina Baldas, Tarcisio Not, Alessandro Ventura, Andrew Bradbury, Roberto Marzari.
Abstract
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.Entities:
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Year: 2002 PMID： 12392549 DOI： 10.1046/j.1432-1033.2002.03215.x
Source DB: PubMed Journal: Eur J Biochem ISSN： 0014-2956