Molecular dissection of the tissue transglutaminase autoantibody response in celiac disease

R. Marzari, D. Sblattero, F. Florian, E. Tongiorgi, T. Not, A. Tommasini, A. Ventura, A. Bradbury

Research output: Contribution to journalArticlepeer-review

Abstract

Celiac disease (CD) is an intestinal malabsorption characterized by intolerance to cereal proteins accompanied by immunological responses to dietary gliadins and tissue transglutaminase, an autoantigen located in the endomysium. Tissue transglutaminase belongs to the family of enzymes that catalyze protein cross-linking reactions and is constitutively expressed in many tissues as well as being activated during apoptosis. The role of gliadins in eliciting the immune response in CD and how transglutaminase is linked to the primary reaction are still unclear. In this work, we report the production and analysis of six phage Ab libraries from the peripheral and intestinal lymphocytes of three CD patients. We were able to isolate Abs to transglutaminase from all intestinal lymphocytes libraries but not from those obtained from peripheral lymphocytes. This is in contrast to Abs against gliadin, which could be obtained from all libraries, indicating that the humoral response against transglutaminase occurs at the local level, whereas that against gliadin occurs both peripherally and centrally. Abs from all three patients recognized the same transglutaminase epitopes with a bias toward the use of the VH5 Ab variable region family. The possible role of these anti-transglutaminase Abs in the onset of CD and associated antoimmune pathologies is discussed.

Original languageEnglish
Pages (from-to)4170-4176
Number of pages7
JournalJournal of Immunology
Volume166
Issue number6
Publication statusPublished - Mar 15 2001

ASJC Scopus subject areas

  • Immunology

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