Rapid CommunicationsAutoantibodies to tissue transglutaminase as predictors of celiac disease☆,☆☆
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Patients
A total of 106 serum samples from untreated celiac patients (71 female and 35 male) were examined. The patients had different clinical and histopathologic degrees of severity (malabsorption or partial or subtotal villous atrophy) and responded with clinical improvement to gluten withdrawal. The mean age was 32.6 years, ranging from 4 to 80 years. In addition, serum samples from 43 celiac patients (34 female and 9 male; age, 7–79 years; mean age, 34.3 years) consuming a gluten-free diet for 6–12
Results
An ELISA based on serum IgA autoantibodies against tTG was performed; the results are summarized in Table 2. The ELISA procedure was improved from the protocol used in our previous study.9 Blocking with bovine serum albumin was avoided because some serum samples from patients with celiac disease and controls showed antibodies against this food component, therefore possibly falsifying the results. Also, the addition of calcium to the coating buffer was mandatory to improve the sensitivity of the
Discussion
We used an ELISA based on tTG, the recently discovered endomysial autoantigen in celiac disease, to determine (1) the extent to which detectable IgA anti-tTG was predictive of a positive EMA test result by immunofluorescent examination and (2) to establish the titers of IgA anti-tTG in serum samples from patients with celiac disease and from various controls.
Collectively, IgA anti-tTG titers showed a good correlation with EMA titers, reaching a sensitivity of 98.1% and a specificity of 94.7%.
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2022, Clinica Chimica ActaCitation Excerpt :According to research, tTG is not only a diagnostic marker for CD, but it also plays a role in the disease's etiology [38]. tTG may aggravate the inflammatory process in CD patients by damaging the extracellular villous matrix and acting as a target for intestinal villous epithelial cells to be destroyed [39]. Indeed, the aforementioned reactions are significant, first, tTG may eliminate particular glutamine residues from immunogenic gliadin peptides, resulting in epitopes with a higher affinity for DQ2 [40,41].
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Address requests for reprints to: Detlef Schuppan, M.D., Ph.D., Medizinische Klinik I, University of Erlangen-Nürnberg, Krankenhausstrasse 12, 91054 Erlangen, Germany. e-mail: [email protected]; fax: (49) 9131-8536003.
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Supported by grants SFB 366 C5 and Schu 646/4-1 from the Deutsche Forschungsgesellschaft and by a grant from the German Celiac Society.