Abstract
Healthy reticulin- and endomysium-antibody-positive first-degree relatives of coeliac disease (CD) patients, irrespective of the appearance of the small-bowel mucosa, are genetically similar to known CD patients (Lancet 1991;338:1350-53). Recently we identified human noncollagenous extracellular matrix proteins to be targets for these antibodies (Lancet 1991;338:724-25). We now hypothesised fibroblasts to synthesise and secrete CD-specific autoantigens. A human embryonic fibroblast cell line, found to stain positively with CD patient sera IgA, was cultured for 4 days with tritiated amino acids. The fibroblasts synthesised and secreted a large-molecular-weight protein complex reacting with the IgA. The protein complex, separated using HPLC gel filtration, was decomposed and nine different protein molecules (17-39 kD) with 3H activity was detected, four of which reacted with CD patient sera IgA. In affinity chromatography these molecules bound to reticulin and endomysium antibodies but not to gliadin antibodies. The fibroblast-derived proteins and the formed autoantibodies may be important in the pathogenesis of CD. We hypothesise a gliadin-triggered autoimmune mechanism to be operative.
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Mäki, M., Marttinen, A. & Visakorpi, J. FIBROBLAST-DERIVED HUMAN PROTEINS ARE TARGETS FOR GENETICALLY DETERMINED RETICULIN AND ENDOMYSIUM AUTOANTIBODIES. Pediatr Res 35, 41 (1994). https://doi.org/10.1203/00006450-199402000-00071
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DOI: https://doi.org/10.1203/00006450-199402000-00071