{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,18]],"date-time":"2026-08-18T00:49:31Z","timestamp":1787014171627,"version":"build-2736575974"},"reference-count":31,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2020,2,21]],"date-time":"2020-02-21T00:00:00Z","timestamp":1582243200000},"content-version":"vor","delay-in-days":20,"URL":"http:\/\/creativecommons.org\/licenses\/by-nc\/4.0\/"}],"funder":[{"name":"University of Oslo, department of Dentistry"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["European J Oral Sciences"],"published-print":{"date-parts":[[2020,2]]},"abstract":"<jats:p>Previously we detected increased levels of IgA to the enamel matrix protein amelogenin in children with untreated coeliac disease (CeD). The biological impact of autoantibodies to amelogenin may depend on which part of the amelogenin (epitopes) they bind. Sera or blood samples from 146 untreated children with CeD from two different cohorts and 25 non\u2010CeD control children were tested for IgA anti\u2010amelogenin (Emdogain) reactivity. The 32 CeD children and six controls with the highest reactivity were selected for detailed IgA anti\u2010amelogenin (AMELX) epitope mapping using 31 overlapping, 10\u201322mer peptides in ELISA. The dominating reactivity were to six peptides in a 75\u2010amino\u2010acid (aa)\u2010long central segment (aa 75\u2013150) containing enzymatic cleavage sites for matrix metalloproteinase 20 (MMP\u201020) and kallikrein\u2010related peptidase 4 (KLK\u20104) and to two N\u2010terminal peptides (aa 13\u201341) included in the tyrosine\u2010rich amelogenin peptide fragment, which is important for self\u2010assembly. Only two of the six control children reacted to single, but different peptides. Solid\u2010phase extraction with gliadin\u2010 and Emdogain\u2010coated Sepharose revealed a gliadin cross\u2010reactive central region and a putative conformation\u2010dependent, apparently non\u2010cross\u2010reactive N\u2010terminal region. High IgA anti\u2010amelogenin reactivity may interfere with normal amelogenesis by inhibiting amelogenin self\u2010assembly, amelogenin\u2010hydroxyapatite interaction, and\/or enzymatic degradation.<\/jats:p>","DOI":"10.1111\/eos.12672","type":"journal-article","created":{"date-parts":[[2020,2,21]],"date-time":"2020-02-21T13:45:05Z","timestamp":1582292705000},"page":"27-36","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["Epitope mapping of anti\u2010amelogenin IgA in coeliac disease"],"prefix":"10.1111","volume":"128","author":[{"given":"Sanja","family":"Petronijevic","sequence":"first","affiliation":[{"name":"Institute of Oral Biology Faculty of Dentistry University of Oslo Oslo Norway"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Solveig","family":"Stig","sequence":"additional","affiliation":[{"name":"Institute of Oral Biology Faculty of Dentistry University of Oslo Oslo 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