Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8261844 | Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease | 2010 | 11 Pages |
Abstract
Celiac disease is characterized by the secretion of IgA-class autoantibodies that target tissue transglutaminase (tTG). It is now recognized that anti-tTG antibodies are functional and not mere bystanders in the pathogenesis of celiac disease. Here we report that interaction between anti-tTG antibodies and extracellular membrane-bound tTG inhibits peptide 31-43 (but not peptide 57-68) uptake by cells, thereby impairing the ability of p31-43 to drive Caco-2 cells into S-phase. This effect did not involve tTG catalytic activity. Because anti-tTG antibodies interfered with epidermal growth factor endocytosis, we assume that they exert their effect by reducing peptide 31-43 endocytosis. Our results suggest that cell-surface tTG plays a hitherto unknown role in the regulation of gliadin peptide uptake and endocytosis.
Keywords
Gliadin peptidePBSFBSAnti-transglutaminase antibodyM-β-CDERKTTGMDCEGFPFAEndocytosisBrdUbromodeoxyuridineCeliac diseaseTransglutaminaseTissue transglutaminasefetal bovine serumepidermal growth factormethyl-β-cyclodextrinPhosphate-buffered salineMonodansylcadaverineparaformaldehydeextracellular signal-regulated kinase
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Authors
Ivana Caputo, Maria Vittoria Barone, Marilena Lepretti, Stefania Martucciello, Ivan Nista, Riccardo Troncone, Salvatore Auricchio, Daniele Sblattero, Carla Esposito,