Celiac anti-tissue transglutaminase antibodies interfere with the uptake of alpha gliadin peptide 31–43 but not of peptide 57–68 by epithelial cells

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• 作者：Ivana Caputo ; Maria Vittoria Barone ; Marilena Lepretti ; Stefania Martucciello ; Ivan Nista ; Riccardo Troncone ; Salvatore Auricchio ; Daniele Sblattero ; Carla Esposito
• 关键词：Transglutaminase ; Anti-transglutaminase antibody ; Gliadin peptide ; Celiac disease ; Endocytosis
• 刊名：Biochimica et Biophysica Acta (BBA)/Molecular Basis of Disease
• 出版年：2010
• 出版时间：September 2010
• 年：2010
• 卷：1802
• 期：9
• 页码：717-727
• 全文大小：1921 K

文摘

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.