Rapid disruption of intestinal barrier function by gliadin involves altered expression of apical junctional proteins
作者： Guy R. Sander , Adrian G. Cummins , Barry C. Powell
DOI: 10.1016/J.FEBSLET.2005.07.066
关键词: Coeliac disease 、 Gliadin 、 Barrier function 、 Tight junction 、 Cell biology 、 Caco-2 、 Adherens junction 、 Biochemistry 、 Biology 、 Occludin 、 Actin
摘要: Coeliac disease is a chronic enteropathy caused by the ingestion of wheat gliadin and other cereal prolamines derived from rye barley. In present work, we investigated mechanisms underlying altered barrier function properties exerted gliadin-derived peptides in human Caco-2 intestinal epithelial cells. We demonstrate that alters almost immediately decreasing transepithelial resistance increasing permeability to small molecules (4 kDa). Gliadin reorganisation actin filaments expression tight junction proteins occludin, claudin-3 claudin-4, TJ-associated protein ZO-1 adherens E-cadherin.
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