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FEBS Lett. 2005 Aug 29;579(21):4851-5.

Rapid disruption of intestinal barrier function by gliadin involves altered expression of apical junctional proteins.

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Tissue Development and Repair, Epithelial Biology Laboratory, Child Health Research Institute, 72 King William Road, North Adelaide, SA 5006, Australia.


Coeliac disease is a chronic enteropathy caused by the ingestion of wheat gliadin and other cereal prolamines derived from rye and barley. In the present work, we investigated the mechanisms underlying altered barrier function properties exerted by gliadin-derived peptides in human Caco-2 intestinal epithelial cells. We demonstrate that gliadin alters barrier function almost immediately by decreasing transepithelial resistance and increasing permeability to small molecules (4 kDa). Gliadin caused a reorganisation of actin filaments and altered expression of the tight junction proteins occludin, claudin-3 and claudin-4, the TJ-associated protein ZO-1 and the adherens junction protein E-cadherin.

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