Rapid disruption of intestinal barrier function by gliadin involves altered expression of apical junctional proteins.
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.
Sander
Guy R
GR
Tissue Development and Repair, Epithelial Biology Laboratory, Child Health Research Institute, 72 King William Road, North Adelaide, SA 5006, Australia. guy.sander@adelaide.edu.au
Cummins
Adrian G
AG
Henshall
Tanya
T
Powell
Barry C
BC
D000199:Actins / Q000378:metabolism; D022005:Adherens Junctions / Q000737:chemistry / Q000378:metabolism*; D018938:Caco-2 Cells; D015820:Cadherins / Q000378:metabolism; D062465:Claudin-3; D062506:Claudin-4; D005903:Gliadin / Q000378:metabolism*; D006801:Humans; D007413:Intestinal Mucosa / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism; D062793:Occludin; D010539:Permeability; D010750:Phosphoproteins / Q000378:metabolism; D019108:Tight Junctions / Q000737:chemistry / Q000378:metabolism*; D062826:Zonula Occludens-1 Protein
D000199:Actins; C568122:CLDN3 protein, human; C568157:CLDN4 protein, human; D015820:Cadherins; D062465:Claudin-3; D062506:Claudin-4; D008565:Membrane Proteins; C568985:OCLN protein, human; D062793:Occludin; D010750:Phosphoproteins; C569042:TJP1 protein, human; D062826:Zonula Occludens-1 Protein; D005903:Gliadin