Altered expression, localization, and phosphorylation of epithelial junctional proteins in celiac disease

Rachele Ciccocioppo, Alberto Finamore, Carmen Ara, Antonio Di Sabatino, Elena Mengheri, Gino R. Corazza

Research output: Contribution to journalArticlepeer-review


We aimed to study the expression and localization of the molecular components of enterocyte junctions in celiac disease together with the level of tyrosine phosphorylation, a phenomenon known to affect their cellular distribution and function, and to explore the influence of proinflammatory cytokines. Duodenal biopsy specimens from patients with celiac disease and control subjects were used for immunoprecipitation, immunoblotting, and immunolocalization by using antioccludin, anti-zonula occludens (ZO)-1, anti-E-cadherin, anti-β-catenin, and antiphosphotyrosine antibodies. The same procedures were carried out on filter-grown Caco-2 cells incubated in the absence or presence ofinterferon jand tumor necrosis factor α. In active celiac disease, the absence of a phosphorylated ZO-1 and the extensive phosphorylation of β-catenin might be responsible for the absence of membranous localization of occludin and E-cadherin, respectively. The in vitro system showed an influence of the cytokines on the assembly of these complexes that proved the opposite to celiac samples as far as tight junctions were concerned because the presence of a phosphorylated ZO-1 enables occludin to localize in the membrane.

Original languageEnglish
Pages (from-to)502-511
Number of pages10
JournalAmerican Journal of Clinical Pathology
Issue number4
Publication statusPublished - Apr 2006


  • Celiac disease
  • Cytokines
  • Enterocyte junctions
  • Tyrosine phosphorylation

ASJC Scopus subject areas

  • Pathology and Forensic Medicine


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