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Activation of PAR-1 induces enterocyte apoptosis and increases permeability in caspase-3 and tyrosine kinase dependent fashion


, : Activation of PAR-1 induces enterocyte apoptosis and increases permeability in caspase-3 and tyrosine kinase dependent fashion. FASEB Journal 17(4-5): Abstract No 513 10, March

Protease-activated receptor-1 (PAR-1) is implicated in intestinal inflammation. This study characterizes novel effects of PAR-1 activation on epithelial apoptosis and permeability. METHODS: In vitro: 1) Duodenal epithelial monolayers were incubated with 25 ?M TFLLR (TF; PAR-1 agonist), 5 U/ml thrombin, or 25 ?M RLLFT (RL; reverse peptide) and assessed for apoptosis. 2) Monolayers were pre-treated with/without 120 ?M caspase-3 inhibitor (DEVD), then incubated with apical or basolateral TF, thrombin, or RL, and assessed for permeability (FITC-dextran). 3) Monolayers were pre-treated with/without DEVD, 5 ?M PP1 (src inhibitor), or 20 ?M tyrphostin (TP; tyrosine kinase inhibitor), incubated with TF, thrombin, or RL, and assessed for tight junctional integrity and apoptosis (ZO-1/Hoechst staining). In vivo: C57Bl6 mice were given intracolonic 1.2 mM DEVD, followed by 200 ?g TF or RL, and then assessed for colonic permeability (51Cr-EDTA). RESULTS: At 2 and 24 h, both TF and thrombin, induced enterocyte apoptosis, increased permeability (apical or basolateral), and disrupted ZO-1. All effects were inhibited by DEVD. TP, but not PP1, prevented ZO-1 injury and enterocyte apoptosis. TF increased colonic permeability; the effect was blocked by DEVD. SUMMARY: Induction of enterocyte apoptosis by PAR-1 agonists reduces epithelial barrier function in caspase-3 and tyrosine kinase dependent fashion. (NSERC/CCFC).

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