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. Author manuscript; available in PMC: 2012 Apr 1.

Published in final edited form as: Exp Cell Res. 2010 Nov 25;317(6):859–872. doi: 10.1016/j.yexcr.2010.11.011

HPAEC grown on Flexcell plates were transfected with p190RhoGAP-specific siRNA or non-specific RNA duplexes. After 72 hr cell monolayers were preconditioned at pathologic (18%) levels of CS for 2 hr and stimulated with thrombin (0.1 U/ml, 15 min) with or without OxPAPC pretreatment (10 μg/ml, 15 min). A: F-actin was visualized by immunofluorescence staining with Texas-Red phalloidin. Paracellular gaps are marked by arrows. Bar graphs represent quantitative analysis of gap formation in control and treated HPAEC. Data are expressed as mean ± SD of three independent experiments; *p<0.05. B: Phosphorylation of MLC was detected by western blot with phospho-specific antibodies. Equal protein loading was confirmed by re-preobing of membranes with β-tubulin antibody. Result of densitometry shown as mean ± SD, * p<0.05

HPAEC grown on Flexcell plates were transfected with p190RhoGAP-specific siRNA or non-specific RNA duplexes. After 72 hr cell monolayers were preconditioned at pathologic (18%) levels of CS for 2 hr and stimulated with thrombin (0.1 U/ml, 15 min) with or without OxPAPC pretreatment (10 μg/ml, 15 min). A: F-actin was visualized by immunofluorescence staining with Texas-Red phalloidin. Paracellular gaps are marked by arrows. Bar graphs represent quantitative analysis of gap formation in control and treated HPAEC. Data are expressed as mean ± SD of three independent experiments; *p<0.05. B: Phosphorylation of MLC was detected by western blot with phospho-specific antibodies. Equal protein loading was confirmed by re-preobing of membranes with β-tubulin antibody. Result of densitometry shown as mean ± SD, * p<0.05