Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8384171 | FEBS Letters | 2006 | 8 Pages |
Abstract
Acyl-homoserine lactone (HSL) quorum sensing molecules play an important role in regulation of virulence gene expression in Pseudomonas aeruginosa. Here, we show that 3O-C12-HSL can disrupt barrier integrity in human epithelial Caco-2 cells as evidenced by decreased transepithelial electrical resistance (TER), increased paracellular flux, reduction in the expression and distribution of ZO-1 and occludin, and reorganization of F-actin. P. aeruginosa 3O-C12-HSL activate p38 and p42/44 kinases, and inhibition of these kinases partly prevented 3O-C12-HSL-induced changes in TER, paracellular flux and expression of occludin and ZO-1. These findings demonstrate that P. aeruginosa 3O-C12-HSL can modulate tight junction integrity of Caco-2 cells.
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Authors
Elena Vikström, Farideh Tafazoli, Karl-Eric Magnusson,