Ionic radiocontrast media disrupt intercellular contacts via an extracellular XXXX -independent mechanism.

@entity8 @entity137 @entity1496 @entity7568 @entity235 @entity141 @entity4527 @entity4946 @entity7567 @entity10527 @entity872 @entity3460 @entity460 @entity70897 @entity874 @entity6111
Direct cytotoxic effects of radiocontrast (RC) agents have been implicated in radiocontrast @entity8 (RCIN). The interaction between extracellular @entity460 , which plays a central role in intercellular contacts, and the in vitro @entity137 of RC was tested in Madin-Darby @entity235 kidney (MDCK) cell monolayers grown on permeable supports. Cell viability was determined by @entity3460 exclusion. The function of intercellular junctions was assessed by measuring the electrical transmonolayer resistance (TMR). The cell contacts were examined with indirect immunofluorescence microscopy using antibodies against the junctional proteins @entity70897 . The ionic RC agents @entity4946 and @entity7567 (74 mg @entity1496 /ml), but not the nonionic compounds @entity6111 or @entity7568 , decreased ionized @entity460 ( @entity141 ) in the incubation media from 1.48 +/- 0.04 mM (control) to 0.89 +/- 0.06 mM ( @entity4946 ), respectively to 1.05 +/- 0.08 mM ( @entity7567 ). @entity4946 , and to a lesser extent @entity7567 , reduced the number of viable MDCK cells and showed a redistribution of the @entity10527 , @entity872 and @entity874 immunofluorescence signal with a parallel decrease of the TMR indicating an impaired monolayer integrity. A similar reduction of extracellular @entity141 through @entity4527 failed to reproduce these effects. Conversely, raising @entity141 in @entity4946 -containing media to control levels did not abrogate its @entity137 . In conclusion, the ionic RC agents @entity4946 and @entity7567 , but not the nonionic compounds @entity6111 or @entity7568 , reduce extracellular @entity141 in vitro. However, this reduction of @entity141 does not explain their cytotoxic effects which could contribute to the pathogenesis of RCIN in vivo by opening intercellular junctions.
