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J Appl Physiol 95: 1889-1895, 2003. First published July 3, 2003; doi:10.1152/japplphysiol.00225.2003
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Rho inhibition decreases TNF-induced endothelial MAPK activation and monolayer permeability

Fiemu E. Nwariaku,1 Patricia Rothenbach,1 Zijuan Liu,1 Xudong Zhu,1 Richard H. Turnage,2 and Lance S. Terada1

1Departments of Surgery and Pulmonary Medicine, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9156; and 2Department of Surgery, Louisiana State University Health Sciences Center, Shreveport, Louisiana 71115

Submitted 3 March 2003 ; accepted in final form 30 June 2003

Our laboratory previously demonstrated that MAPK activation is an important signal during cytokine-induced endothelial permeability (Nwariaku FE, Liu Z, Terada L, Duffy S, Sarosi G, and Turnage R. Shock 18: 82-85, 2002). Because GTP-binding proteins have been implicated in MAPK activation, we now hypothesize that the GTP-binding protein Rho is a mediator of TNF-induced MAPK activation and increased endothelial permeability. Transmonolayer permeability was assessed in human lung microvascular cells by measuring transmonolayer electrical resistance. MAPK activity was assessed by using a phospho-specific immunoprecipitation kinase assay and by comparing Western blots for phospho-MAPK with total MAPK. MAPK inhibitors used were SB-202190 and PD-098059, whereas Clostridium botulinum C3 transferase was used as a Rho inactivator. Rho-associated coiled-coil kinase was inhibited with Y-27632. TNF increased pulmonary endothelial permeability in vitro and caused a rapid, sustained increase in endothelial p38 and extracellular signal-regulated kinase MAPK activity. Inhibition of p38 and extracellular signal-regulated kinase MAPK with SB-202190 and PD-098059, respectively, decreased TNF-induced endothelial permeability. C3 transferase attenuated TNF-induced MAPK activation and blocked TNF-induced endothelial permeability. Finally, inhibition of Rho-associated coiled-coil kinase with Y-27632 prevented both MAPK activation and TNF-induced decreases in transmonolayer resistance. Rho acts upstream of mitogen-activated protein kinases in mediating TNF-induced pulmonary endothelial leak.

endothelium; guanosine 5'-triphosphate-binding proteins; cytokines; tumor necrosis factor; mitogen-activated protein kinase; extracellular signal-regulated kinase; p38; cell signaling


Address for reprint requests and other correspondence: F. E. Nwariaku, 5323 Harry Hines Blvd., Dallas, TX 75390-9156 (E-mail: fiemu.nwariaku{at}UTSouthwestern.edu).




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