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Department of Physiology, The University of Arizona, and The Benjamin W. Zweifach Microcirculation Laboratories, Department of Veteran Affairs Medical Center, Tucson, Arizona 85723
Thrombin-induced endothelial monolayer hyperpermeability is thought to
result from increased F-actin stress fiber-related contractile tension,
a process regulated by the small GTP-binding protein Rho. We tested
whether this process was dependent on the Rho-associated protein
kinase, ROCK, using a specific ROCK inhibitor, Y-27632. The effects of
Y-27632 on thrombin-induced myosin light chain phosphorylation (MLCP)
and tyrosine phosphorylation of p125 focal adhesion kinase
(p125FAK) and paxillin were measured by Western blotting.
F-actin organization and content were analyzed by digital imaging, and
endothelial monolayer permeability was measured in bovine pulmonary
artery endothelial cell (EC) monolayers using a size-selective
permeability assay. Y-27632 enhanced EC monolayer barrier function due
to a decline in small-pore number that was associated with increased EC
surface area, reduced F-actin content, and reorganization of F-actin to
-catenin-containing cell-cell adherens junctions. Although Y-27632
prevented thrombin-induced MLCP, stress fiber formation, and the
increased phosphotyrosine content of paxillin and p125FAK,
it attenuated but did not prevent the thrombin-induced formation of
large paracellular holes. These data indicate that thrombin-induced stress fiber formation is ROCK dependent. In contrast, thrombin-induced paracellular hole formation occurs in a ROCK-independent manner, whereas thrombin-induced monolayer hyperpermeability appears to be
partially ROCK dependent.
nonmuscle myosin; myosin light chain phosphorylation; paxillin; Y-27632; immunofluorescent digital imaging; Rho-associated coiled-coil forming kinase
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