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J Biol Chem, Vol. 274, Issue 35, 24930-24934, August 27, 1999
From the Departments of Surgery and Medical Physiology, Texas A&M
University System Health Science Center, Temple, Texas 76504
The endothelial adherens junction is formed by
complexes of transmembrane adhesive proteins, of which
Activated Neutrophils Induce Hyperpermeability and
Phosphorylation of Adherens Junction Proteins in Coronary Venular
Endothelial Cells
-catenin is
known to connect the junctional protein vascular endothelial
(VE)-cadherin to the cytoskeleton and to play a signaling role in the
regulation of junction-cytoskeleton interaction. In this study, we
investigated the effect of neutrophil activation on endothelial
monolayer integrity and on -catenin and VE-cadherin modification.
Treatment of cultured bovine coronary endothelial monolayers with
C5a-activated neutrophils resulted in an increase in permeability as
measured by albumin clearance across the monolayer. Furthermore, large
scale intercellular gap formation was observed in coincidence with the
hyperpermeability response. Immunofluorescence analysis showed that
-catenin and VE-cadherin staining changed from a uniform
distribution along the membrane of control cells to a diffuse pattern
for both proteins and finger-like projections for -catenin in
neutrophil-exposed monolayers. Correlatively, there was an increase in
actin stress fiber formation in treated cells. Finally, -catenin and
VE-cadherin from neutrophil-treated endothelial cells showed a
significant increase in tyrosine phosphorylation. Our results are the
first to link neutrophil-mediated changes in adherens junctions with intercellular gap formation and hyperpermeability in microvascular endothelial cells. These data suggest that neutrophils may
regulate endothelial barrier function through a process conferring
conformational changes to -catenin and VE-cadherin.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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