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J Biol Chem, Vol. 273, Issue 52, 35371-35380, December 25, 1998
From the Division of Infectious Diseases, Departments of Pathology
and Medicine, Department of Veterans Affairs Medical Center, University
of Maryland School of Medicine, Baltimore, Maryland 21201
Bacterial lipopolysaccharide or endotoxin induces
actin reorganization, increased paracellular permeability, and
endothelial cell detachment from the underlying extracellular matrix
in vitro. We studied the effect of endotoxin on
transendothelial albumin flux and detachment of endothelial cells
cultured on gelatin-impregnated filters. The endotoxin-induced changes
in endothelial barrier function and detachment occurred at doses and
times that were compatible with endotoxin-induced apoptosis. Since the
actin cytoskeleton and cell-cell and cell-matrix adhesion all
participate in the regulation of the paracellular pathway and
cell-matrix interactions, we studied whether protein components of the
actin-linked adherens junctions were modified in response to endotoxin.
Components of cell-cell (
Bacterial Lipopolysaccharide Disrupts Endothelial Monolayer
Integrity and Survival Signaling Events through Caspase Cleavage of
Adherens Junction Proteins
- and 
-catenin) and cell-matrix (focal
adhesion kinase and p130Cas) adherens junctions were
cleaved by caspases activated during apoptosis with dose and time
requirements that paralleled those seen for barrier dysfunction and
detachment. Cleavage of focal adhesion kinase led to its dissociation
from the focal adhesion-associated signaling protein, paxillin,
resulting in reduced paxillin tyrosine phosphorylation. Inhibition of
caspase-mediated cleavage of these proteins protected against
detachment but not opening of the paracellular pathway. Therefore,
endotoxin-induced disruption of endothelial monolayer integrity and
survival signaling events is mediated, in part, through caspase
cleavage of adherens junction proteins.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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