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J Biol Chem, Vol. 273, Issue 32, 20185-20188, August 7, 1998
From the Endothelial cells play a pivotal role in the
inflammatory process by coordinating the recruitment of inflammatory
cells to sites of tissue injury. Lipopolysaccharide (LPS) activates
many of the proinflammatory and procoagulant responses of endothelial cells, and endothelial injury is thought to play a crucial role in the
pathogenesis of septic shock due to Gram-negative bacteria. The
receptor used by LPS to signal endothelial responses has not been
identified. It is also not known how LPS induces endothelial injury/death. In this study, we demonstrate that LPS mediates endothelial apoptosis by a FADD-dependent pathway. FADD is
a death domain-containing protein that binds to certain members of the tumor necrosis factor receptor family, namely TNFR1, Fas, and DR3.
However, none of these receptors appear to be involved in LPS-mediated
death, suggesting that LPS may utilize a novel death domain-containing
protein to transduce a death signal.
Lipopolysaccharide Mediates Endothelial Apoptosis by a
FADD-dependent Pathway
,,
Department of Pathology and Laboratory
Medicine, University of British Columbia and St. Paul's Hospital,
Vancouver, British Columbia, Canada V6Z 1Y6 and the Departments of
¶ Molecular Biotechnology and § Medicine, University of
Washington, Seattle, Washington 98195
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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