Deacylated lipopolysaccharide inhibits plasminogen activator inhibitor-1, prostacyclin, and prostaglandin E2 induction by lipopolysaccharide but not by tumor necrosis factor-α

Francis X. Riedo, Robert S. Munford, William B. Campbell, Joan S. Reisch, Kenneth R. Chien, Robert D. Gerard

Research output: Contribution to journalArticle

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Abstract

Bacterial LPS and TNF induce vascular endothelial cells to express a variety of response molecules. LPS that is partially deacylated (dLPS) by a human neutrophil enzyme blocks the ability of LPS, but not TNF, to augment one of these responses, the expression of endothelial cell surface molecules that promote neutrophil adherence (J. Exp. Med. 1987; 165:1393-1402). We show that dLPS can inhibit the ability of LPS, but not TNF, to elicit the expression of plasminogen activator inhibitor-1 (PAI-1), prostacyclin, and PGE2 by human umbilical vein endothelial cells. dLPS also prevented the accumulation of specific PAI-1 mRNA in response to LPS, but not to TNF. Neither the LPS- or TNF-induced expression of PAI-1 nor the dLPS inhibition of the LPS response was mediated by prostanoids. These results indicate that dLPS can specifically block a variety of endothelial cell responses to LPS and provide support for the hypotheses 1) that dLPS and LPS may interact with a common target molecule on or in endothelial cells, and 2) that dLPS, produced by enzymatic deacylation of LPS in vivo, could inhibit endothelial cell stimulation by LPS and thereby limit the host inflammatory response to invasive gram-negative bacteria.

Original languageEnglish (US)
Pages (from-to)3506-3512
Number of pages7
JournalJournal of Immunology
Volume144
Issue number9
StatePublished - May 1 1990

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Plasminogen Activator Inhibitor 1
Epoprostenol
Dinoprostone
Lipopolysaccharides
Endothelial Cells
Tumor Necrosis Factor-alpha
Neutrophils
Human Umbilical Vein Endothelial Cells
Gram-Negative Bacteria
Prostaglandins
deacylated lipopolysaccharides
Messenger RNA
Enzymes

ASJC Scopus subject areas

  • Immunology

Cite this

Deacylated lipopolysaccharide inhibits plasminogen activator inhibitor-1, prostacyclin, and prostaglandin E2 induction by lipopolysaccharide but not by tumor necrosis factor-α. / Riedo, Francis X.; Munford, Robert S.; Campbell, William B.; Reisch, Joan S.; Chien, Kenneth R.; Gerard, Robert D.

In: Journal of Immunology, Vol. 144, No. 9, 01.05.1990, p. 3506-3512.

Research output: Contribution to journalArticle

Riedo, Francis X. ; Munford, Robert S. ; Campbell, William B. ; Reisch, Joan S. ; Chien, Kenneth R. ; Gerard, Robert D. / Deacylated lipopolysaccharide inhibits plasminogen activator inhibitor-1, prostacyclin, and prostaglandin E2 induction by lipopolysaccharide but not by tumor necrosis factor-α. In: Journal of Immunology. 1990 ; Vol. 144, No. 9. pp. 3506-3512.
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abstract = "Bacterial LPS and TNF induce vascular endothelial cells to express a variety of response molecules. LPS that is partially deacylated (dLPS) by a human neutrophil enzyme blocks the ability of LPS, but not TNF, to augment one of these responses, the expression of endothelial cell surface molecules that promote neutrophil adherence (J. Exp. Med. 1987; 165:1393-1402). We show that dLPS can inhibit the ability of LPS, but not TNF, to elicit the expression of plasminogen activator inhibitor-1 (PAI-1), prostacyclin, and PGE2 by human umbilical vein endothelial cells. dLPS also prevented the accumulation of specific PAI-1 mRNA in response to LPS, but not to TNF. Neither the LPS- or TNF-induced expression of PAI-1 nor the dLPS inhibition of the LPS response was mediated by prostanoids. These results indicate that dLPS can specifically block a variety of endothelial cell responses to LPS and provide support for the hypotheses 1) that dLPS and LPS may interact with a common target molecule on or in endothelial cells, and 2) that dLPS, produced by enzymatic deacylation of LPS in vivo, could inhibit endothelial cell stimulation by LPS and thereby limit the host inflammatory response to invasive gram-negative bacteria.",
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