Human endothelial cell adhesiveness for neutrophils, induced by Escherichia coli lipopolysaccharide in vitro, is inhibited by Bacteroides fragilis lipopolysaccharide.
Human endothelial cell adhesiveness for neutrophils, induced by Escherichia coli lipopolysaccharide in vitro, is inhibited by Bacteroides fragilis lipopolysaccharide.
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DOI：
10.4049/jimmunol.143.9.3025
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发表时间：
1989-11
影响因子：
4.4
通讯作者：
David K. Magnuson;A. Weintraub;Timothy H. Pohlman;Ronald V. Maier
中科院分区：
文献类型：
--
作者：
David K. Magnuson;A. Weintraub;Timothy H. Pohlman;Ronald V. Maier
Recent studies in vitro have demonstrated that LPS from Gram-negative bacteria are capable of inducing endothelial cells to express a cell surface property that promotes the adherence of neutrophils (polymorphonuclear cells, PMN). We have investigated the effects of LPS from Bacteroides fragilis, an organism documented to have little toxicity in vivo, on the induction of this property in human endothelial cells. Monolayers of cultured human umbilical vein endothelial cells (HUVE) exhibited no increase in adhesiveness for 51Cr-radiolabeled PMN after 4 h of exposure to B. fragilis LPS from 1 ng to 10 micrograms/ml. Escherichia coli LPS elicited a dose-dependent enhancement of HUVE adhesiveness for PMN over the same concentration range, reaching a maximum of 49.4 +/- 6.6% at 10 micrograms/ml. Like E. coli LPS, B. fragilis LPS converted chromogenic substrate in the Limulus amebocyte lysate assay, and was directly cytotoxic to bovine aortic endothelial cells. Both B. fragilis LPS activities required doses two-to-three log-fold higher than for E. coli LPS. In addition, we found that B. fragilis LPS inhibited the induction of HUVE adhesiveness for PMN by E. coli LPS. This inhibition was also dose-dependent, becoming maximal (greater than 80%) when B. fragilis LPS was in 10- to 20-fold excess. Tumor necrosis factor and IL-1, two monokines which also elicit HUVE adhesiveness for PMN, were not inhibited by B. fragilis LPS, suggesting a mechanism of HUVE activation by LPS which is signal-specific, and which recognizes specificities of LPS structure.
