A RECOMBINANT AMINO‐TERMINAL FRAGMENT OF BACTERICIDAL/PERMEABILITY INCREASING PROTEIN (rBPI23) INHIBITS SOLUBLE CD14‐MEDIATED LIPOPLYSACCHARIDE‐INDUCED ENDOTHELIAL ADHERENCE FOR HUMAN NEUTROPHILS
作者:
Kun Huang,
Paul Conlon,
Dianne Fishwild,
期刊:
Shock
(OVID Available online 1994)
卷期:
Volume 1,
issue 2
页码: 81-86
ISSN:1073-2322
年代: 1994
出版商: OVID
数据来源: OVID
摘要:
Exposure of cultured human umbilical vein endothelial cells (HUVEC) to lipopolysaccharide (LPS) or interleukin 1 (IL-1) causes increased expression of adhesion molecules such as E-selectin and CD54 by HUVEC and consequently increased adherence of peripheral blood neutrophils. A recombinant amino-terminal fragment of bactericidal/permeability increasing protein (rBPI23) was shown to specifically block the LPS-induced adhesiveness of HUVEC for neutrophils. rBPI23also prevented the LPS-but not IL-1β-induced upregulation on HUVEC of E-selectin and CD54. Furthermore, this inhibition was evident even when the endothelial cells were exposed to LPS for up to 1–2 h prior to rBPI23addition. The inhibitory effects of an anti-CD14 monoclonal antibodies (mAb) were similar to those of rBPI23. Combination of the anti-CD14 mAb and rBPI23resulted inhibition greater than either one used alone. These studies demonstrate that rBPI23acts as a specific and potent inhibitor of soluble CD14-mediated LPS induction.
点击下载:
PDF
(568KB)
返 回