Adherence to endothelial cells induces release of soluble Tumor Necrosis Factor (TNF) receptor forms from neutrophil granulocytes

被引：6

作者：

Björnberg, F ^{[1
]}

Lantz, M ^{[1
]}

机构：

[1] Lund Univ, Dept Hematol, S-22100 Lund, Sweden

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1998年 / 244卷 / 02期

关键词：

D O I：

10.1006/bbrc.1998.8302

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

The TNF receptors, TNF-R55 and TNF-R75, may undergo proteolytic cleavage and form soluble receptor forms, TNF-R55-BP and TNF-R75-BP. Neutrophils are abundant with both forms of TNF-receptors, while endothelial cells (ECV 304) only express TNF-R55. Human neutrophils were allowed to interact with an unstimulated or a IL-1 beta stimulated endothelium followed by determination of TNF-R75-BP with ELISA. Neutrophils in suspension or in contact with an unstimulated endothelium released only low amounts of TNF-R75-BP. However, neutrophils released significant amounts of TNF-R75-BP after adherence to an endothelium stimulated with IL-1 beta. Neutrophils were not generally activated during adherence since concomitant release of lactoferrin from neutrophils only reached levels of 1-5% compared with incubation with phorbolesters. Blocking integrins with antibodies to CD11/CD18 resulted in inhibition of both neutrophil adherence to an endothelium and shedding of TNF-R75, In addition, TNF-R55-BP decreased the production of TNF from IL-1 beta stimulated endothelial cells, suggesting that soluble TNF receptor forms are able to inhibit TNF production. (C) 1998 Academic Press.

引用

页码：594 / 598

页数：5

共 31 条

[1]

Bennett TA, 1996, J IMMUNOL, V156, P3093

[2]

BJORNBERG F, 1994, LYMPHOKINE CYTOK RES, V13, P203

[3]

METALLOPROTEASES AND SERINE PROTEASES ARE INVOLVED IN THE CLEAVAGE OF THE 2 TUMOR-NECROSIS-FACTOR (TNF) RECEPTORS TO SOLUBLE FORMS IN THE MYELOID CELL-LINES U-937 AND THP-1 [J].