Effect of Interleukin-13 or Tumor Necrosis Factor-Alpha on Eosinophil Adhesion to Endothelial Cells under Physiological Flow Conditions

2007 ◽  
Vol 143 (1) ◽  
pp. 33-37 ◽  
Author(s):  
Hiroshi Tachimoto ◽  
Motohiro Ebisawa
Keyword(s):  
Endothelial Cells ◽  
Tumor Necrosis Factor ◽  
Tumor Necrosis Factor Alpha ◽  
Tumor Necrosis ◽  
Flow Conditions ◽  
Necrosis Factor Alpha ◽  
Interleukin 13 ◽  
Physiological Flow ◽  
Factor Alpha ◽  
Necrosis Factor

scholarly journals Regulation of thrombomodulin by tumor necrosis factor-alpha: comparison of transcriptional and posttranscriptional mechanisms

Blood ◽  
1991 ◽  
Vol 77 (3) ◽  
pp. 542-550 ◽  
Author(s):  
SR Lentz ◽  
M Tsiang ◽  
JE Sadler
Keyword(s):  
Endothelial Cells ◽  
Tumor Necrosis Factor ◽  
Tumor Necrosis Factor Alpha ◽  
Posttranscriptional Regulation ◽  
Tumor Necrosis ◽  
Vascular Endothelial Cells ◽  
Necrosis Factor Alpha ◽  
Subsequent Decrease ◽  
Factor Alpha ◽  
Necrosis Factor

Abstract The procoagulant properties of cultured vascular endothelial cells are enhanced in response to inflammatory cytokines such as tumor necrosis factor-alpha (TNF). A major component of this response is a reduction in expression of thrombomodulin, a cell surface cofactor for the activation of protein C. Regulation of thrombomodulin expression by TNF has been reported to occur through multiple mechanisms. To determine the relative roles of transcriptional and posttranscriptional regulation, the effect of TNF on the turnover of thrombomodulin protein and mRNA was examined in human and bovine endothelial cells. Quantitative nuclease S1 protection assays showed a 70% to 90% reduction in thrombomodulin mRNA within 4 hours of the addition of 1.0 nmol/L TNF to the culture medium. The decrease in thrombomodulin mRNA resulted from inhibition of transcription, followed by rapid degradation of thrombomodulin transcripts (t1/2 less than or equal to 3 hours). In pulse-chase incubations, thrombomodulin synthesis decreased parallel with mRNA, but the rate of degradation of radiolabeled thrombomodulin was not significantly altered by TNF. Human thrombomodulin was degraded with a t1/2 of 8.2 +/- 2.4 hours (SD) or 7.5 +/- 1.3 hours (SD) in the absence or presence of TNF, respectively. We conclude that TNF acts primarily to inhibit thrombomodulin transcription. The subsequent decrease in activity results from the inherent instability of thrombomodulin mRNA and protein in these cells, and not from the regulation of thrombomodulin degradation.

scholarly journals The Extracellular Adherence Protein from Staphylococcus aureus Inhibits Neutrophil Binding to Endothelial Cells

2004 ◽  
Vol 72 (10) ◽  
pp. 6164-6167 ◽  
Author(s):  
Axana Haggar ◽  
Cecilia Ehrnfelt ◽  
Jan Holgersson ◽  
Jan-Ingmar Flock
Keyword(s):  
Staphylococcus Aureus ◽  
Endothelial Cells ◽  
Tumor Necrosis Factor ◽  
Tumor Necrosis Factor Alpha ◽  
Tumor Necrosis ◽  
Neutrophil Adhesion ◽  
Necrosis Factor Alpha ◽  
Factor Alpha ◽  
Necrosis Factor ◽  
Adhesion Assays

ABSTRACT Extracellular adherence protein (Eap) from Staphylococcus aureus inhibits the adherence of neutrophils to nonstimulated and tumor necrosis factor alpha-stimulated endothelial cells in both static adhesion assays and flow adhesion assays. Consequently, Eap also impaired their transendothelial migration. During an S. aureus infection, Eap may thus serve to reduce inflammation by inhibiting neutrophil adhesion and extravasation.

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