Human allogeneic lymphocytes trigger endothelial cell tissue factor expression by a tumor necrosis factor-dependent pathway

1998 ◽  
Vol 132 (6) ◽  
pp. 530-540 ◽  
Author(s):  
Pascale Reverdiau-Moalic ◽  
Herve Watler ◽  
Sophie Iochmann ◽  
Claire Pouplard ◽  
Elisabeth Rideau ◽  
...  
Keyword(s):  
Endothelial Cell ◽  
Tumor Necrosis Factor ◽  
Tissue Factor ◽  
Tumor Necrosis ◽  
Tissue Factor Expression ◽  
Cell Tissue ◽  
Factor Expression ◽  
Dependent Pathway ◽  
Necrosis Factor ◽  
Allogeneic Lymphocytes

scholarly journals CD8+ T-Cell–Derived Tumor Necrosis Factor Can Induce Tissue Factor Expression on Monocytes

2019 ◽  
Vol 220 (1) ◽  
pp. 73-77 ◽  
Author(s):  
Michael L Freeman ◽  
Soumya Panigrahi ◽  
Bonnie Chen ◽  
Steven Juchnowski ◽  
Scott F Sieg ◽  
...  
Keyword(s):  
T Cell ◽  
Tumor Necrosis Factor ◽  
Tissue Factor ◽  
Tumor Necrosis ◽  
Cd8 T Cell ◽  
Tissue Factor Expression ◽  
Factor Expression ◽  
Necrosis Factor

Induction of Tissue Factor Expression in Whole Blood: Lack of Evidence for the Presence of Tissue Factor Expression in Granulocytes

2000 ◽  
Vol 83 (06) ◽  
pp. 861-867 ◽  
Author(s):  
Bjarne Østerud ◽  
Jan Olsen ◽  
L. Vijaya Rao
Keyword(s):  
Tumor Necrosis Factor ◽  
Tissue Factor ◽  
Whole Blood ◽  
Blood Cells ◽  
Tumor Necrosis ◽  
Platelet Rich Plasma ◽  
Tissue Factor Expression ◽  
Factor Expression ◽  
Activated Monocytes ◽  
Necrosis Factor

SummaryThe present investigation was undertaken to explore the effect of platelets, tumor necrosis factor (TNF) and phorbel ester [phorbol 12-myristate 13-acetate (PMA)] on lipopolysaccharide (LPS)-induced tissue factor (TF) activity and TF antigen by using Western blot and ELISA-techniques. LPS was found to induce correlating levels of TF antigen and the activity in monocytes. TNF and PMA, when used alone, failed to induce TF activity and the antigen in monocytes, but enhanced the LPS-induced TF activity and the antigen by 2 to 3-fold. Addition of platelet rich plasma to isolated blood cells enhanced the LPS-induced TF activity but not the antigen levels in monocytes. In contrast to whole platelets, platelet lysates enhanced both LPS-induced TF activity and the antigen. Granulocytes isolated from heparinized plasma incubated for 2 or 24 h with LPS alone or together with PMA, failed to generate TF antigen or the activity. Although granulocyte preparations isolated from whole blood that was incubated for 24 h with LPS and PMA apparently possessed a significant amount of TF activity and the antigen, this could be accounted for by trace levels of contaminating monocytes. Upregulation of LPS-induced TF activity but not the antigen by platelets in the presence of granulocytes suggests that the increased TF activity could be the result of PS enrichment of monocytes by fusion or platelets with activated monocytes.

Induction of tissue factor expression by anti-β2-glycoprotein I is mediated by tumor necrosis factor α

2019 ◽  
Vol 49 (2) ◽  
pp. 228-234 ◽  
Author(s):  
Anne Hollerbach ◽  
Nadine Müller-Calleja ◽  
Antje Canisius ◽  
Carolin Orning ◽  
Karl J. Lackner
Keyword(s):  
Tumor Necrosis Factor ◽  
Tissue Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Tissue Factor Expression ◽  
Glycoprotein I ◽  
Factor Expression ◽  
Factor Α ◽  
Necrosis Factor

scholarly journals Both tumor necrosis factor receptors, TNFR60 and TNFR80, are involved in signaling endothelial tissue factor expression by juxtacrine tumor necrosis factor alpha

Blood ◽  
1995 ◽  
Vol 86 (5) ◽  
pp. 1836-1841 ◽  
Author(s):  
EF Schmid ◽  
K Binder ◽  
M Grell ◽  
P Scheurich ◽  
K Pfizenmaier
Keyword(s):  
Tumor Necrosis Factor ◽  
Tissue Factor ◽  
Tumor Necrosis ◽  
Cell Activation ◽  
Tnf Alpha ◽  
Signal Pathways ◽  
Tissue Factor Expression ◽  
Tnf Receptors ◽  
Factor Expression ◽  
Necrosis Factor

We have investigated the role of the two distinct tumor necrosis factor (TNF) receptors (TNFR60 and TNFR80) in endothelial cell activation employing an in vitro model of tumor necrosis factor alpha (TNF-alpha)- dependent tissue factor production of human umbilical vein endothelial cells (HUVECs). In this model, tissue factor is produced either on addition of exogeneous TNF-alpha, or by induction of endogenous TNF- alpha via adhesion molecule-linked signal pathways. Under both conditions, tissue factor expression could be partially blocked by antagonistic antibodies against either TNFR60 or TNFR80 and was fully inhibited by simultaneous application of both antibodies. Selective inhibitors of either TNFR60 or TNFR80-induced signal pathways inhibited tissue factor expression, and selective triggering of either of the two TNF receptors by agonistic antibodies induced this response in HUVECs. Furthermore, a coculture system of HUVECs and Chinese hamster ovary transfectants expressing a noncleavable, exclusively membrane-bound form of TNF-alpha resulted in a potent activation of HUVECs with synergistic action of both TNF receptors. Together, these data underline the importance of juxtacrine pathways in endothelial cell activation of procoagulant functions and show that membrane TNF-alpha and both TNFR types play a critical role.

The Factor VIII Bypassing Activity of Prothrombin Complex Concentrates: The Roles of Factor VIla and of Endothelial Cell Tissue Factor

1991 ◽  
Vol 66 (05) ◽  
pp. 559-564 ◽  
Author(s):  
Jerome M Teitel
Keyword(s):  
Factor Viii ◽  
Tissue Factor ◽  
Factor Viia ◽  
Factor Xa ◽  
Procoagulant Activity ◽  
Tissue Factor Expression ◽  
Prothrombin Complex Concentrates ◽  
Cell Tissue ◽  
Factor Expression ◽  
Necrosis Factor

SummaryAn experimental model incorporating cultured endothelial cells (EC) was used to study the "factor VIII bypassing" activity of prothrombin complex concentrates (PCC), a property exploited in the treatment of hemophiliacs with alloantibodies to factor VIII. Two PCC preparations were ineffective as stimuli of tissue factor expression by EC. However, incubation with a combination of PCC plus endotoxin (lipopolysaccharide, LPS) or tumor necrosis factor (TNF) induced much greater tissue factor expression than was seen in response to either substance alone. PCC expressed an additional direct procoagulant activity at the EC surface, which could not be attributed to either thrombin or factor Xa, and which was diminished by an anti-tissue factor antibody. Therefore factor VIIa, which was detectable in both PCC preparations, likely provided this additional direct procoagulant activity at the EC surface. We also excluded the possibility that coagulation proteases contained in or generated in the presence of PCC are protected from inactivation by AT III. Therefore, PCC can indirectly bypass factor VIII by enhancing induced endothelial tissue factor expression, and also possess direct procoagulant activity, probably mediated by factor VIIa.

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