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Ticagrelor, but not clopidogrel, reduces arterial thrombosis via endothelial tissue factor suppression. Ticagrelor reduced TNF-alpha (show TNF Proteins)-induced TF expression via proteasomal degradation.
Macrophage tissue factor prothrombotic activity is regulated by integrin-alpha4/arf6 (show ARF6 Proteins) trafficking.
Evening primrose oil and forskolin decreased the prothrombotic effect of celecoxib initiated by a LPS (show TLR4 Proteins) challenge in mice, and this effect was, at least partly, mediated by mitigating TF expression and activity.
Thrombin (show F2 Proteins)-independent contribution of tissue factor to inflammation and cardiac hypertrophy in a mouse model of sickle cell disease.
These findings reveal a novel biological function and mechanism of the protein C (show PROC Proteins) pathway in which protein S and the aPC (show APC Proteins)-cleaved form of fV are cofactors for anti-inflammatory cell signaling by aPC (show APC Proteins) in the context of endotoxemia and infection
Lung epithelial tissue factor regulates alveolar procoagulant activity and permeability in acute lung injury.
PGE2 increases both TF expression and activity through the regulation of the EP1 (show PTGER1 Proteins)/SIRT1 (show SIRT1 Proteins) pathway.
Fas (show FAS Proteins)-initiated, caspase-3 (show CASP3 Proteins)-dependent hepatocyte apoptosis increases tissue factor procoagulant activity through a mechanism involving phosphatidylserine externalization.
Heme promotes tissue factor-dependent coagulation activation and induces tissue factor expression on leukocytes in vivo.
TF is essential for the development of pericyte coverage of tumor microvessels and aPL (show FASL Proteins)-induced tumor cell expression of chemokine ligand 2 (show CXCL2 Proteins), a mediator of pericyte recruitment
The proinflammatory cytokine IL-33 (show IL33 Proteins) induces differential tissue factor expression and activity in monocyte subsets, as well as the release of procoagulant microvesicless. In this manner, IL-33 (show IL33 Proteins) may contribute to the formation of a prothrombotic state characteristic for cardiovascular disease.
Pin1 (show PIN1 Proteins) is a fast-acting enzyme which may be utilised by cells to protect the phosphorylation state of TF in activated cells prolonging TF activity and release, and therefore ensuring adequate haemostasis.
Circulating pentraxin nCRP has little pro-angiogenic effect but when dissociated into mCRP on the surface of endothelial cells it is able to trigger potent proangiogenic effects by inducing F3-gene upregulation and TF signaling.
In the presence of tissue factor-positive cancer cells, the CAR-modified T cells (TF-CAR T) were highly activated and showed specific cytotoxicity to TF-positive cancer cells.
TF is an angiogenic-specific receptor and the target molecule for fVII (show F7 Proteins)-targeted therapeutics.
It was demonstrated that the nature of the clot (show TXNDC17 Proteins) formed, as determined from the quartz crystal microbalance parameters, was highly dependent on the rate of clot (show TXNDC17 Proteins) formation resulting from the TF concentration used for activation. These parameters could also be related to physical clot (show TXNDC17 Proteins) characteristics such as fibrin fibre diameter and fibre density, as determined by scanning electron microscopic image analysis.
Through induction of TF in vascular endothelial cells, IL-33 (show IL33 Proteins) could enhance their thrombotic capacity and thereby might impact on thrombus formation in the setting of atherosclerosis.
Tissue Factor was highly expressed in 73.6 % of osteosarcoma biopsies, and expression associated significantly with disease-free survival.
Platelet tissue factor activity and membrane cholesterol are increased in hypercholesterolemia and normalized by rosuvastatin, but not by atorvastatin.
the identification of platelet TF and TLR4 (show TLR4 Proteins) as regulators of the effect of E. coli O111 might represent a novel therapeutic target to reduce the devastating consequences of the hemostatic disorder during sepsis.
Arterial (18)F-fluorodeoxyglucose uptake reflects balloon catheter-induced thrombus formation and tissue factor expression via nuclear factor-kappaB in rabbit atherosclerotic lesions.
Polycations could present a new class of anticoagulants with such unique upstream downregulation of blood coagulation, selectively blocking tissue factor-dependent factor VII (show TH Proteins) activation.
Upregulated TF expression and increased plasma TF level during reperfusion period, reduced plasma TFPI-1 (show TFPI Proteins) level during reperfusion period.
lectin-like oxidized LDL receptor (show OLR1 Proteins) Oxidized low-density lipoprotein receptor (show LDLR Proteins) 1expression appears to be closely associated with tissue factor expression, apoptotic events and morphological vulnerability in atherosclerotic lesions
Tissue factor expression on porcine neonatal islet cell clusters is an important initiator of instant blood-mediated inflammatory reaction in islet xenotransplantation.
Prolonged clopidogrel treatment reduced coronary tissue factor (TF) expression and tended to reduce the blood TF level post-PCI (show SERPINA5 Proteins), thus possibly modulating the risk of late thrombosis.
Procoagulant porcine tissue factor is induced in primary pig aortic endothelial cells only by fresh human plasma, and not by heat-inactivated plasma.
myocardial infarction induced proinflammatory gene and protein expression in peripheral blood mononuclear cells of tissue factor cyclo-oxygenase-2, monocyte chemoattractant protein-1 (show CCL2 Proteins) and CRP (show CRP Proteins)
This gene encodes coagulation factor III which is a cell surface glycoprotein. This factor enables cells to initiate the blood coagulation cascades, and it functions as the high-affinity receptor for the coagulation factor VII. The resulting complex provides a catalytic event that is responsible for initiation of the coagulation protease cascades by specific limited proteolysis. Unlike the other cofactors of these protease cascades, which circulate as nonfunctional precursors, this factor is a potent initiator that is fully functional when expressed on cell surfaces. There are 3 distinct domains of this factor: extracellular, transmembrane, and cytoplasmic. This protein is the only one in the coagulation pathway for which a congenital deficiency has not been described. Alternate splicing results in multiple transcript variants.
, coagulation factor III
, tissue factor
, brain tissue factor
, coagulation factor 3