Tissue Factor in Health and Disease

Semeraro, Nicola; Colucci, Mario

doi:10.1055/s-0038-1657625

Cited by 180 publications

(156 citation statements)

References 68 publications

(43 reference statements)

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“…25 More recently, a role for TF in signal transduction, tumor metastasis, growth, wound-healing, and angiogenesis has been reported. [25][26][27] Under physiological conditions, the transmembrane form of TF is exclusively expressed by extravascular cells. How- …”

Section: Discussionmentioning

confidence: 99%

Elevated Numbers of Tissue-Factor Exposing Microparticles Correlate With Components of the Metabolic Syndrome in Uncomplicated Type 2 Diabetes Mellitus

et al. 2002

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Background— Type 2 diabetes is associated with accelerated atherosclerosis. Because cell-derived microparticles support coagulation and inflammation, they may be involved in atherogenesis. We characterized circulating microparticles both in patients with uncomplicated, well-regulated type 2 diabetes and in healthy subjects, as well as their relationship with coagulation and metabolic control. Methods and Results— Microparticles were isolated from plasma, stained with annexin V, cell-specific monoclonal antibodies (MoAbs) and a MoAb directed against tissue factor (TF), and analyzed by flow cytometry. Microparticle numbers and origin were comparable in the two groups, but the median number of TF-positive microparticles was twice as high in patients than in controls ( P =0.018). Patients had higher percentages of TF-positive microparticles from T-helper cells ( P =0.045), granulocytes ( P =0.004), and platelets ( P =0.002). Subpopulations of TF-positive microparticles from platelets and T-helper cells exposed granulocytic markers. Correlations were found between the numbers of various TF-positive microparticle subpopulations and body mass index, fasting plasma glucose and insulin, or tumor necrosis factor-α and serum HDL cholesterol. Microparticles from patients generated less thrombin in vitro ( P =0.007). Microparticle numbers did not correlate with in vivo coagulation markers prothrombin fragment F 1+2 and thrombin-antithrombin complexes. Conclusions— TF, possibly of granulocytic origin, is exposed on microparticle subpopulations in asymptomatic patients with well-regulated type 2 diabetes. TF-positive microparticles are associated with components of the metabolic syndrome but not with coagulation. Thus, TF on microparticles may be involved in processes other than coagulation, including transcellular signaling or angiogenesis.

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Section: Discussionmentioning

confidence: 99%

Elevated Numbers of Tissue-Factor Exposing Microparticles Correlate With Components of the Metabolic Syndrome in Uncomplicated Type 2 Diabetes Mellitus

et al. 2002

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“…Lymphocytes, which do not express TF themselves, are required for optimal TF production by monocytes/macrophages (18). Hypercoagulability associated with vascular disease is considered to be principally mediated by TF expressed within atherosclerotic plaque, and on monocytes in the circulation (20,21), and TF expression is associated with macrophage-mediated fibrin deposition, which is common in most inflammatory lesions (22). In this study, we show a potent and rapid induction of TF activity, mRNA, and protein on normal human monocytes by SAA.…”

Section: Serum Amyloid a Induces Monocyte Tissue Factormentioning

confidence: 99%

Serum Amyloid A Induces Monocyte Tissue Factor

Cai

Song

Endoh

et al. 2007

The Journal of Immunology

106

121

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C-reactive protein (CRP) and serum amyloid A (SAA) increase in the blood of patients with inflammatory conditions and CRP-induced monocyte tissue factor (TF) may contribute to inflammation-associated thrombosis. This study demonstrates that SAA is a potent and rapid inducer of human monocyte TF. SAA induced TF mRNA in PBMC within 30 min and optimal procoagulant activity within 4 h, whereas CRP (25 μg/ml)-induced activity was minimal at this time. Unlike CRP, SAA did not synergize with LPS. Procoagulant activity was inhibited by anti-TF and was dependent on factors VII and X, and TF Ag levels were elevated on CD14+ monocytes. Responses were optimal with lymphocytes, although these were not obligatory. Inhibitor studies indicate activation of NF-κB through the ERK1/2 and p38 MAPK pathways; the cyclo-oxygenase pathway was not involved. SAA-induced TF was partially inhibited by high-density lipoprotein, but not by low-density lipoprotein or by apolipoprotein A-I. SAA is a ligand for the receptor for advanced glycation end products (RAGE), and TF generation was suppressed by ∼50% by a RAGE competitor, soluble RAGE, and by ∼85% by anti-RAGE IgG. However, another RAGE ligand, high mobility group box-1 protein, capable of inducing monocyte chemotactic protein-1 mRNA in 2 h, did not induce TF within 24 h. Cross-linking studies confirmed SAA binding to soluble RAGE. Elevated SAA is a marker of disease activity in patients with rheumatoid arthritis, and PBMC from patients with rheumatoid arthritis were more sensitive to SAA than normals, suggesting a new link between inflammation and thrombosis.

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“…The extracellular part of TF is structured in two fibronectin type III-like domains, which shows structural and sequence homology to the cytokine receptor superfamily. The important role of TF in hemostasis and thrombotic disorders such as atherogenesis is well established (see (1)(2)(3)(4)(5)). Recent findings suggest that TF may participate in biological processes other than hemostasis such as angiogenesis (6), embryo vascularization (7), and tumor metastasis (8,9).…”

mentioning

confidence: 99%

Factor VIIa-induced p44/42 Mitogen-activated Protein Kinase Activation Requires the Proteolytic Activity of Factor VIIa and Is Independent of the Tissue Factor Cytoplasmic Domain

Sørensen¹,

Freskgård²,

Nielsen³

et al. 1999

Journal of Biological Chemistry

106

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The extrinsic pathway of blood coagulation is initiated when factor VIIa (FVIIa) 1 circulating in plasma binds to the integral membrane protein, tissue factor (TF), exposed to the blood upon injury of the vessel wall. TF consists of a 219-residue (1-219) extracellular domain, a 23-residue (220 -242) transmembrane domain, and a 21-residue (243-263) cytoplasmic domain. The extracellular part of TF is structured in two fibronectin type III-like domains, which shows structural and sequence homology to the cytokine receptor superfamily. The important role of TF in hemostasis and thrombotic disorders such as atherogenesis is well established (see (1-5)). Recent findings suggest that TF may participate in biological processes other than hemostasis such as angiogenesis (6), embryo vascularization (7), and tumor metastasis (8, 9). Furthermore, it has been reported that binding of FVIIa to cell surface TF-induced intracellular Ca 2ϩ oscillations in a number of TFexpressing cells (10, 11), transient phosphorylation of tyrosine in monocytes (12), alteration in gene expression in fibroblasts (13), and enhanced expression of urokinase receptor in pancreatic cancer cells (14). Additional information about FVIIa/TFinduced signal transduction comes from our previous report showing that binding of FVIIa to cell surface TF resulted in phosphorylation of p44/42 MAPK (15).A potential role for the TF cytoplasmic domain in signal transduction was indicated by studies showing that TF expression markedly increased the metastatic potential of melanoma cells (16) and that the pro-metastatic property was critically dependent on this domain (8, 9). This supposition was further substantiated by experiments showing that the cytoplasmic domain of TF can be phosphorylated by a protein kinase C-dependent mechanism (17) and that a synthetic peptide based on the cytoplasmic domain can work as a substrate for cell lysate protein kinase activity (18). Furthermore, cysteine 245 in the TF cytoplasmic domain was shown to be acylated with long chain fatty acids (19).Although a number of studies, as referred above, suggest that TF is involved in induction of an intracellular activity, it is not clear how signal transduction is mediated across the membrane as a result of binding of FVIIa to TF, just as the role of the cytoplasmic domain of TF in this process is still unclear. The present study explores the effect of removing the TF cytoplasmic domain on p44/42 MAPK signaling and further examines the importance of FVIIa catalytic activity in mediating the activation of the p44/42 MAPK pathway. Our data show that the cytoplasmic TF domain with its putative sites for regulatory modifications is not required for FVIIa-induced p44/42 MAPK phosphorylation. Furthermore, the data provide evidence that specific FVIIa catalytic activity is required and that other serine proteases fail to mimic the response, suggesting that TF/FVIIa may be activating a novel receptor on the cell surface. EXPERIMENTAL PROCEDURESCell Culture-The baby hamster kidney cell line BHK-21 tk...

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Tissue Factor in Health and Disease

Cited by 180 publications

References 68 publications

Elevated Numbers of Tissue-Factor Exposing Microparticles Correlate With Components of the Metabolic Syndrome in Uncomplicated Type 2 Diabetes Mellitus

Elevated Numbers of Tissue-Factor Exposing Microparticles Correlate With Components of the Metabolic Syndrome in Uncomplicated Type 2 Diabetes Mellitus

Serum Amyloid A Induces Monocyte Tissue Factor

Factor VIIa-induced p44/42 Mitogen-activated Protein Kinase Activation Requires the Proteolytic Activity of Factor VIIa and Is Independent of the Tissue Factor Cytoplasmic Domain

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