Effects of tissue factor induced by oxygen free radicals on coronary flow during reperfusion

Golino, Paolo; Ragni, Maurizio; Cirillo, Plinio; Avvedimento, Vittorio Enrico; Feliciello, Antonio; Esposito, Nicola; Scognamiglio, Annalisa; Trimarco, Bruno; Iaccarino, Guido; Condorelli, M; Chiariello, Massimo; Ambrosio, Giuseppe

doi:10.1038/nm0196-35

Cited by 171 publications

(123 citation statements)

References 32 publications

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“…One of the first indications for a nonhemostatic function of TF was its characterization as an immediate early gene that can be induced during cell division 16 and in response to pathophysiologically relevant stimuli, such as cytokines, 17 growth factors, 18 oxidized LDL, 19 and oxygen free radicals. 20 An exciting recent development in TF biology was the demonstration that this protein, a member of the cytokine receptor superfamily, can function as a true signaling receptor. Indeed, signaling via TF has now been documented in many different cell types, including keratinocytes, bladder carcinoma cells, COS-1, and BHK cells.…”

Section: Discussionmentioning

confidence: 99%

Tissue Factor Binding of Activated Factor VII Triggers Smooth Muscle Cell Proliferation via Extracellular Signal–Regulated Kinase Activation

et al. 2004

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Background-Tissue factor (TF) is the main initiator of coagulation in vivo. Recently, however, a role for TF as a cell receptor involved in signal transduction has been suggested. The aim of the present study was to assess whether activated factor VII (FVIIa) binding to TF could induce smooth muscle cell (SMC) proliferation and to clarify the possible intracellular mechanism(s) responsible for this proliferation. Methods and Results-Cell proliferation was induced by FVIIa in a dose-dependent manner, as assessed by [3 H]thymidine incorporation and direct cell counting, whereas no response was observed with active site-inhibited FVIIa (FVIIai), which is identical to FVIIa but is devoid of enzymatic activity. Similarly, no proliferation was observed when binding of FVIIa to TF was prevented by the monoclonal anti-TF antibody AP-1. Activation of the p44/42 mitogen-activated protein (MAP) kinase (extracellular signal-regulated kinases 1 and 2 [ERK 1/2]) pathway on binding of FVIIa to TF was demonstrated by transient ERK phosphorylation in Western blots and by suppression of proliferation with the specific MEK (MAP kinase/ERK kinase) inhibitor UO126. ERK phosphorylation was not observed with FVIIai or when cells were pretreated with AP-1. Conclusions-These data indicate a specific effect by which binding of FVIIa to TF on the surface of SMCs induces proliferation via a coagulation-independent mechanism and possibly indicate a new link between coagulation, inflammation, and atherosclerosis. Key Words: coagulants Ⅲ signal transduction Ⅲ cell division T issue factor (TF) is a cell surface-anchored glycoprotein that binds both the zymogen factor VII (FVII) and the active serine protease factor VIIa (FVIIa). 1 TF/FVIIa complex activates coagulation by cleaving its natural substrates, factors IX and X, ultimately leading to thrombin generation, fibrin deposition, and platelet activation. 1,2 On these grounds, TF has been considered to function as a major initiator of blood coagulation in vivo. Recently, however, some evidence has suggested that TF may mediate important coagulationindependent biological phenomena, including embryonic and oncogenic angiogenesis, 3,4 and inflammation. 5 In addition, recent data indicate that TF/FVIIa interaction may activate different intracellular signals, culminating in a variety of cell responses, thus suggesting a role for TF as a "true" cell membrane receptor. For example, TF/FVIIa interaction has been shown to be a strong chemotactic stimulus for smooth muscle cells (SMCs), mediating their migration in vitro. 6 FVIIa has been also shown to induce phosphorylation of the extracellular signalregulated kinases 1 and 2 (ERK 1/2) 7 and to upregulate poly(A) polymerase, 8 urokinase-type plasminogen activator receptor, 9 and a host of genes identified with the use of cDNA microarrays. 10 However, despite evidence suggesting close links between TF, activation of coagulation, and intracellular signaling, no direct effects of TF/FVIIa on SMC proliferation have yet been demonstrated. Thus, in the pr...

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Section: Discussionmentioning

confidence: 99%

Tissue Factor Binding of Activated Factor VII Triggers Smooth Muscle Cell Proliferation via Extracellular Signal–Regulated Kinase Activation

et al. 2004

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“…antibodies, to degranulation and the production of reactive oxygen species, resulting in endothelial cytotoxicity (2,(6)(7)(8)(9). Interestingly, Golino et a1 have shown that reactive oxygen species produced by neutrophils induce TF expression on endothelial cells (43). In addition, we and others have shown that reactive oxygen species, anti-PR3, IL-1, and TNFa (alone or in combination) can increase the capacity of the endothelium to bind neutrophils (20)(21)(22)25,28,44).…”

Section: Discussionmentioning

confidence: 99%

Induction of interleukin‐1 and subsequent tissue factor expression by anti‐proteinase 3 antibodies in human umbilical vein endothelial cells

Bandt

Ollivier

Meyer

et al. 1997

Arthritis & Rheumatism

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Objective. To assess the ability of anti‐proteinase 3 (anti‐PR3) classic antineutrophil cytoplasmic antibodies (cANCA) to stimulate endothelial expression of tissue factor (TF), which is the main initiator of the coagulation cascade that can lead to endothelial injury and thrombosis in patients with Wegener's granulomatosis. Methods. Human umbilical vein endothelial cells (HUVEC) were grown to confluence and stimulated with affinity‐purified anti‐PR3 antibodies, Igs from healthy subjects, and endotoxin (lipopolysaccharide) as positive control. Results. TF activity was generated in anti‐PR3‐ stimulated cells, as shown by a chromogenic test. This activity was inhibited by specific anti‐TF antibodies. TF messenger RNA (mRNA) was found in anti‐PR3‐ stimulated cells, as detected by reverse transcriptasepolymerase chain reaction, but not in cells stimulated with irrelevant human Igs or Igs from normal control sera. TF expression reached maximum levels 12 hours after exposure to the anti‐PR3 cANCA, and did not require complement. TF mRNA expression was inhibited by cycloheximide, suggesting a requirement for protein synthesis. When added to the incubation medium, interleukin‐1 (IL‐1) receptor antagonist inhibited the induced TF mRNA expression, suggesting that cANCA‐stimulated cells initiate IL‐1 synthesis. Moreover, cANCA induced IL‐lα mRNA before TF mRNA. Conclusion. This study showed that anti‐PR3 treatment of HUVEC induces sequential expression of IL‐lα mRNA and TF mRNA, as well as their corresponding proteins. Both proteins could have pathogenic roles in the vasculitic process, since TF is the main initiator of the coagulation cascade.

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“…Accelerated activation of the coagulation system may lead to pathological conditions, such as stroke 23 and coronary artery disease. 24 On the other hand, certain factor VII genotypes associated with lower plasma factor VII levels (and thus lower prothrombinase activity) are thought to protect against myocardial infarction. 25 Platelets express this procoagulant activity in response to collagens or CVX in a dose-dependent manner, as reported by Alberio et al 11 and confirmed by our results in the present study.…”

Section: Furihata Et Almentioning

confidence: 99%

Variation in Human Platelet Glycoprotein VI Content Modulates Glycoprotein VI–Specific Prothrombinase Activity

Furihata

Clemetson

Deguchi

et al. 2001

ATVB

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Abstract-Glycoprotein VI (GPVI) is a platelet-specific receptor for collagen that figures prominently in signaltransduction. An addition to binding to type I and III collagens, GPVI is also bound specifically by collagen-related peptide and convulxin (CVX), a snake venom protein. We developed a quantitative assay of platelet GPVI in which biotin-conjugated CVX binds selectively to GPVI in separated total platelet proteins by a ligand blot procedure. Using this approach, we have documented a 5-fold range in platelet GPVI content among 23 normal healthy subjects. In addition, we have determined that CVX-induced or collagen-related peptide-induced prothrombinase activity is directly proportional to the platelet content of GPVI. A statistically significant correlation was observed at 2 CVX concentrations: 14.7 ng/mL (R 2 ϭ0.854 and PϽ0.001, nϭ11) and 22 ng/mL (R 2 ϭ0.776 and PϽ0.001, nϭ12). In previous studies, we established a similar range of expression of the integrin collagen receptor ␣ 2 ␤ 1 on platelets of normal subjects. Among 15 donors, there is a direct correlation between platelet ␣ 2 ␤ 1 density and GPVI content (R 2 ϭ0.475 and Pϭ0.004). In view of the well-documented association of GPVI with platelet procoagulant activity, this study suggests that the variation in GPVI content is a potential risk factor that may predispose individuals to hemorrhagic or thromboembolic disorders.

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Effects of tissue factor induced by oxygen free radicals on coronary flow during reperfusion

Cited by 171 publications

References 32 publications

Tissue Factor Binding of Activated Factor VII Triggers Smooth Muscle Cell Proliferation via Extracellular Signal–Regulated Kinase Activation

Tissue Factor Binding of Activated Factor VII Triggers Smooth Muscle Cell Proliferation via Extracellular Signal–Regulated Kinase Activation

Induction of interleukin‐1 and subsequent tissue factor expression by anti‐proteinase 3 antibodies in human umbilical vein endothelial cells

Variation in Human Platelet Glycoprotein VI Content Modulates Glycoprotein VI–Specific Prothrombinase Activity

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