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Brazilian Journal of Medical and... Aug 2003Tissue factor is a transmembrane procoagulant glycoprotein and a member of the cytokine receptor superfamily. It activates the extrinsic coagulation pathway, and induces... (Review)
Review
Tissue factor is a transmembrane procoagulant glycoprotein and a member of the cytokine receptor superfamily. It activates the extrinsic coagulation pathway, and induces the formation of a fibrin clot. Tissue factor is important for both normal homeostasis and the development of many thrombotic diseases. A wide variety of cells are able to synthesize and express tissue factor, including monocytes, granulocytes, platelets and endothelial cells. Tissue factor expression can be induced by cell surface components of pathogenic microorganisms, proinflammatory cytokines and membrane microparticles released from activated host cells. Tissue factor plays an important role in initiating thrombosis associated with inflammation during infection, sepsis, and organ transplant rejection. Recent findings suggest that tissue factor can also function as a receptor and thus may be important in cell signaling. The present minireview will focus on the role of tissue factor in the pathogenesis of septic shock, infectious endocarditis and invasive aspergillosis, as determined by both in vivo and in vitro models.
Topics: Aspergillosis; Blood Coagulation Factors; Endocarditis, Bacterial; Endothelial Cells; Humans; Shock, Septic; Thromboplastin
PubMed: 12886452
DOI: 10.1590/s0100-879x2003000800004 -
Journal of Thrombosis and Haemostasis :... Jan 2018Essentials Two candidate International Standards for thromboplastin (coded RBT/16 and rTF/16) are proposed. International Sensitivity Index (ISI) of proposed standards...
International collaborative study for the calibration of proposed International Standards for thromboplastin, rabbit, plain, and for thromboplastin, recombinant, human, plain.
UNLABELLED
Essentials Two candidate International Standards for thromboplastin (coded RBT/16 and rTF/16) are proposed. International Sensitivity Index (ISI) of proposed standards was assessed in a 20-centre study. The mean ISI for RBT/16 was 1.21 with a between-centre coefficient of variation of 4.6%. The mean ISI for rTF/16 was 1.11 with a between-centre coefficient of variation of 5.7%.
SUMMARY
Background The availability of International Standards for thromboplastin is essential for the calibration of routine reagents and hence the calculation of the International Normalized Ratio (INR). Stocks of the current Fourth International Standards are running low. Candidate replacement materials have been prepared. This article describes the calibration of the proposed Fifth International Standards for thromboplastin, rabbit, plain (coded RBT/16) and for thromboplastin, recombinant, human, plain (coded rTF/16). Methods An international collaborative study was carried out for the assignment of International Sensitivity Indexes (ISIs) to the candidate materials, according to the World Health Organization (WHO) guidelines for thromboplastins and plasma used to control oral anticoagulant therapy with vitamin K antagonists. Results Results were obtained from 20 laboratories. In several cases, deviations from the ISI calibration model were observed, but the average INR deviation attributabled to the model was not greater than 10%. Only valid ISI assessments were used to calculate the mean ISI for each candidate. The mean ISI for RBT/16 was 1.21 (between-laboratory coefficient of variation [CV]: 4.6%), and the mean ISI for rTF/16 was 1.11 (between-laboratory CV: 5.7%). Conclusions The between-laboratory variation of the ISI for candidate material RBT/16 was similar to that of the Fourth International Standard (RBT/05), and the between-laboratory variation of the ISI for candidate material rTF/16 was slightly higher than that of the Fourth International Standard (rTF/09). The candidate materials have been accepted by WHO as the Fifth International Standards for thromboplastin, rabbit plain, and thromboplastin, recombinant, human, plain.
Topics: Animals; Anticoagulants; Blood Coagulation; Calibration; Drug Monitoring; Humans; International Normalized Ratio; Laboratory Proficiency Testing; Observer Variation; Predictive Value of Tests; Prothrombin Time; Rabbits; Recombinant Proteins; Reference Standards; Reproducibility of Results; Thromboplastin
PubMed: 29065247
DOI: 10.1111/jth.13879 -
Trends in Molecular Medicine Feb 2019Intravascular infusion is the most popular route for therapeutic multipotent mesenchymal stromal/stem cell (MSC) delivery in hundreds of clinical trials. Meta-analysis... (Review)
Review
Intravascular infusion is the most popular route for therapeutic multipotent mesenchymal stromal/stem cell (MSC) delivery in hundreds of clinical trials. Meta-analysis has demonstrated that bone marrow MSC infusion is safe. It is not clear if this also applies to diverse new cell products derived from other sources, such as adipose and perinatal tissues. Different MSC products display varying levels of highly procoagulant tissue factor (TF) and may adversely trigger the instant blood-mediated inflammatory reaction (IBMIR). Suitable strategies for assessing and controlling hemocompatibility and optimized cell delivery are crucial for the development of safer and more effective MSC therapies.
Topics: Animals; Clinical Trials as Topic; Humans; Inflammation; Mesenchymal Stem Cell Transplantation; Mesenchymal Stem Cells; Thromboplastin
PubMed: 30711482
DOI: 10.1016/j.molmed.2018.12.006 -
Clinical Cardiology Apr 1990Recent advances in the understanding of blood coagulation provide strong evidence that exposure of tissue factor is the "match" which initiates blood coagulation. A... (Review)
Review
Recent advances in the understanding of blood coagulation provide strong evidence that exposure of tissue factor is the "match" which initiates blood coagulation. A novel plasma protease inhibitor, called EPI or LACI, effectively extinguishes this "match," leaving Factors IXa, VIII, X, V, and II to function as a "fuse." Activated Factors IX, X, and II are controlled by heparin-enhancable protease inhibitors. Activated Factors VIII and V are destroyed by the protein C/S system. Fibrinolysis is largely cell-based and controlled by differential secretion of plasminogen activators and plasminogen activator inhibitors.
Topics: Blood Coagulation; Factor VII; Fibrinolysis; Humans; Lipoproteins; Thromboplastin
PubMed: 2191814
DOI: No ID Found -
Arteriosclerosis, Thrombosis, and... Dec 2009
Review
Topics: Alternative Splicing; Animals; History, 20th Century; History, 21st Century; Humans; Signal Transduction; Thromboplastin; Thrombosis
PubMed: 19923557
DOI: 10.1161/ATVBAHA.109.198929 -
Blood Jul 2021
Topics: Cells, Cultured; Thromboplastin
PubMed: 34323941
DOI: 10.1182/blood.2021012459 -
Journal of Thrombosis and Haemostasis :... Apr 2018Essentials Tissue factor (TF) enhances factor VIIa (FVIIa) activity through structural and dynamic changes. We analyzed conservation of TF-activated FVIIa allosteric... (Comparative Study)
Comparative Study
UNLABELLED
Essentials Tissue factor (TF) enhances factor VIIa (FVIIa) activity through structural and dynamic changes. We analyzed conservation of TF-activated FVIIa allosteric networks in extant vertebrate lamprey. Lamprey Tf/FVIIa molecular dynamics show conserved Tf-induced structural/dynamic FVIIa changes. Lamprey Tf activation of FVIIa allosteric networks follows molecular pathways similar to human.
SUMMARY
Background Previous studies have provided insight into the molecular basis of human tissue factor (TF) activation of activated factor VII (FVIIa). TF-induced allosteric networks of FVIIa activation have been rationalized through analysis of the dynamic changes and residue connectivities in the human soluble TF (sTF)/FVIIa complex structure during molecular dynamics (MD) simulation. Evolutionary conservation of the molecular mechanisms for TF-induced allosteric FVIIa activation between humans and extant vertebrate jawless fish (lampreys), where blood coagulation emerged more than 500 million years ago, is unknown and of considerable interest. Objective To model the sTf/FVIIa complex from cloned Petromyzon marinus lamprey sequences, and with comparisons to human sTF/FVlla investigate conservation of allosteric mechanisms of FVIIa activity enhancement by soluble TF using MD simulations. Methods Full-length cDNAs of lamprey tf and f7 were cloned and characterized. Comparative models of lamprey sTf/FVIIa complex and free FVIIa were determined based on constructed human sTF/FVIIa complex and free FVIIa models, used in full-atomic MD simulations, and characterized using dynamic network analysis approaches. Results Allosteric paths of correlated motion from Tf contact points in lamprey sTf/FVIIa to the FVIIa active site were determined and quantified, and were found to encompass residue-residue interactions along significantly similar paths compared with human. Conclusions Despite low conservation of residues between lamprey and human proteins, 30% TF and 39% FVII, the structural and protein dynamic effects of TF activation of FVIIa appear conserved and, moreover, present in extant vertebrate proteins from 500 million years ago when TF/FVIIa-initiated extrinsic pathway blood coagulation emerged.
Topics: Allosteric Regulation; Amino Acid Sequence; Animals; Blood Coagulation; Cloning, Molecular; Conserved Sequence; Evolution, Molecular; Factor VIIa; Fish Proteins; Humans; Lampreys; Molecular Dynamics Simulation; Protein Conformation; Prothrombin Time; Structure-Activity Relationship; Thromboplastin
PubMed: 29418058
DOI: 10.1111/jth.13968 -
Arteriosclerosis, Thrombosis, and... Jan 2021
Topics: Aldehydes; Cell-Derived Microparticles; Extracellular Vesicles; Oxidative Stress; Thromboplastin
PubMed: 33356372
DOI: 10.1161/ATVBAHA.120.315437 -
Arteriosclerosis, Thrombosis, and... Jan 2005How does tissue factor (TF), whose principle role is to support clotting factor VIIa (FVIIa) in triggering the coagulation cascade, affect various pathophysiological... (Review)
Review
How does tissue factor (TF), whose principle role is to support clotting factor VIIa (FVIIa) in triggering the coagulation cascade, affect various pathophysiological processes? One of the answers is that TF interaction with FVIIa not only initiates clotting but also induces cell signaling via activation of G-protein-coupled protease activated receptors (PARs). Recent studies using various cell model systems and limited in vivo systems are beginning to define how TF-VIIa-induced signaling regulates cellular behavior. Signaling pathways initiated by both TF-VIIa protease activation of PARs and phosphorylation of the TF-cytoplasmic domain appear to regulate cellular functions. In the present article, we review the emerging data on the mechanism of TF-mediated cell signaling and how it regulates various cellular responses, with particular focus on TF-VIIa protease-dependent signaling.
Topics: Animals; Factor VIIa; Humans; Signal Transduction; Thromboplastin
PubMed: 15569823
DOI: 10.1161/01.ATV.0000151624.45775.13 -
International Journal of Molecular... Jun 2022Histones are cationic nuclear proteins that are essential for the structure and functions of eukaryotic chromatin. However, extracellular histones trigger inflammatory...
Histones are cationic nuclear proteins that are essential for the structure and functions of eukaryotic chromatin. However, extracellular histones trigger inflammatory responses and contribute to death in sepsis by unknown mechanisms. We recently reported that inflammasome activation and pyroptosis trigger coagulation activation through a tissue-factor (TF)-dependent mechanism. We used a combination of various deficient mice to elucidate the molecular mechanism of histone-induced coagulation. We showed that histones trigger coagulation activation in vivo, as evidenced by coagulation parameters and fibrin deposition in tissues. However, histone-induced coagulopathy was neither dependent on intracellular inflammasome pathways involving caspase 1/11 and gasdermin D (GSDMD), nor on cell surface receptor TLR2- and TLR4-mediated host immune response, as the deficiency of these genes in mice did not protect against histone-induced coagulopathy. The incubation of histones with macrophages induced lytic cell death and phosphatidylserine (PS) exposure, which is required for TF activity, a key initiator of coagulation. The neutralization of TF diminished the histone-induced coagulation. Our findings revealed lytic cell death as a novel mechanism of histone-induced coagulation activation and thrombosis.
Topics: Animals; Disseminated Intravascular Coagulation; Histones; Inflammasomes; Mice; Pyroptosis; Thromboplastin
PubMed: 35743244
DOI: 10.3390/ijms23126800