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Critical Reviews in Biochemistry and... 2015The plasma coagulation system in mammalian blood consists of a cascade of enzyme activation events in which serine proteases activate the proteins (proenzymes and... (Review)
Review
The plasma coagulation system in mammalian blood consists of a cascade of enzyme activation events in which serine proteases activate the proteins (proenzymes and procofactors) in the next step of the cascade via limited proteolysis. The ultimate outcome is the polymerization of fibrin and the activation of platelets, leading to a blood clot. This process is protective, as it prevents excessive blood loss following injury (normal hemostasis). Unfortunately, the blood clotting system can also lead to unwanted blood clots inside blood vessels (pathologic thrombosis), which is a leading cause of disability and death in the developed world. There are two main mechanisms for triggering the blood clotting, termed the tissue factor pathway and the contact pathway. Only one of these pathways (the tissue factor pathway) functions in normal hemostasis. Both pathways, however, are thought to contribute to thrombosis. An emerging concept is that the contact pathway functions in host pathogen defenses. This review focuses on how the initiation phase of the blood clotting cascade is regulated in both pathways, with a discussion of the contributions of these pathways to hemostasis versus thrombosis.
Topics: Animals; Blood Coagulation; Hemostasis; Humans; Models, Biological; Platelet Activation; Proteolysis; Thromboplastin; Thrombosis
PubMed: 26018600
DOI: 10.3109/10409238.2015.1050550 -
Lancet (London, England) Apr 1978
Topics: Prothrombin Time; Thromboplastin
PubMed: 76256
DOI: 10.1016/s0140-6736(78)90831-0 -
Haemostasis 1988Molecular genetics, biochemistry, and cell biology of thromboplastin are briefly reviewed with special emphasis on its biosynthesis by endothelial cells. (Review)
Review
Molecular genetics, biochemistry, and cell biology of thromboplastin are briefly reviewed with special emphasis on its biosynthesis by endothelial cells.
Topics: Animals; Cloning, Molecular; Endothelium; Glycosylation; Humans; Molecular Structure; Protein Sorting Signals; Signal Transduction; Thromboplastin; Tissue Distribution
PubMed: 3069639
DOI: 10.1159/000215809 -
British Medical Journal Sep 1971
Topics: Prothrombin; Thromboplastin; United Kingdom
PubMed: 5569990
DOI: 10.1136/bmj.3.5775.638-c -
Thrombosis and Haemostasis Aug 1977
Topics: Humans; Thromboplastin
PubMed: 579502
DOI: No ID Found -
International Journal of Laboratory... Jun 2020
Comparative Study
Topics: Aged; Female; Humans; Indicators and Reagents; Male; Middle Aged; Prothrombin Time; Thromboplastin
PubMed: 32110846
DOI: 10.1111/ijlh.13172 -
Advances in Experimental Medicine and... 2020The hemostatic cascade is initiated by the transmembrane coagulation proteinĀ - tissue factor (TF) and eventuates in fibrin formation. Heparanase protein was... (Review)
Review
The hemostatic cascade is initiated by the transmembrane coagulation proteinĀ - tissue factor (TF) and eventuates in fibrin formation. Heparanase protein was demonstrated to directly enhance TF activity resulting in increased activation of the coagulation system. In addition, heparanase was found to increase hemostatic system activation via two other mechanisms: up-regulating TF expression in endothelial cells and releasing the protein tissue factor pathway inhibitor (TFPI) from the cell surface. Peptides derived from TFPI-2, a protein similar to TFPI, were shown to inhibit the TF/heparanase complex as well as attenuate sepsis and tumor growth. Increased heparanase procoagulant activity was observed in several clinical settings, including women using oral contraceptives, women at delivery, patients following orthopedic surgery and patients with diabetic foot, shift work female nurses, patients with lung cancer, retinal vein thrombosis and prosthetic heart valve thrombosis. Remarkably, the heparanase profile was significantly different across the tested groups. Inhibition of TF / heparanase interaction may represent a new target for attenuating coagulation, cancer and inflammation.
Topics: Blood Coagulation; Endothelial Cells; Glucuronidase; Humans; Inflammation; Neoplasms; Thromboplastin
PubMed: 32274737
DOI: 10.1007/978-3-030-34521-1_33 -
Thrombosis Research May 2012Tissue factor plays a primary role in both hemorrhage control and thrombosis depending upon whether its presentation is extravascular or intravascular. The molecular... (Review)
Review
Tissue factor plays a primary role in both hemorrhage control and thrombosis depending upon whether its presentation is extravascular or intravascular. The molecular architecture and function of the tissue factor molecule and its role in the activations of factor IX and factor X have been elegantly elucidated but controversies prevail with respect to distinctions between tissue factor sources and tissue factor "activity." This presentation will review data on the architecture and functions of the tissue factor-factor VIIa complex and discuss the elements of the controversies associated with tissue factor presentation in both normal and pathologic milieu.
Topics: Animals; Factor VIIa; Humans; Models, Molecular; Thromboplastin
PubMed: 22401799
DOI: 10.1016/j.thromres.2012.02.018 -
Journal of Clinical Pathology Oct 1989
Topics: Humans; Prothrombin Time; Quality Control; Thromboplastin
PubMed: 2584421
DOI: 10.1136/jcp.42.10.1118-b -
Clinical and Laboratory Haematology Sep 1995Tissue thromboplastin inhibition assay (TTI) is a sensitive test for lupus anticoagulant (LA). We have performed TTI in 12 LA positive patients using a new recombinant...
Tissue thromboplastin inhibition assay (TTI) is a sensitive test for lupus anticoagulant (LA). We have performed TTI in 12 LA positive patients using a new recombinant human tissue factor (Innovin, IN) and compared it with Thromborel S (TH), a commonly used human placenta thromboplastin. The effect of using two different dilutions of each thromboplastin (1:10 & 1:26) was investigated. A 1:26 dilution discriminated better than the 1:10 and this was more evident for Innovin. The mean value obtained with a 1:26 IN dilution was statistically different from that observed with TH at the same dilution. Furthermore, when PT and TTI ratios were considered, differences were statistically significant and seemed to increase depending on thromboplastin dilutions. When we used IN at 1:26 all LA positive patients had a value > 1.2. Then we compared TTI at a 1:26 dilution with dilute Russell's Viper Venom Time (dRVVT) in 50 consecutive patients with suspected lupus anticoagulant not treated with warfarin or heparin. In these patients the diagnosis of lupus anticoagulant was carried out using dilute APTT mixing studies and a platelet neutralization procedure: four out of 50 patients thus tested were LA positive. When dRVVT or TTI-I 1:26 were used, five patients were positive for lupus anticoagulant. Innovin showed similar sensitivity of dRVVT for detection of lupus anticoagulant. It is likely that higher dilutions of thromboplastins could further improve the specificity of this method.
Topics: Adult; Case-Control Studies; Female; Humans; Lupus Coagulation Inhibitor; Male; Middle Aged; Recombinant Proteins; Sensitivity and Specificity; Thromboplastin
PubMed: 8719896
DOI: No ID Found