Fibrinogenolysis

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Fibrinogenolysis
Specialty Hematology

Primary fibrinogenolysis is a medical condition that appears with abnormal production of fibrinogen/fibrin degradation products (FDP), degradation of coagulation factors V, VIII, IX, XI and/or degradation of the fibrin present in any pre-existing localized thrombi and hemostatic clots. [1] [2]

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<span class="mw-page-title-main">Thrombus</span> Blood clot

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Fibrinogen is a glycoprotein complex, produced in the liver, that circulates in the blood of all vertebrates. During tissue and vascular injury, it is converted enzymatically by thrombin to fibrin and then to a fibrin-based blood clot. Fibrin clots function primarily to occlude blood vessels to stop bleeding. Fibrin also binds and reduces the activity of thrombin. This activity, sometimes referred to as antithrombin I, limits clotting. Fibrin also mediates blood platelet and endothelial cell spreading, tissue fibroblast proliferation, capillary tube formation, and angiogenesis and thereby promotes revascularization and wound healing.

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Thrombin is a serine protease, an enzyme that, in humans, is encoded by the F2 gene. Prothrombin is proteolytically cleaved to form thrombin in the clotting process. Thrombin in turn acts as a serine protease that converts soluble fibrinogen into insoluble strands of fibrin, as well as catalyzing many other coagulation-related reactions.

Fibrinolysis is a process that prevents blood clots from growing and becoming problematic. Primary fibrinolysis is a normal body process, while secondary fibrinolysis is the breakdown of clots due to a medicine, a medical disorder, or some other cause.

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D-dimer is a Dimer (dahy-mer) that is a fibrin degradation product, a small protein fragment present in the blood after a blood clot is degraded by fibrinolysis. It is so named because it contains two D fragments of the fibrin protein joined by a cross-link, hence forming a protein dimer.

<span class="mw-page-title-main">Factor XIII</span>

Factor XIII or fibrin stabilizing factor is a zymogen found in blood of humans and some other animals. It is activated by thrombin to factor XIIIa. Factor XIIIa is an enzyme of the blood coagulation system that crosslinks fibrin. Deficiency of XIII worsens clot stability and increases bleeding tendency.

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<span class="mw-page-title-main">Fibrin degradation product</span>

Fibrin degradation products (FDPs), also known as fibrin split products, are components of the blood produced by clot degeneration. Clotting, also called coagulation, at the wound site produces a mass of fibrin threads called a net that remains in place until the cut is healed. As a cut heals, the clotting slows down. Eventually the clot is broken down and dissolved by plasmin. When the clot and fibrin net dissolve, fragments of protein are released into the body. These fragments are fibrin degradation products or FDPs. If your body is unable to dissolve a clot, you may have abnormal levels of FDPs. The most notable subtype of fibrin degradation products is D-dimer.

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Fibrinogen alpha chain is a protein that in humans is encoded by the FGA gene.

<span class="mw-page-title-main">Fibrinogen beta chain</span> Protein-coding gene in the species Homo sapiens

Fibrinogen beta chain, also known as FGB, is a gene found in humans and most other vertebrates with a similar system of blood coagulation.

<span class="mw-page-title-main">Fibrin glue</span>

Fibrin glue is a surgical formulation used to create a fibrin clot for hemostasis, cartilage repair surgeries or wound healing. It contains separately packaged human fibrinogen and human thrombin.

A fibrin scaffold is a network of protein that holds together and supports a variety of living tissues. It is produced naturally by the body after injury, but also can be engineered as a tissue substitute to speed healing. The scaffold consists of naturally occurring biomaterials composed of a cross-linked fibrin network and has a broad use in biomedical applications.

Fibrin monomers are monomers of fibrin which are formed by the cleavage of fibrinogen by thrombin. Levels of fibrin monomers in can be measured using blood tests and can serve as a marker of in vivo fibrinogenesis and coagulation activation. They may be useful in the evaluation hypercoagulability.

References

  1. Marder VJ, Williams WJ, Beutler E, Erslev AJ, Lichtman MA, eds. (1990). "Consumptive thrombohemorrhagic disorders". Hematology.
  2. Potron G, Caen JP, Tobelem G, Soria C, eds. (1988). "Fisiopatologia delle iperfibrinolisi". Milano: Masson.