query: which protein is responsible for the breakdown of a fibrin clot

pos: Fibrinolysis side effects, especially on kidney. Fibrinolysis Fibrinolysis is a process that prevents blood clots from growing and becoming problematic. This process has two types: primary fibrinolysis and secondary fibrinolysis. The primary type is a normal body process, whereas secondary fibrinolysis is the breakdown of clots due to a medicine, a medical disorder, or some other cause. In fibrinolysis, a fibrin clot, the product of coagulation, is broken down. Its main enzyme plasmin cuts the fibrin mesh at various places, leading to the production of circulating fragments that are cleared by other proteases or by the kidney and liver. Plasmin is

pos: Disseminated intravascular coagulation thrombin that converts fibrinogen to fibrin; the stable fibrin clot being the final product of hemostasis. The fibrinolytic system then functions to break down fibrinogen and fibrin. Activation of the fibrinolytic system generates plasmin (in the presence of thrombin), which is responsible for the lysis of fibrin clots. The breakdown of fibrinogen and fibrin results in polypeptides called fibrin degradation products (FDPs) or fibrin split products (FSPs). In a state of homeostasis, the presence of plasmin is critical, as it is the central proteolytic enzyme of coagulation and is also necessary for the breakdown of clots, or fibrinolysis. In DIC,

pos: Fibrin degradation product Fibrin degradation product 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

pos: Fibrin degradation product liver, colon, rectal, ovarian, esophageal, cervical, trophoblastic, thyroid, malignant lymphoma, and pancreatic. Fibrin degradation product 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

pos: Tenecteplase that is derived from native t-PA by modifications at three sites of the protein structure. It binds to the fibrin component of the thrombus (blood clot) and selectively converts thrombus-bound plasminogen to plasmin, which degrades the fibrin matrix of the thrombus. Tenecteplase has a higher fibrin specificity and greater resistance to inactivation by its endogenous inhibitor (PAI-1) compared to native t-PA. The abbreviation TNK is common for referring to tenecteplase, but abbreviating drug names is not best practice in medicine, and in fact "TNK" is one of the examples given on the Institute for Safe Medication Practices (ISMP) do-not-use list.

pos: Tissue plasminogen activator encoded by the "PLAT" gene, which is located on chromosome 8. The primary transcript produced by this gene undergoes alternative splicing, producing three distinct messenger RNAs. Tissue plasminogen activator Tissue plasminogen activator (abbreviated tPA or PLAT) is a protein involved in the breakdown of blood clots. It is a serine protease () found on endothelial cells, the cells that line the blood vessels. As an enzyme, it catalyzes the conversion of plasminogen to plasmin, the major enzyme responsible for clot breakdown. Human tPA has a molecular weight of ~70 kDa in the single-chain form. tPA can be manufactured using recombinant

pos: Thrombus secreted by several streptococcal bacteria. This drug is administered intravenously and can be used to dissolve blood clots in coronary vessels. However, streptokinase is nonspecific and can digest almost any protein, which can lead to many secondary problems. Another clot-dissolving enzyme that works faster and is more specific is tissue plasminogen activator (tPA). This drug is made by transgenic bacteria and it converts plasminogen into the clot-dissolving enzyme, plasmin. There are also some anticoagulants that come from animals that work by dissolving fibrin. For example, "Haementeria ghilianii", an Amazon leech, produces an enzyme called hementin from its salivary glands. ,

pos: Fibrinolysis side effects, especially on kidney. Fibrinolysis Fibrinolysis is a process that prevents blood clots from growing and becoming problematic. This process has two types: primary fibrinolysis and secondary fibrinolysis. The primary type is a normal body process, whereas secondary fibrinolysis is the breakdown of clots due to a medicine, a medical disorder, or some other cause. In fibrinolysis, a fibrin clot, the product of coagulation, is broken down. Its main enzyme plasmin cuts the fibrin mesh at various places, leading to the production of circulating fragments that are cleared by other proteases or by the kidney and liver. Plasmin is

pos: Fibrinolysis Fibrinolysis Fibrinolysis is a process that prevents blood clots from growing and becoming problematic. This process has two types: primary fibrinolysis and secondary fibrinolysis. The primary type is a normal body process, whereas secondary fibrinolysis is the breakdown of clots due to a medicine, a medical disorder, or some other cause. In fibrinolysis, a fibrin clot, the product of coagulation, is broken down. Its main enzyme plasmin cuts the fibrin mesh at various places, leading to the production of circulating fragments that are cleared by other proteases or by the kidney and liver. Plasmin is produced in an inactive form,

pos: Tissue plasminogen activator Tissue plasminogen activator Tissue plasminogen activator (abbreviated tPA or PLAT) is a protein involved in the breakdown of blood clots. It is a serine protease () found on endothelial cells, the cells that line the blood vessels. As an enzyme, it catalyzes the conversion of plasminogen to plasmin, the major enzyme responsible for clot breakdown. Human tPA has a molecular weight of ~70 kDa in the single-chain form. tPA can be manufactured using recombinant biotechnology techniques; tPA produced by such means are referred to as recombinant tissue plasminogen activator (rtPA). Specific rtPAs include alteplase, reteplase, and tenecteplase. They are used

pos: Désiré Collen life saving biotech drug. Recombinant t-PA has been primarily used for dissolving blood clots causing acute myocardial infarction or acute ischemic stroke. T-PA is a protease that converts inactive plasminogen into active plasmin, which in turn cleaves fibrin, the main component of blood clots. Upon cleavage of the long fibrin strands by plasmin, the clot falls apart and dissolves. Between August 1977 and September 1978 Désiré Collen and Bjorn Wiman elucidated that the conversion of plasminogen to plasmin takes place when both proteins are bound to fibrin in the blood clot. This molecular model for the regulation and control of

pos: Hyperfibrinolysis in acute ischemic events or in patients with stroke. In patients with severe trauma, hyperfibrinolysis is associated with poor outcome. Moreover, hyperfibrinolysis may be associated with blood brain barrier impairment, a plasmin-dependent effect due to an increased generation of bradykinin. Bleeding is caused by the generation of fibrinogen degradation products which interfere with regular fibrin polymerization and inhibit platelet aggregation. Moreover, plasmin which is formed in excess in hyperfibrinolysis can proteolytically activate or inactivate many plasmatic or cellular proteins involved in hemostasis. Especially the degradation of fibrinogen, an essential protein for platelet aggregation and clot stability, may be a major

pos: Fibrinolysis plasminogen, in the liver. Although plasminogen cannot cleave fibrin, it still has an affinity for it, and is incorporated into the clot when it is formed. Tissue plasminogen activator (t-PA) and urokinase are the agents that convert plasminogen to the active plasmin, thus allowing fibrinolysis to occur. t-PA is released into the blood very slowly by the damaged endothelium of the blood vessels, such that, after several days (when the bleeding has stopped), the clot is broken down. This occurs because plasminogen became entrapped within the clot when it formed; as it is slowly activated, it breaks down the fibrin

pos: D-dimer proteofibrils. Another thrombin-generated enzyme, factor XIII, then crosslinks the fibrin proteofibrils at the D fragment site, leading to the formation of an insoluble gel which serves as a scaffold for blood clot formation. The circulating enzyme plasmin, the main enzyme of fibrinolysis, cleaves the fibrin gel in a number of places. The resultant fragments, "high molecular weight polymers", are digested several times more by plasmin to lead to intermediate and then to small polymers (fibrin degradation products or FDPs). The cross-link between two D fragments remains intact, however, and these are exposed on the surface when the fibrin fragments are

pos: Tissue plasminogen activator and cleared from the body through receptors present therein. One of the specific receptors responsible for this processes is a scavenger protein, specifically the LDL Receptor Related Protein (LRP1). tPA additionally can be bound by a plasminogen activator inhibitor (PAI), resulting in inactivation of its activity, and following clearing from the body by the liver. Lastly, tPA can bind plasminogen cleaving off the bound plasmin from it. Plasmin, another type of protease, can either be bound by a plasmin inhibitor, or work to degrade fibrin clots, which is the highest utilized and desired pathway. Tissue plasminogen activator is a protein

pos: Fibrinolysis mesh. t-PA and urokinase are themselves inhibited by plasminogen activator inhibitor-1 and plasminogen activator inhibitor-2 (PAI-1 and PAI-2). In contrast, plasmin further stimulates plasmin generation by producing more active forms of both tissue plasminogen activator (tPA) and urokinase. Alpha 2-antiplasmin and alpha 2-macroglobulin inactivate plasmin. Plasmin activity is also reduced by thrombin-activatable fibrinolysis inhibitor (TAFI), which modifies fibrin to make it more resistant to the tPA-mediated plasminogen. When plasmin breaks down fibrin, a number of soluble parts are produced. These are called fibrin degradation products (FDPs). FDPs compete with thrombin, and thus slow down clot formation by preventing the conversion

pos: Coagulation increase affinity to FXa, thrombin, or both). Quantitative or qualitative deficiency of antithrombin (inborn or acquired, e.g., in proteinuria) leads to thrombophilia. Tissue factor pathway inhibitor (TFPI) limits the action of tissue factor (TF). It also inhibits excessive TF-mediated activation of FVII and FX. Plasmin is generated by proteolytic cleavage of plasminogen, a plasma protein synthesized in the liver. This cleavage is catalyzed by tissue plasminogen activator (t-PA), which is synthesized and secreted by endothelium. Plasmin proteolytically cleaves fibrin into fibrin degradation products that inhibit excessive fibrin formation. Prostacyclin (PGI) is released by endothelium and activates platelet G protein-linked receptors.

pos: Staphylokinase Staphylokinase Staphylokinase (SAK) is an amino acid enzyme from "Staphylococcus aureus". It contains 136 amino acid residues and is a 15kDa protein. Growth of Staphylokinase is seen in late exponential phase. It is positively regulated by the "agr" gene regulator. It activates plasminogen to form plasmin, which digest fibrin clots. This disrupts the fibrin meshwork which can often form to keep an infection localized. Staphylokinase interacts with plasminogen to form a 1:1 complex that exposes the active site of the plasminogen molecule. The plasmin Sak complex is neutralized by α- antiplasmin in plasma in the absence of fibrin, resulting in

pos: Fibrinogen and activating, blood platelets through binding to their GpIIb/IIIa surface membrane fibrinogen receptor. Fibrin participates in limiting blood clot formation and lysing formed blood clots by at least two important mechanisms. First, it possesses three low affinity binding sites (two in fibrin's E domain; one in its D domain) for thrombin; this binding sequesters thrombin from attacking fibrinogen. Second, fibrin's Aα chain accelerates by at least 100-fold the mount of plasmin activated by tissue plasminogen activator; plasmin breaks-down blood clots. Plasmin's attack on fibrin releases D-dimers (also termed DD dimers). The detection of these dimers in blood is used as

pos: Plasminogen activator Plasminogen activator Plasminogen activators are serine proteases that catalyze the activation of plasmin via proteolytic cleavage of its zymogen form plasminogen. Plasmin is an important factor in fibrinolysis, the breakdown of fibrin polymers formed during blood clotting. There are two main plasminogen activators: urokinase (uPA) and tissue plasminogen activator (tPA). Tissue plasminogen activators are used to treat medical conditions related to blood clotting including embolic or thrombotic stroke, myocardial infarction, and pulmonary embolism. Plasminogen activators are inhibited by plasminogen activator inhibitor-1, plasminogen activator inhibitor-2, and protein C inhibitor. Produced mainly in the liver, plasminogen is the inactive zymogen form of

pos: Plasmin Plasmin Plasmin is an important enzyme () present in blood that degrades many blood plasma proteins, including fibrin clots. The degradation of fibrin is termed fibrinolysis. In humans, the plasmin protein is encoded by the "PLG" gene. Plasmin is a serine protease that acts to dissolve fibrin blood clots. Apart from fibrinolysis, plasmin proteolyses proteins in various other systems: It activates collagenases, some mediators of the complement system, and weakens the wall of the Graafian follicle, leading to ovulation. It cleaves fibrin, fibronectin, thrombospondin, laminin, and von Willebrand factor. Plasmin, like trypsin, belongs to the family of serine proteases. Plasmin

neg: Integrin an integrin on the surface of blood platelets (thrombocytes) responsible for attachment to fibrin within a developing blood clot. This molecule dramatically increases its binding affinity for fibrin/fibrinogen through association of platelets with exposed collagens in the wound site. Upon association of platelets with collagen, GPIIbIIIa changes shape, allowing it to bind to fibrin and other blood components to form the clot matrix and stop blood loss. Integrins couple the ECM outside a cell to the cytoskeleton (in particular, the microfilaments) inside the cell. Which ligand in the ECM the integrin can bind to is defined by which α and

neg: Fibrin Fibrin Fibrin (also called Factor Ia) is a fibrous, non-globular protein involved in the clotting of blood. It is formed by the action of the protease thrombin on fibrinogen which causes it to polymerize. The polymerized fibrin together with platelets forms a hemostatic plug or clot over a wound site. When the lining of a blood vessel is broken, platelets are attracted forming a platelet plug. These platelets have thrombin receptors on their surfaces that bind serum thrombin molecules which in turn convert soluble fibrinogen in the serum into fibrin at the wound site. Fibrin forms long strands of tough

neg: Coagulase is called "staphylothrombin", which enables the enzyme protease to convert fibrinogen, a plasma protein produced by the liver, to fibrin. This results in clotting of the blood. Coagulase is tightly bound to the surface of the bacterium "S. aureus" and can coat its surface with fibrin upon contact with blood. The fibrin clot may protect the bacterium from phagocytosis and isolate it from other defenses of the host. The fibrin coat can therefore make the bacteria more virulent. Bound coagulase is part of the larger family of MSCRAMM. The coagulase test has traditionally been used to differentiate "Staphylococcus aureus" from

neg: Thrombin glutamine residues in fibrin. The covalent bonds increase the stability of the fibrin clot. Thrombin interacts with thrombomodulin. As part of its activity in the coagulation cascade, thrombin also promotes platelet activation and aggregation via activation of protease-activated receptors on the cell membrane of the platelet. Thrombin bound to thrombomodulin activates protein C, an inhibitor of the coagulation cascade. The activation of protein C is greatly enhanced following the binding of thrombin to thrombomodulin, an integral membrane protein expressed by endothelial cells. Activated protein C inactivates factors Va and VIIIa. Binding of activated protein C to protein S leads to

neg: Fibrin insoluble protein that are bound to the platelets. Factor XIII completes the cross-linking of fibrin so that it hardens and contracts. The cross-linked fibrin forms a mesh atop the platelet plug that completes the clot. Excessive generation of fibrin due to activation of the coagulation cascade leads to thrombosis, the blockage of a vessel by an agglutination of red blood cells, platelets, polymerized fibrin and other components. Ineffective generation or premature lysis of fibrin increases the likelihood of a hemorrhage. Dysfunction or disease of the liver can lead to a decrease in the production of fibrin's inactive precursor, fibrinogen, or

neg: Batroxobin synthesis using "Pichia pastoris" seems promising for producing high quality recombinant batroxobin. As described earlier, batroxobin is an enzyme which has a serine protease activity on its substrate, fibrinogen. A serine protease cleaves a protein at the position of a serine, to degenerate a protein. Batroxobin is comparable to the enzyme thrombin, which is also a serine protease for fibrinogen. Fibrinogen is an important protein for hemostasis, because it plays a critical role in platelet aggregation and fibrin clot formation. Normally when one is wounded, thrombin cleaves the fibrinogen, which forms clots. As a result, the wound is ‘closed’ by

neg: FGL1 the other members of the fibrinogen family to aid in fibrin clot formation. FGL-1 may play a role in the development of hepatocellular carcinomas. FGL1 Fibrinogen-like protein 1 (FGL-1) is a protein that is structurally related to fibrinogen. In humans, FLG-1 is encoded by the "FGL1" gene. Four splice variants exist for this gene. Fibrinogen-like protein 1 is a member of the fibrinogen family of proteins, which also includes fibrinogen, fibrinogen-like protein 2, and clotting factors V, VIII, and XIII. FGL-1 is homologous to the carboxy terminus of the fibrinogen beta- and gamma- subunits which contains the four conserved cysteines

neg: Hirudin a helical loop that forms many hydrophobic contacts. Natural rudin contains a mixture of various isoforms of the protein. However, recombinant techniques can be used to produce homogeneous preparations of hirudin. A key event in the final stages of blood coagulation is the conversion of fibrinogen into fibrin by the serine protease enzyme thrombin. Thrombin is produced from prothrombin, by the action of an enzyme, prothrombinase (Factor Xa along with Factor Va as a cofactor), in the final states of coagulation. Fibrin is then cross linked by factor XIII (Fibrin Stabilizing Factor) to form a blood clot. The principal inhibitor

neg: D-dimer D-dimer D-dimer (or D dimer) is a fibrin degradation product (or FDP), 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. D-dimer concentration may be determined by a blood test to help diagnose thrombosis. Since its introduction in the 1990s, it has become an important test performed in patients with suspected thrombotic disorders. While a negative result practically rules out thrombosis, a positive result can indicate thrombosis but does not rule out other potential causes.

neg: D-dimer D-dimer D-dimer (or D dimer) is a fibrin degradation product (or FDP), 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. D-dimer concentration may be determined by a blood test to help diagnose thrombosis. Since its introduction in the 1990s, it has become an important test performed in patients with suspected thrombotic disorders. While a negative result practically rules out thrombosis, a positive result can indicate thrombosis but does not rule out other potential causes.

neg: Thrombophilia fibrinogen, and activates a number of other enzymes and cofactors (factor XIII, factor XI, factor V and factor VIII, TAFI) that enhance the fibrin clot. The process is inhibited by TFPI (which inactivates the first step catalyzed by factor VIIa/tissue factor), antithrombin (which inactivates thrombin, factor IXa, Xa and XIa), protein C (which inhibits factors Va and VIIIa in the presence of protein S), and protein Z (which inhibits factor Xa). In thrombophilia, the balance between "procoagulant" and "anticoagulant" activity is disturbed. The severity of the imbalance determines the likelihood that someone develops thrombosis. Even small perturbances of proteins, such

neg: Congenital afibrinogenemia formation of the protein. In normal conditions, fibrinogen is converted to fibrin when it is cleaved by the enzyme thrombin in the blood. The newly formed fibrin forms a fiber-rich network that helps trap red blood cells to start the coagulation process and form a clot. Since there is no fibrinogen present during afibrinogenemia, fibrin can not be formed to aid in this process. When a problem of fibrinogen is suspected, the following tests can be ordered: Blood fibrinogen levels of less than 0.1 g/L and prolonged bleeding test times are indicators of an individual having afibrinogenemia. The most common

neg: Low molecular weight heparin a protease cleaves and subsequently activates the next protease in the sequence. Since each protease can activate several molecules of the next protease in the series, this biological cascade is amplified. The final result of these reactions is to convert fibrinogen, a soluble protein, to insoluble threads of fibrin. Together with platelets, the fibrin threads form a stable blood clot. Antithrombin (AT), a serine protease inhibitor, is the major plasma inhibitor of coagulation proteases. LMWHs inhibit the coagulation process through binding to AT via a pentasaccharide sequence. This binding leads to a conformational change of AT which accelerates its inhibition

neg: Edoxaban inhibits thrombin-induced platelet aggregation. Inhibition of factor Xa in the coagulation cascade reduces thrombin generation and thrombus formation. Factor Xa (FXa) is an essential blood coagulation factor that is responsible for the initiation of the coagulation cascade. FXa cleaves prothrombin to its active form thrombin, which then acts to convert soluble fibrinogen to insoluble fibrin and to activate platelets. Stabilization of the platelet aggregation by fibrin mesh ultimately leads to clot formation. A number of anticoagulants inhibit the activity of Factor Xa. Unfractionated heparin (UFH), low molecular weight heparin (LMWH), and fondaparinux inhibit the activity of factor Xa indirectly by

neg: Platelet-poor plasma find use in tissue engineering applications as an autologous degradable scaffold. This plasma portion is frequently discarded when used with PRP treatments. Platelet-poor plasma Platelet-Poor Plasma (PPP) is blood plasma with very low number of platelets (< 10 X 10/μL). Traditionally, PPP was recommended for use in platelet aggregation studies to both adjust the Platelet-rich plasma concentration, and to serve as a control. PPP may have elevated levels of fibrinogen, which has the ability to form a fibrin-rich clot once activated. Wound healing requires cell migration and attachment, which is facilitated by this fibrin clot. Fibrin sealants have found use

neg: Platelet-poor plasma Platelet-poor plasma Platelet-Poor Plasma (PPP) is blood plasma with very low number of platelets (< 10 X 10/μL). Traditionally, PPP was recommended for use in platelet aggregation studies to both adjust the Platelet-rich plasma concentration, and to serve as a control. PPP may have elevated levels of fibrinogen, which has the ability to form a fibrin-rich clot once activated. Wound healing requires cell migration and attachment, which is facilitated by this fibrin clot. Fibrin sealants have found use in many clinical situations such as blood management, orthopaedic surgery, and cosmetic surgery. As a byproduct of PRP preparation, PPP may also

neg: Intravascular immunity blood vessel which seal leaky vessels and are important in blood coagulation. Fibrin provides a matrix to trap pathogens and recruit immune cells. Characteristics such as elongation and thickness of fibrin and protofibril, the precursor of fibrin, are determined by many factors including environmental conditions, physiological conditions, and branching of the fibrin fibers. This in turn influences the clot structure such as permeability, stiffness, and how easily the clot can be retracted. The shift from immunothrombosis to a more pathogenic thrombosis is due to dysregulated immunothrombosis. Intravascular immunity Intravascular immunity describes the immune response in the bloodstream, and its role

neg: Fibrin glue Fibrin glue Fibrin glue (also called fibrin sealant) is a surgical formulation used to create a fibrin clot for hemostasis or wound healing. It is made up of fibrinogen (lyophilised pooled human concentrate) and thrombin (bovine, which is reconstituted with calcium chloride) that are applied to a site of tissue damage to glue them together. Thrombin is an enzyme and converts fibrinogen into fibrin monomers between 10 and 60 seconds giving rise to a three-dimensional gel. Factors that influence dimensional structure of fibrin gel giving rise to fine or coarse gel: Formulations from different manufacturers may also contain aprotinin, fibronectin

neg: Cerebral venous sinus thrombosis condition does not lead to hydrocephalus, however, because there is no difference in pressure between various parts of the brain. Any blood clot forms due to an imbalance between coagulation (the formation of the insoluble blood protein fibrin) and fibrinolysis. The three major mechanisms for such an imbalance are enumerated in Virchow's triad: alterations in normal blood flow, injury to the blood vessel wall, and alterations in the constitution of blood (hypercoagulability). Most cases of cerebral venous sinus thrombosis are due to hypercoagulability. It is possible for the clot to break off and migrate (embolise) to the lungs, causing a

neg: Fibrin glue and plasminogen. This glue can be used for repairing dura tears, bronchial fistulas and for achieving hemostasis after spleen and liver trauma. It is also employed in "no sutures" corneal transplantation, pterygium excision with amniotic membrane or conjunctival autograft, and in ocular trauma for corneal or conjunctival defects. It can also be used for skin graft donor site wounds to reduce postoperative pain. Fibrin glue Fibrin glue (also called fibrin sealant) is a surgical formulation used to create a fibrin clot for hemostasis or wound healing. It is made up of fibrinogen (lyophilised pooled human concentrate) and thrombin (bovine, which

neg: Thrombin time Thrombin time The thrombin time (TT), also known as the thrombin clotting time (TCT) is a blood test that measures the time it takes for a clot to form in the plasma of a blood sample containing anticoagulant, after an excess of thrombin has been added. It is used to diagnose blood coagulation disorders and to assess the effectiveness of fibrinolytic therapy. This test is repeated with pooled plasma from normal patients. The difference in time between the test and the 'normal' indicates an abnormality in the conversion of fibrinogen (a soluble protein) to fibrin, an insoluble protein. The thrombin

neg: Apixaban prothrombin to thrombin, the final enzyme in the coagulation cascade that is responsible for fibrin clot formation. Apixaban has no direct effect on platelet aggregation, but by inhibiting factor Xa, it indirectly decreases clot formation induced by thrombin. A new drug application (NDA) for the approval of apixaban was submitted to the FDA by Bristol-Myers Squibb and Pfizer jointly after conclusion of the ARISTOTLE clinical trial in 2011. Apixaban was approved for the prevention of stroke in people with atrial fibrillation on December 28, 2012. On March 14, 2014, it was approved for the additional use of preventing deep vein

neg: Factor VIII a stable noncovalent complex with von Willebrand factor. Upon activation by thrombin (factor IIa), it dissociates from the complex to interact with factor IXa in the coagulation cascade. It is a cofactor to factor IXa in the activation of factor X, which, in turn, with its cofactor factor Va, activates more thrombin. Thrombin cleaves fibrinogen into fibrin which polymerizes and crosslinks (using factor XIII) into a blood clot. No longer protected by vWF, activated FVIII is proteolytically inactivated in the process (most prominently by activated protein C and factor IXa) and quickly cleared from the blood stream. Factor VIII is

neg: Discovery and development of direct Xa inhibitors converts fibrinogen to fibrin which leads to clot formation. Factor Xa is an activated serine protease that occupies a key role in the blood coagulation pathway by converting prothrombin to thrombin. Inhibition of factor Xa leads to antithrombotic effects by decreasing the amount of thrombin. Directly targeting factor Xa is suggested to be an effective approach to anticoagulation. In 1987 antistasin was tested as the first direct Xa inhibitor. Antistasin is a protein made up of 119 amino acid residues, of which 20 are cysteines involved in 10 disulfide bonds. It acts as a slow, tight-binding inhibitor of factor Xa

neg: D-dimer Its main use, therefore, is to exclude thromboembolic disease where the probability is low. In addition, it is used in the diagnosis of the blood disorder disseminated intravascular coagulation. Coagulation, the formation of a blood clot or thrombus, occurs when the proteins of the coagulation cascade are activated, either by contact with damaged blood vessel wall and exposure to collagen in the tissue space (intrinsic pathway) or by activation of factor VII by tissue activating factors (extrinsic pathway). Both pathways lead to the generation of thrombin, an enzyme that turns the soluble blood protein fibrinogen into fibrin, which aggregates into

neg: Factor V Leiden city Leiden, where it was first identified in 1994 by Prof R. Bertina under the direction of (and in the laboratory of) Prof P. Reitsma. Abnormal, recurrent venous thromboses. In the normal person, factor V functions as a cofactor to allow factor Xa to activate prothrombin, resulting in the enzyme thrombin. Thrombin in turn cleaves fibrinogen to form fibrin, which polymerizes to form the dense meshwork that makes up the majority of a clot. Activated protein C (aPC) is a natural anticoagulant that acts to limit the extent of clotting by cleaving and degrading factor V. Factor V Leiden is

neg: Platelet-rich fibrin Platelet-rich fibrin Platelet-rich fibrin (PRF) or leucocyte- and platelet-rich fibrin (L-PRF) is a second-generation PRP where autologous platelets and leucocytes are present in a complex fibrin matrix to accelerate the healing of soft and hard tissue and is used as a tissue-engineering scaffold for endodontics. To obtain PRF, required quantity of blood is drawn quickly into test tubes without an anticoagulant and centrifuged immediately. Blood can be centrifuged using a tabletop centrifuge for at least 10 min at 3000 revolution per minute. The resultant product consists of the following three layers; topmost layer consisting of platelet poor plasma, PRF clot

neg: Platelet-rich fibrin in the middle, and red blood cells at the bottom. PRF is available as a fibrin clot. PRF clot can be removed from the test tube using a sterile tweezer-like instrument. After lifting, the RBC layer attached to the PRF clot can be carefully removed using a sterilized scissor. Platelet activation in response to tissue damage occurs during the process of making PRF release several biologically active proteins including; platelet alpha granules, platelet‑derived growth factor (PGDF), transforming growth factors‑β (TGF‑β), vascular endothelial growth factor (VEGF), and epidermal growth factor. Actually the platelets and leukocyte cytokines are important part in role

neg: Fibrinogen above this range associated with pathological bleeding and/or thrombosis. Fibrinogen has a circulating half-life of ~4 days. During blood clotting, thrombin attacks the N-terminus of the Aα and Bβ chains in fibrinogen to form individual fibrin strands plus two small polypeptides, fibrinopeptides a and b derived from these respective chains. The individual fibrin strands then polymerize and are cross-linked with other fibrin stands by blood factor XIIIa to form an extensive interconnected fibrin network that is the basis for the formation of a mature fibrin clot. In addition to forming fibrin, fibrinogen also promotes blood clotting by forming bridges between,

neg: Schistocyte a result of mechanical destruction (fragmentation hemolysis) of a normal red blood cell. This occurs when there is damage to the blood vessel and a clot begins to form. The formation of the fibrin strands in the vessels occurs as part of the clot formation process. The red blood cells get trapped in the fibrin strands and the sheer force of the blood flow causes the red blood cell to break. The resulting fragmented cell is called the schistocyte. A normal schistocyte count for a healthy individual is <0.5% although usual values are found to be <0.2%. A schistocyte count

neg: Fibrin scaffold Matrigel, salmon fibrin promotes the neurite growth best and it is more proteolysis resistant than mammalian fibrins. Because down to 0 °C, salmon fibrinogen can clot whereas polymerization of human fibrinogen occurs slowly below 37 °C, this can be taken as an advantage in surgical settings that are cooler. Therefore, for treatment of central nervous system damages, salmon fibrin can be a useful biomaterial. For sciatic nerve regeneration, fibrin scaffold is used with glial derived neurotrophic factor (GDNF) in a recent study. Survival of both sensory and motor neurons is promoted by glial-derived neurotrophic factor and its delivery to peripheral

neg: Thromboelastometry (or a lower alpha-angle) is usually caused by poor platelet function, low platelet count, fibrin polymerization disorders or fibrinogen deficiency. Apparently also FXIII seems to be involved already in this phase. Higher concentrations of heparin can also prolong CFT in the INTEM assay, but not in HEPTEM, EXTEM, FIBTEM or APTEM (see under “reagents”). A shortening of CFT (or a high alpha-angle) indicate hypercoagulability. MCF (Maximum clot firmness): MCF is the greatest vertical amplitude of the trace. It reflects the absolute strength of the fibrin and platelet clot. A low MCF is indicative of decreased platelet number or function, decreased

neg: Platelet on receptors and secrete chemical messengers: "activation". Third, they connect to each other through receptor bridges: "aggregation". Formation of this platelet plug (primary hemostasis) is associated with activation of the coagulation cascade with resultant fibrin deposition and linking (secondary hemostasis). These processes may overlap: the spectrum is from a predominantly platelet plug, or "white clot" to a predominantly fibrin, or "red clot" or the more typical mixture. Some would add the subsequent "retraction" and "platelet inhibition" as fourth and fifth steps to the completion of the process and still others a sixth step "wound repair". Platelets also participate in both

neg: Dysfibrinogenemia to form mature gel-like fibrin clots. Subsequent fibrinolysis pathways act to limit clot formation and dissolve clots no longer needed. Fibrinogen and its Aα fibrin chain have several functions in this process: Based on these fibrinogen functions, a fibrinogen mutation may act either to inhibit or promote blood clot formation and/or lysis to thereby produce in individuals a diathesis to develop pathological bleeding, thrombosis, or both conditions. Congenital dysfibrinogenemia is most often caused by a single autosomal dominant missense mutation in the "Aα", "Bβ", or "γ" gene; rarely, it is caused by a homozygous or compound heterozygous missense mutation, a

neg: Thrombus Thrombus A thrombus, colloquially called a blood clot, is the final product of the blood coagulation step in hemostasis. There are two components to a thrombus: aggregated platelets and red blood cells that form a plug, and a mesh of cross-linked fibrin protein. The substance making up a thrombus is sometimes called cruor. A thrombus is a healthy response to injury intended to prevent bleeding, but can be harmful in thrombosis, when clots obstruct blood flow through healthy blood vessels. Mural thrombi are thrombi that adhere to the wall of a blood vessel. They occur in large vessels such as

neg: Fibrinolysis refers to the dissolution of the thrombus due to various agents while fibrinolysis refers specifically to the agents causing fibrin breakdown in the clot. Antifibrinolytics, such as aminocaproic acid (ε-aminocaproic acid) and tranexamic acid are used as inhibitors of fibrinolysis. Their application may be beneficial in patients with hyperfibrinolysis because they arrest bleeding rapidly if the other components of the haemostatic system are not severely affected. This may help to avoid the use of blood products such as fresh frozen plasma with its associated risks of infections or anaphylactic reactions. The antifibrinolytic drug aprotinin was abandoned after identification of major

neg: Fibrinogen Fibrinogen Fibrinogen (factor I) is a glycoprotein that circulates in the blood of vertebrates. During tissue and vascular injury it is converted enzymatically by thrombin to fibrin and subsequently to a fibrin-based blood clot. Fibrinogen functions primarily to occlude blood vessels and thereby stop excessive bleeding. However, fibrinogen's product, fibrin, binds and reduces the activity of thrombin. This activity, sometimes referred to as antithrombin I, serves to limit blood clotting. Loss or reduction in this antithrombin 1 activity due to mutations in fibrinogen genes or hypo-fibrinogen conditions can lead to excessive blood clotting and thrombosis. Fibrin also mediates blood platelet

neg: Thromboelastometry is used for therapeutic decisions regarding the administration of fresh frozen plasma, coagulation factors, fibrinogen or platelets. EXTEM is also the base activator for FIBTEM and APTEM. FIBTEM test is an EXTEM based assay for the fibrin part of the clot. FIBTEM eliminates the platelet contribution of clot formation by inhibiting the platelets irreversibly with cytochalasin D, a potent inhibitor of actin polymerization which disrupts actin microfilaments, an essential part of a cytoskeleton-mediated contractibility apparatus of the platelet. The use of cytochalasin is more favorable than using glycoprotein IIb/ IIIa inhibitors which block platelet incompletely, especially at higher platelet counts.

neg: Thromboelastometry FIBTEM allows for the detection of fibrinogen deficiency or fibrin polymerization disorders, e.g. induced by certain plasma expanders, and may identify rapidly the need to substitute fibrinogen. FIBTEM results correlate well in many cases with the Clauss fibrinogen assay, but is additionally influenced by fibrin polymerization disorders which cannot reliably be detected with clotting tests. APTEM test is an EXTEM based assay in which fibrinolysis is inhibited by aprotinin in the reagent. A significant improvement of the clot in APTEM compared to EXTEM allows to detect fulminant hyperfibrinolysis. Therefore, the test helps in identifying the necessity of administrating antifibrinolytic drugs.

neg: Fibronectin fibronectin remains associated with the clot, covalently cross-linked to fibrin with the help of Factor XIII (fibrin-stabilizing factor). Fibroblasts play a major role in wound healing by adhering to fibrin. Fibroblast adhesion to fibrin requires fibronectin, and was strongest when the fibronectin was cross-linked to the fibrin. Patients with Factor XIII deficiencies display impairment in wound healing as fibroblasts don't grow well in fibrin lacking Factor XIII. Fibronectin promotes particle phagocytosis by both macrophages and fibroblasts. Collagen deposition at the wound site by fibroblasts takes place with the help of fibronectin. Fibronectin was also observed to be closely associated with

neg: Fibrin scaffold Fibrin scaffold 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 consists of the blood proteins fibrinogen and thrombin which participate in blood clotting. Fibrin glue or fibrin sealant is also referred to as a fibrin based scaffold and used to control surgical bleeding, speed wound healing, seal

neg: Thrombosis the risk of recurrence or progression. Thrombosis Thrombosis (from Ancient Greek θρόμβωσις "thrómbōsis" "clotting”) is the formation of a blood clot inside a blood vessel, obstructing the flow of blood through the circulatory system. When a blood vessel (a vein or an artery) is injured, the body uses platelets (thrombocytes) and fibrin to form a blood clot to prevent blood loss. Even when a blood vessel is not injured, blood clots may form in the body under certain conditions. A clot, or a piece of the clot, that breaks free and begins to travel around the body is known as

neg: Thrombosis Thrombosis Thrombosis (from Ancient Greek θρόμβωσις "thrómbōsis" "clotting”) is the formation of a blood clot inside a blood vessel, obstructing the flow of blood through the circulatory system. When a blood vessel (a vein or an artery) is injured, the body uses platelets (thrombocytes) and fibrin to form a blood clot to prevent blood loss. Even when a blood vessel is not injured, blood clots may form in the body under certain conditions. A clot, or a piece of the clot, that breaks free and begins to travel around the body is known as an embolus. Thrombosis may occur in

neg: Factor XIII on fibrin to form γ-glutamyl-Є-lysyl amide cross links between fibrin molecules to form an insoluble clot. FXIII is also known as Laki–Lorand factor, after Kalman Laki and Laszlo Lorand, the scientists who first proposed its existence in 1948. A 2005 conference recommended standardization of nomenclature. Zymogen factor XIII is a 320kDa glycoprotein tetramer consisting of twice two subunits (2 A and 2 B), the genes for which are on different chromosomes: Factor XIII has two forms: a plasmatic form that flows freely in the blood plasma, and a cellular form carried inside platelet alpha-granules. The cellular form is a dimer

neg: Diagnostic microbiology positive test while nothing happening is a negative result. Cetrimide agar slants is a selective agar used to isolate "Pseudomonas aeruginosa""." The CLO test is used to diagnose "H. Pylori" in patient biopsies. A sample of the biopsy is places in a medium containing urea, which "H. Pylori" can use in some of its biochemical pathways. Consumption of urea indicates a positive test result. The coagulase test determines whether an organism can produce the enzyme coagulase, which causes the fibrin to clot. Inoculating a plasma test tube with the microbe indicates whether coagulase is produced. A clot indicates the presence

neg: Factor XIII Factor XIII Factor XIII or fibrin stabilizing factor is an enzyme () of the blood coagulation system that crosslinks fibrin. Deficiency of this factor (FXIIID) affects clot stability. FXIIID, while generally rare, does occur, with Iran having the highest global incidence of the disorder with 473 cases. The city of Khash, located in Sistan and Balochistan provinces, has the highest incidence in Iran, with a high rate of consanguineous marriage. Factor XIII is a transglutaminase that circulates in the plasma as a heterotetramer of two catalytic A subunits and two carrier B subunits. When thrombin has converted fibrinogen to fibrin,

neg: Discovery and development of direct thrombin inhibitors it converts soluble fibrinogen to an insoluble fibrin complex. Furthermore, it activates factors V, VIII and XI, all by cleaving the sequences GlyGlyGlyValArg-GlyPro and PhePheSerAlaArg-GlyHis, selectively between Arginine (Arg) and Glycine (Gly). These factors generate more thrombin. Thrombin also activates factor XIII that stabilizes the fibrin complex and therefore the clot and it stimulates platelets, which help with the coagulation. Given this broad action of thrombin it stands as a good drug target for anticoagulant drugs such as heparin, warfarin and DTIs and antiplatelet drugs like aspirin. Thrombin is in the serine protease family. It has 3 binding domains in

neg: Pseudoaneurysm into fibrin, which then polymerizes to form a blood clot. Under ultrasound guidance, thrombin can be injected directly into a pseudoaneurysm, causing it to clot. Advantages are that the technique is relatively easy to perform, is successful, and is minimally invasive. One contraindication to this procedure is if there is an arteriovenous fistula (communication between an artery and vein), in addition to the pseudoaneurysm. This occurs with about 10% of pseudoaneurysms. If this is present, thrombin injected into the pseudoaneurysm could then enter the venous circulation and possibly lead to distant thrombosis. Open surgery may also be performed to remove

neg: Coagulation factor XIII, A1 polypeptide origin. Upon cleavage of the activation peptide by thrombin and in the presence of calcium ion, the plasma factor XIII dissociates its B subunits and yields the same active enzyme, factor XIIIa, as platelet factor XIII. This enzyme acts as a transglutaminase to catalyze the formation of gamma-glutamyl-epsilon-lysine crosslinking between fibrin molecules, thus stabilizing the fibrin clot. It also crosslinks alpha-2-plasmin inhibitor, or fibronectin, to the alpha chains of fibrin. Factor XIII deficiency is classified into two categories: type I deficiency, characterized by the lack of both the A and B subunits; and type II deficiency, characterized by the lack

neg: Fibrinogen been proposed as a predictor of hemorrhagic complications during catheter-directed trombolysis for acute or subacute peripheral native artery and arterial bypass occlusions. However, a systematic review of the available literature until January 2016 found that the predictive value of plasma fibrinogen level for predicting hemorrhagic complications after catheter-directed thrombolysis is unproven. Fibrinogen Fibrinogen (factor I) is a glycoprotein that circulates in the blood of vertebrates. During tissue and vascular injury it is converted enzymatically by thrombin to fibrin and subsequently to a fibrin-based blood clot. Fibrinogen functions primarily to occlude blood vessels and thereby stop excessive bleeding. However, fibrinogen's product,

neg: Protein metabolism follows a bimolecular ping pong mechanism. Protein biosynthesis relies on four processes: Protein anabolism is the process by which protein are formed from amino acids (anabolic amino acid synthesis). Protein catabolism is the process by which proteins are broken down to their amino acids. This is also called proteolysis. This can be followed by further amino acid degradation. The following list contains links to information about the metabolism of individual amino acids. Protein metabolism Protein metabolism denotes the various biochemical processes responsible for the synthesis of proteins and amino acids, and the breakdown of proteins (and other large molecules) by

neg: Gingival graft and hematopoietic stem cells). A small amount of blood ( per tube) is harvested and spun in a centrifuge for eight minutes at 1300 rpm. A fibrin clot packed with blood-derived growth factors, extra cellular matrix and hematopoietic stem cells is fabricated and implanted into the gums above the area of gum recession. Advanced platelet-rich fibrin will promote the patient's own gums to fabricate more gum thus eliminating the need to harvest gums from the roof of the mouth or the use of allografting tissue. Following this procedure, patients require less recovery time due to enhanced healing factors. And improve

neg: Liver synthesis of glucose from certain amino acids, lactate, or glycerol. Adipose and liver cells produce glycerol by breakdown of fat, which the liver uses for gluconeogenesis. The liver is responsible for the mainstay of protein metabolism, synthesis as well as degradation. It is also responsible for a large part of amino acid synthesis. The liver plays a role in the production of clotting factors, as well as red blood cell production. Some of the proteins synthesized by the liver include coagulation factors I (fibrinogen), II (prothrombin), V, VII, VIII, IX, X, XI, XIII, as well as protein C, protein S

neg: Hementerin (FGB) chains, by degrading cross-linked fibrin. It has no degrading action on amide, plasminogen and casein. In addition, hementerin inhibits platelet aggregation induced by collagen via the activation of a nitridergic pathway. Inhibition is probably achieved by enhanced nitric oxide synthase activity. Calcium is a cofactor (ligand) in this activity. The fibrinolytic activity is inhibited by EDTA, a metal chelator agent, which removes zinc from the molecule. Hementerin is a protein with 30 aminoacids, in the following sequence: XTLSEPEPTC SIEYFRYQAI EDCEYSISVK. Hementerin Hementerin is a metalloprotease found in the saliva of a hematophagous leech, "Haementeria depressa", which is responsible for

neg: Aureolysin coagulation as well as the activation of urokinase. However, it also mediates "S. aureus" cell wall and secreted proteins to promote this change. For example, clumping factor B is a surface protein that is responsible for the binding of fibrinogen around the bacterium to hide it within a clot. Aureolysin is responsible for the cleavage of clumping factor B, which causes the loss of "S. aureus" binding to fibrinogen. By this mechanism, it may act as a self-regulatory mechanism for dissemination and spreading in combination with activation of fibrinolysis, while the protease simultaneously provides protection against complement activation. It has

neg: Glycoprotein IIb/IIIa to the same strands of fibrinogen, resulting in a clot. The coagulation cascade then follows to stabilize the clot, as thrombin (factor IIa) converts the soluble fibrinogen into insoluble fibrin strands. These strands are then cross-linked by factor XIII to form a stabilized blood clot. Defects in glycoprotein IIb/IIIa cause Glanzmann's thrombasthenia. Autoantibodies against IIb/IIIa can be produced in immune thrombocytopenic purpura. Glycoprotein IIb/IIIa inhibitors can be used to prevent blood clots in an effort to decrease the risk of heart attack or stroke. Glycoprotein IIb/IIIa In medicine, glycoprotein IIb/IIIa (GPIIb/IIIa, also known as integrin αβ) is an integrin complex

neg: Exoenzyme and released out of the cell. In humans, a majority of such exoenzymes can be found in the digestive system and are used for metabolic breakdown of macronutrients via hydrolysis. Breakdown of these nutrients allows for their incorporation into other metabolic pathways. Necrotizing enzymes destroy cells and tissue. One of the best known examples is an exoenzyme produced by Streptococcus pyogenes that causes necrotizing fasciitis in humans. By binding to prothrombin, coagulase facilitates clotting in a cell by ultimately converting fibrinogen to fibrin. Bacteria such as Staphylococcus aureus use the enzyme to form a layer of fibrin around their cell

neg: Eosinophil High concentrations of these DNA traps are known to cause cellular damage, as the granules they contain are responsible for the ligand-induced secretion of eosinophilic toxins which cause structural damage. There is evidence to suggest that eosinophil granule protein expression is regulated by the non-coding RNA EGOT. Following activation, eosinophils effector functions include production of the following: There are also eosinophils that play a role in fighting viral infections, which is evident from the abundance of RNases they contain within their granules, and in fibrin removal during inflammation. Eosinophils, along with basophils and mast cells, are important mediators of allergic

neg: C7orf25 main transcription factors that bind to the promoter are listed below. C7orf25 protein UPF0415 is believed to be active in ATP dependent protein breakdown in the proteosome pathway. It is expressed ubiquitously in humans. UPF0415 protein C7orf25 has one paralog which is FLJ18411. UPF0415 is also highly conserved in vertebrates. The following table shows a small selection of orthologs found using BLAST and BLAT and their identity to C7orf25 protein UPF0415. UPF0415 protein C7orf25 is not a transmembrane protein as it has no transmembrane domains. C7orf25 protein UPF0415 has multiple phosphorylation which are believed to be responsible in protein activation.

neg: Fibrin bound ligands. The experimental method used to obtain the image was X-ray diffraction, and it has a resolution of 2.30 Å. The structure is mainly made up of single alpha helices shown in red and beta sheets shown in yellow. The two blue structures are the bound ligands. The chemical structures of the ligands are Ca ion, alpha-D-mannose (CHO), and D-glucosamine (CHNO). Fibrin Fibrin (also called Factor Ia) is a fibrous, non-globular protein involved in the clotting of blood. It is formed by the action of the protease thrombin on fibrinogen which causes it to polymerize. The polymerized fibrin together

neg: Fibrinogen alpha chain Fibrinogen alpha chain Fibrinogen alpha chain is a protein that in humans is encoded by the "FGA" gene. The protein encoded by this gene is the alpha component of fibrinogen, a blood-borne glycoprotein composed of three pairs of nonidentical polypeptide chains. Following vascular injury, fibrinogen is cleaved by thrombin to form fibrin, which is the most abundant component of blood clots. In addition, various cleavage products of fibrinogen and fibrin regulate cell adhesion and spreading, display vasoconstrictor and chemotactic activities, and are mitogens for several cell types. Mutations in this gene lead to several disorders, including dysfibrinogenemia, hypofibrinogenemia, afibrinogenemia, and

neg: Fibrin scaffold Less cytotoxicity is observed due to less use of transfection agents like lipofectamine and steady degradation of fibrin. Consequently, each cell type requires optimization of fibrinogen and pDNA concentrations for higher transfection yields and studies towards high-throughput transfection microarray experiments are promising. Fibrin scaffold 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

neg: Fibrinolysis syndrome levels of fibrin, or therefore non-existent fibrin. Fibrinolysis syndrome Fibrinolysis syndrome (also known as "Defibrinating syndrome") is characterized by an acute hemorrhagic state brought about by inability of the blood to clot, with massive hemorrhages into the skin producing blackish, purplish swellings and sloughing. Hemorrhages (this includes severe bleeding of any particular area. Be it: nasal, rectal, oral, it also includes bleeding from scrapes, cuts, bruises (big bruises that do not disappear in the first two to three days). The cause for Fibrinolysis syndrome, is the inability of the body to produce blood-coagulates to stop bleeding. What causes the body

neg: Thromboelastography MA (AA) and MA (ADP), respectively. The difference between the patient’s whole blood result and AA/ADP added results are used to calculate the percent inhibition. Because the R value on the TEG represents the time it takes for clot formation to start, it is a reflection of coagulation factor activity. Coagulation factors are essentially enzymes that drive clot formation. Thus, a prolonged R time should be treated with plasma. The alpha angle represents the thrombin burst and conversion of fibrinogen to fibrin. Thus, a depressed alpha angle should be treated with either cryoprecipitate or large volumes of plasma. 80% of

neg: Factor XIII these cells. Factor XIII Factor XIII or fibrin stabilizing factor is an enzyme () of the blood coagulation system that crosslinks fibrin. Deficiency of this factor (FXIIID) affects clot stability. FXIIID, while generally rare, does occur, with Iran having the highest global incidence of the disorder with 473 cases. The city of Khash, located in Sistan and Balochistan provinces, has the highest incidence in Iran, with a high rate of consanguineous marriage. Factor XIII is a transglutaminase that circulates in the plasma as a heterotetramer of two catalytic A subunits and two carrier B subunits. When thrombin has converted fibrinogen

neg: Congenital hypofibrinogenemia propensity to develop thrombosis in a disorder causing a decrease in a critical protein for blood clotting may be due to the function of fibrin (the split product of fibrinogen that is the basis for forming blood clots) to promote the lysis or desolution of blood clots. Lower levels of fibrin may reduce the lysis of early fibrin strand depositions and thereby allow these depositions to develop into clots. Congenital hypofibrinogenemia must be distinguished from: a) congenital afibrinogenemia, a rare disorder in which blood fibrinogen levels are either exceedingly low or undetectable due to mutations in both fibrinogen genes; b)

neg: Thrombin time be between 15 and 20 seconds. Thrombin time can be prolonged by heparin, fibrin degradation products, and fibrinogen deficiency or abnormality. After separating the plasma from the whole blood by centrifugation, bovine thrombin is added to the sample of plasma. Clot formation is detected optically or mechanically by a coagulation instrument. The time between the addition of the thrombin and the clot formation is recorded as the thrombin clotting time. Whole blood is taken with either citrate or oxalate additive (if using the vacutainer system, this is a light blue top tube). As with other coagulation assays, the tube must

neg: Dysfibrinogenemia both ends termed D domains and central nodule termed the E domain. The normal process of blood clot formation involves the coordinated operation of two separate pathways that feed into a final common pathway: 1) primary hemostasis, i.e. the adhesion, activation, and aggregation of circulating blood platelets at sites of vascular injury and 2) secondary hemostasis, i.e. cleavage of the Aα and Bβ chains of fibrinogen by thrombin to form individual fibrin strands plus the respective fibrinopeptides A and B formed from this cleavage. In the final common pathway fibrin is cross-linked by activated clotting factor XIII (termed factor XIIIa)

neg: Wound healing order to achieve hemostasis, or stop blood loss by way of a fibrin clot. Thereafter, various soluble factors (including chemokines and cytokines) are released to attract cells that phagocytise debris, bacteria, and damaged tissue, in addition to releasing signaling molecules that initiate the proliferative phase of wound healing. When tissue is first wounded, blood comes in contact with collagen, triggering blood platelets to begin secreting inflammatory factors. Platelets also express sticky glycoproteins on their cell membranes that allow them to aggregate, forming a mass. Fibrin and fibronectin cross-link together and form a plug that traps proteins and particles and prevents

neg: Fibrin scaffold there is complete degradation of fibrin matrix after four weeks. Another study to assess if fibrin glue enriched with platelet is better than just platelet rich plasma (PRP) on bone formation was conducted. Each combined with bone marrow mesenchymal stem cells and bone morphogenetic protein 2 (BMP-2) are injected into the subcutaneous space. Results shows that fibrin glue enriched with platelet has better osteogenic properties when compared to PRP. To initiate and speed up tissue repair and regeneration, platelet-rich fibrin gels are ideal since they have a high concentration of platelet releasing growth factors and bioactive proteins. Addition of fibrin

neg: Bivalirudin heparin. US (United States) Indications: EU (European) indications: Mechanism of action" Bivalirudin directly inhibits thrombin by specifically binding both to the catalytic site and to the anion-binding exosite of circulating and clot-bound thrombin. Thrombin is a serine proteinase that plays a central role in the thrombotic process. It cleaves fibrinogen into fibrin monomers, activates Factor V, VIII, and XIII, allowing fibrin to develop a covalently cross-linked framework that stabilizes the thrombus. Thrombin also promotes further thrombin generation, and activates platelets, stimulating aggregation and granule release. The binding of bivalirudin to thrombin is reversible as thrombin slowly cleaves the bivalirudin-Arg-Pro bond,

neg: Darexaban to insoluble fibrin and to activate platelets. Stabilization of the platelet aggregation by fibrin mesh ultimately leads to clot formation. Darexaban is rapidly absorbed and extensively metabolized in the liver to its active metabolite, darexaban glucuronide (YM-222714) during first pass metabolism via glucuronidation. The metabolism of darexaban also occurs in the small intestine but to a much lesser extent. Glucuronidation of darexaban occurs quickly, thus the half life of darexaban itself is short. However, the resultant darexaban glucuronide metabolite has a long half life of approximately 14–18 hours, reaching its maximum levels in the blood 1-1.5 hour post dose. As

neg: Fetal bovine serum the harvesting of blood from the bovine fetus after the fetus is removed from the slaughtered cow. The blood is collected aseptically into a sterile container or blood bag and then allowed to clot. The normal method of collection is cardiac puncture, wherein a needle is inserted into the heart. This minimizes "the danger of serum contamination with micro-organisms from the fetus itself, and the environment". It is then centrifuged to remove the fibrin clot and the remaining blood cells from the clear yellow (straw) colored serum. The serum is frozen prior to further processing that is necessary to make

neg: Fibrinogen alpha chain renal amyloidosis. Alternative splicing results in two isoforms that vary in the carboxy-terminus. Fibrinogen alpha chain has been shown to interact with Tissue plasminogen activator. Fibrinogen alpha chain Fibrinogen alpha chain is a protein that in humans is encoded by the "FGA" gene. The protein encoded by this gene is the alpha component of fibrinogen, a blood-borne glycoprotein composed of three pairs of nonidentical polypeptide chains. Following vascular injury, fibrinogen is cleaved by thrombin to form fibrin, which is the most abundant component of blood clots. In addition, various cleavage products of fibrinogen and fibrin regulate cell adhesion and spreading,

neg: Fibronectin Along with fibrin, plasma fibronectin is deposited at the site of injury, forming a blood clot that stops bleeding and protects the underlying tissue. As repair of the injured tissue continues, fibroblasts and macrophages begin to remodel the area, degrading the proteins that form the provisional blood clot matrix and replacing them with a matrix that more resembles the normal, surrounding tissue. Fibroblasts secrete proteases, including matrix metalloproteinases, that digest the plasma fibronectin, and then the fibroblasts secrete cellular fibronectin and assemble it into an insoluble matrix. Fragmentation of fibronectin by proteases has been suggested to promote wound contraction, a

neg: Omega-3 fatty acid circulation and increase the breakdown of fibrin, a protein involved in blood clotting and scar formation. Omega−3 fatty acids reduce blood triglyceride levels but do not significantly change the level of LDL cholesterol or HDL cholesterol in the blood. The American Heart Association position (2011) is that borderline elevated triglycerides, defined as 150–199 mg/dL, can be lowered by 0.5-1.0 grams of EPA and DHA per day; high triglycerides 200–499 mg/dL benefit from 1-2 g/day; and >500 mg/dL be treated under a physician's supervision with 2-4 g/day using a prescription product. ALA does not confer the cardiovascular health benefits of EPA

neg: Thromboelastometry fibrinogen level or fibrin polymerization disorders, or low activity of factor XIII. A mechanically weak clot represents a severe bleeding risk and should initiate immediate therapeutic steps. High doses of heparin can lower MCF in the INTEM assay, but not in HEPTEM, EXTEM, FIBTEM or APTEM (see under “reagents”). A5, A 10, A15 or A20 value These values describe the clot firmness (or amplitude) obtained after 10, 15 or 20 minutes (beginning from CFT) and provide a forecast on the expected MCF value at an earlier stage already. A recent investigation has validated this approach for the A15 value in

neg: Cerastocytin cerastotin (from the venom of Cerastes cerastes), as well as thrombocytin (from Bothrops atrox) and many others, are serine proteases that function in a way very similar to thrombin. Like thrombin, these proteases are capable of inducing platelet aggregation, and some even fibrin clot formation, at nanomolar concentrations. Cerastocytin, like most other serine proteases, thrombin specifically, has three distinguishing features: the hydrophobic pocket, the positive surface and the catalytic triad. Additionally, the tertiary structure of cerastocytin is maintained by disulfide bridges similar to those formed in other serine proteases. This structural similarity results of cerastocytin’s ability to clot platelets and

neg: Thromboelastography 37 °C, but different temperatures can be selected, e.g. for patients with hypothermia. Sonoclot is the latest version of Thromboelastography which takes into account the initial viscosity changes (which typically happens before Fibrin polymerization) and later the elastic changes of the developed clot. There are several types of assays that can be run using TEG: Standard (kaolin), RapidTEG, heparinase, Functional Fibrinogen and PlateletMapping. A standard TEG is the most commonly ordered test and includes the parameters noted above. A RapidTEG uses tissue factor in addition to kaolin thereby further speeding up the reaction. In this assay, the R-value is replaced

neg: Staphylococcus aureus or enzyme-based tests. A Gram stain is first performed to guide the way, which should show typical Gram-positive bacteria, cocci, in clusters. Second, the isolate is cultured on mannitol salt agar, which is a selective medium with 7–9% NaCl that allows "S. aureus" to grow, producing yellow-colored colonies as a result of mannitol fermentation and subsequent drop in the medium's pH. Furthermore, for differentiation on the species level, catalase (positive for all "Staphylococcus" species), coagulase (fibrin clot formation, positive for "S. aureus"), DNAse (zone of clearance on DNase agar), lipase (a yellow color and rancid odor smell), and phosphatase (a