Two small peptide chains removed from the N-terminal segment of the alpha chains of fibrinogen by the action of thrombin during the blood coagulation process. Each peptide chain contains 18 amino acid residues. In vivo, fibrinopeptide A is used as a marker to determine the rate of conversion of fibrinogen to fibrin by thrombin.
Two small peptide chains removed from the N-terminal segment of the beta chains of fibrinogen by the action of thrombin. Each peptide chain contains 20 amino acid residues. The removal of fibrinopeptides B is not required for coagulation.
Fibrinogens which have a functional defect as the result of one or more amino acid substitutions in the amino acid sequence of normal fibrinogen. Abnormalities of the fibrinogen molecule may impair any of the major steps involved in the conversion of fibrinogen into stabilized fibrin, such as cleavage of the fibrinopeptides by thrombin, polymerization and cross-linking of fibrin. The resulting dysfibrinogenemias can be clinically silent or can be associated with bleeding, thrombosis or defective wound healing.
Plasma glycoprotein clotted by thrombin, composed of a dimer of three non-identical pairs of polypeptide chains (alpha, beta, gamma) held together by disulfide bonds. Fibrinogen clotting is a sol-gel change involving complex molecular arrangements: whereas fibrinogen is cleaved by thrombin to form polypeptides A and B, the proteolytic action of other enzymes yields different fibrinogen degradation products.
A proteolytic enzyme obtained from the venom of fer-de-lance (Bothrops atrox). It is used as a plasma clotting agent for fibrinogen and for the detection of fibrinogen degradation products. The presence of heparin does not interfere with the clotting test. Hemocoagulase is a mixture containing batroxobin and factor X activator. EC 3.4.21.-.
A protein derived from FIBRINOGEN in the presence of THROMBIN, which forms part of the blood clot.
A platelet-specific protein which is released when platelets aggregate. Elevated plasma levels have been reported after deep venous thrombosis, pre-eclampsia, myocardial infarction with mural thrombosis, and myeloproliferative disorders. Measurement of beta-thromboglobulin in biological fluids by radioimmunoassay is used for the diagnosis and assessment of progress of thromboembolic disorders.
An enzyme formed from PROTHROMBIN that converts FIBRINOGEN to FIBRIN.
Soluble protein fragments formed by the proteolytic action of plasmin on fibrin or fibrinogen. FDP and their complexes profoundly impair the hemostatic process and are a major cause of hemorrhage in intravascular coagulation and fibrinolysis.
An enzyme fraction from the venom of the Malayan pit viper, Agkistrodon rhodostoma. It catalyzes the hydrolysis of a number of amino acid esters and a limited proteolysis of fibrinogen. It is used clinically to produce controlled defibrination in patients requiring anticoagulant therapy. EC 3.4.21.-.
The process of the interaction of BLOOD COAGULATION FACTORS that results in an insoluble FIBRIN clot.
Clotting time of PLASMA mixed with a THROMBIN solution. It is a measure of the conversion of FIBRINOGEN to FIBRIN, which is prolonged by AFIBRINOGENEMIA, abnormal fibrinogen, or the presence of inhibitory substances, e.g., fibrin-fibrinogen degradation products, or HEPARIN. BATROXOBIN, a thrombin-like enzyme unaffected by the presence of heparin, may be used in place of thrombin.
A chromogenic substrate that permits direct measurement of peptide hydrolase activity, e.g., papain and trypsin, by colorimetry. The substrate liberates p-nitroaniline as a chromogenic product.
A plasma alpha 2 glycoprotein that accounts for the major antithrombin activity of normal plasma and also inhibits several other enzymes. It is a member of the serpin superfamily.
Arginine derivative which is a substrate for many proteolytic enzymes. As a substrate for the esterase from the first component of complement, it inhibits the action of C(l) on C(4).
The process which spontaneously arrests the flow of BLOOD from vessels carrying blood under pressure. It is accomplished by contraction of the vessels, adhesion and aggregation of formed blood elements (eg. ERYTHROCYTE AGGREGATION), and the process of BLOOD COAGULATION.
A plasma protein that is the inactive precursor of thrombin. It is converted to thrombin by a prothrombin activator complex consisting of factor Xa, factor V, phospholipid, and calcium ions. Deficiency of prothrombin leads to hypoprothrombinemia.
Single-chain polypeptides of about 65 amino acids (7 kDa) from LEECHES that have a neutral hydrophobic N terminus, an acidic hydrophilic C terminus, and a compact, hydrophobic core region. Recombinant hirudins lack tyr-63 sulfation and are referred to as 'desulfato-hirudins'. They form a stable non-covalent complex with ALPHA-THROMBIN, thereby abolishing its ability to cleave FIBRINOGEN.
A CXC chemokine that is found in the alpha granules of PLATELETS. The protein has a molecular size of 7800 kDa and can occur as a monomer, a dimer or a tetramer depending upon its concentration in solution. Platelet factor 4 has a high affinity for HEPARIN and is often found complexed with GLYCOPROTEINS such as PROTEIN C.
A nonapeptide that is found in neurons, peripheral organs, and plasma. This neuropeptide induces mainly delta sleep in mammals. In addition to sleep, the peptide has been observed to affect electrophysiological activity, neurotransmitter levels in the brain, circadian and locomotor patterns, hormonal levels, psychological performance, and the activity of neuropharmacological drugs including their withdrawal.
Endogenous substances, usually proteins, that are involved in the blood coagulation process.
Hemorrhagic and thrombotic disorders that occur as a consequence of abnormalities in blood coagulation due to a variety of factors such as COAGULATION PROTEIN DISORDERS; BLOOD PLATELET DISORDERS; BLOOD PROTEIN DISORDERS or nutritional conditions.
The natural enzymatic dissolution of FIBRIN.
Clotting time of PLASMA recalcified in the presence of excess TISSUE THROMBOPLASTIN. Factors measured are FIBRINOGEN; PROTHROMBIN; FACTOR V; FACTOR VII; and FACTOR X. It is used for monitoring anticoagulant therapy with COUMARINS.
Limbless REPTILES of the suborder Serpentes.
A deficiency or absence of FIBRINOGEN in the blood.
A disorder characterized by procoagulant substances entering the general circulation causing a systemic thrombotic process. The activation of the clotting mechanism may arise from any of a number of disorders. A majority of the patients manifest skin lesions, sometimes leading to PURPURA FULMINANS.
Laboratory tests for evaluating the individual's clotting mechanism.
Hydrofluoric acid. A solution of hydrogen fluoride in water. It is a colorless fuming liquid which can cause painful burns.
Serum proteins with an electrophoretic mobility that falls between ALPHA-GLOBULINS and GAMMA-GLOBULINS.
A fibrin-stabilizing plasma enzyme (TRANSGLUTAMINASES) that is activated by THROMBIN and CALCIUM to form FACTOR XIIIA. It is important for stabilizing the formation of the fibrin polymer (clot) which culminates the coagulation cascade.
Formation and development of a thrombus or blood clot in the blood vessel.
A highly acidic mucopolysaccharide formed of equal parts of sulfated D-glucosamine and D-glucuronic acid with sulfaminic bridges. The molecular weight ranges from six to twenty thousand. Heparin occurs in and is obtained from liver, lung, mast cells, etc., of vertebrates. Its function is unknown, but it is used to prevent blood clotting in vivo and vitro, in the form of many different salts.
A product of the lysis of plasminogen (profibrinolysin) by PLASMINOGEN activators. It is composed of two polypeptide chains, light (B) and heavy (A), with a molecular weight of 75,000. It is the major proteolytic enzyme involved in blood clot retraction or the lysis of fibrin and quickly inactivated by antiplasmins.
Classic quantitative assay for detection of antigen-antibody reactions using a radioactively labeled substance (radioligand) either directly or indirectly to measure the binding of the unlabeled substance to a specific antibody or other receptor system. Non-immunogenic substances (e.g., haptens) can be measured if coupled to larger carrier proteins (e.g., bovine gamma-globulin or human serum albumin) capable of inducing antibody formation.
Streptococcal fibrinolysin . An enzyme produced by hemolytic streptococci. It hydrolyzes amide linkages and serves as an activator of plasminogen. It is used in thrombolytic therapy and is used also in mixtures with streptodornase (STREPTODORNASE AND STREPTOKINASE). EC 3.4.-.
The time required for the appearance of FIBRIN strands following the mixing of PLASMA with phospholipid platelet substitute (e.g., crude cephalins, soybean phosphatides). It is a test of the intrinsic pathway (factors VIII, IX, XI, and XII) and the common pathway (fibrinogen, prothrombin, factors V and X) of BLOOD COAGULATION. It is used as a screening test and to monitor HEPARIN therapy.
A clinical syndrome characterized by the development of CHEST PAIN at rest with concomitant transient ST segment elevation in the ELECTROCARDIOGRAM, but with preserved exercise capacity.
Non-nucleated disk-shaped cells formed in the megakaryocyte and found in the blood of all mammals. They are mainly involved in blood coagulation.
Venoms from snakes of the subfamily Crotalinae or pit vipers, found mostly in the Americas. They include the rattlesnake, cottonmouth, fer-de-lance, bushmaster, and American copperhead. Their venoms contain nontoxic proteins, cardio-, hemo-, cyto-, and neurotoxins, and many enzymes, especially phospholipases A. Many of the toxins have been characterized.
Precordial pain at rest, which may precede a MYOCARDIAL INFARCTION.
Constituent composed of protein and phospholipid that is widely distributed in many tissues. It serves as a cofactor with factor VIIa to activate factor X in the extrinsic pathway of blood coagulation.
Stable iodine atoms that have the same atomic number as the element iodine, but differ in atomic weight. I-127 is the only naturally occurring stable iodine isotope.

Inhibition of thrombin generation by simvastatin and lack of additive effects of aspirin in patients with marked hypercholesterolemia. (1/203)

OBJECTIVES: To assess the effects of aspirin compared with simvastatin on thrombin generation in hypercholesterolemic men, and to establish whether the reduction of elevated blood cholesterol by simvastatin would affect the action of aspirin on thrombin formation. BACKGROUND: Aspirin inhibits thrombin formation, but its performance is blunted in hypercholesterolemia. By virtue of altering lipid profile, statins could be expected to influence thrombin generation. METHODS: Thirty-three men, aged 34 to 61 years, with minimal or no clinical symptoms, serum total cholesterol >6.5 mmol/liter and serum triglycerides <4.6 mmol/liter, completed the study consisting of three treatment phases. First, they received 300 mg of aspirin daily for two weeks (phase I), which was then replaced by simvastatin at the average dose of 24 mg/d for three months (phase II). In phase III, aspirin, 300 mg/day, was added for two weeks to simvastatin, the dose of which remained unchanged. Thrombin generation was assessed: 1) in vivo, by measuring levels of fibrinopeptide A (FPA) and prothrombin fragment 1+2 (F1+2) in venous blood; and 2) ex vivo, by monitoring the rates of increase of FPA and F1+2 in blood emerging from standardized skin incisions of a forearm. A mathematical model was used to describe the kinetics of thrombin formation at the site of microvascular injury. RESULTS: Two-week treatment with aspirin had no effect on thrombin markers in vivo, while ex vivo it depressed the total amount of thrombin formed, though not the reaction rate. After simvastatin treatment, serum cholesterol decreased by 31% and LDL cholesterol by 42%, while thrombin generation became markedly depressed. In venous blood, FPA was significantly reduced. Concomitantly, the initial thrombin concentration and total amount of thrombin generated decreased significantly. Addition of aspirin to simvastatin (phase III) had no further effect on any of these parameters. CONCLUSIONS: In men with hypercholesterolemia, lowering serum cholesterol level by a three-month simvastatin treatment is accompanied by a marked reduction of thrombin generation both at basal conditions in venous blood and after activation of hemostasis by microvascular injury. Once blood cholesterol became reduced, adding aspirin to simvastatin did not enhance dampening of thrombin formation.  (+info)

Dose response of intravenous heparin on markers of thrombosis during primary total hip replacement. (2/203)

BACKGROUND: Thrombogenesis in total hip replacement (THR) begins during surgery on the femur. This study assesses the effect of two doses of unfractionated intravenous heparin administered before femoral preparation during THR on circulating markers of thrombosis. METHODS: Seventy-five patients undergoing hybrid primary THR were randomly assigned to receive blinded intravenous injection of either saline or 10 or 20 U/kg of unfractionated heparin after insertion of the acetabular component. Central venous blood samples were assayed for prothrombin F1+2 (F1+2), thrombin-antithrombin complexes (TAT), fibrinopeptide A (FPA), and D-dimer. RESULTS: No changes in the markers of thrombosis were noted after insertion of the acetabular component. During surgery on the femur, significant increases in all markers were noted in the saline group (P < 0.0001). Heparin did not affect D-dimer or TAT. Twenty units per kilogram of heparin significantly reduced the increase of F1+2 after relocation of the hip joint (P < 0.001). Administration of both 10 and 20 U/kg significantly reduced the increase in FPA during implantation of the femoral component (P < 0.0001). A fourfold increase in FPA was noted in 6 of 25 patients receiving 10 U/kg of heparin but in none receiving 20 U/kg (P = 0.03). Intraoperative heparin did not affect intra- or postoperative blood loss, postoperative hematocrit, or surgeon's subjective assessments of bleeding. No bleeding complications were noted. CONCLUSIONS: This study demonstrates that 20 U/kg of heparin administered before surgery on the femur suppresses fibrin formation during primary THR. This finding provides the pathophysiologic basis for the clinical use of intraoperative heparin during THR.  (+info)

Prognostic significance of elevated hemostatic markers in patients with acute myocardial infarction. (3/203)

OBJECTIVES: The purpose of this study was to determine whether the elevated levels of hemostatic markers in the early phase of myocardial infarction may serve as risk factors for subsequent cardiac mortality. BACKGROUND: Increased plasma hemostatic markers were noted in acute myocardial infarction, indicating that the blood coagulation system is highly activated in those patients. However, there are few clinical data concerning the association between the elevated hemostatic markers and survival in patients with myocardial infarction. METHODS: Blood samples were obtained from 64 patients (mean age 67 +/- 11 years; 49 male) with acute myocardial infarction within 12 h after the onset of symptoms and before the initiation of any antithrombotic treatment. We measured plasma concentrations of fibrinopeptide A (FPA), prothrombin fragment 1+2 (F1+2) and thrombin-antithrombin complex (TAT) using the enzyme-linked immunosorbent assay method, and examined the associations between the level of these markers and survival with Cox proportional hazards models. RESULTS: The follow-up time was 27 +/- 17 months, and 19 patients died of cardiac causes during the follow-up. Univariate survival analysis identified Killip class IV (hazard ratio 4.86; 95% confidence interval [CI] 1.55-15.19), left ventricular ejection fraction (hazard ratio 0.94; 95% CI 0.90-0.99), FPA (hazard ratio 1.54; 95% CI 1.13-2.10), F1+2 (hazard ratio 2.03; 95% CI 1.17-3.53) and TAT (hazard ratio 1.88; 95% CI 1.27-2.79) as significant factors associated with cardiac mortality. In multivariate analyses, only FPA level (hazard ratio 1.84; 95% CI 1.03-3.30) and left ventricular ejection fraction (hazard ratio 0.93; 95% CI 0.88-0.98) were independent predictors of cardiac mortality. CONCLUSIONS: Elevated FPA in the early phase of myocardial infarction identifies patients with increased risk for subsequent cardiac death. This association appears to be independent of residual left ventricular function after infarction.  (+info)

An integrated study of fibrinogen during blood coagulation. (4/203)

The rate of conversion of fibrinogen (Fg) to the insoluble product fibrin (Fn) is a key factor in hemostasis. We have developed methods to quantitate fibrinopeptides (FPs) and soluble and insoluble Fg/Fn products during the tissue factor induced clotting of whole blood. Significant FPA generation (>50%) occurs prior to visible clotting (4 +/- 0.2 min) coincident with factor XIII activation. At this time Fg is mostly in solution along with high molecular weight cross-linked products. Cross-linking of gamma-chains is virtually complete (5 min) prior to the release of FPB, a process that does not occur until after clot formation. FPB is detected still attached to the beta-chain throughout the time course demonstrating release of only low levels of FPB from the clot. After release of FPB a carboxypeptidase-B-like enzyme removes the carboxyl-terminal arginine resulting exclusively in des-Arg FPB by the 20-min time point. This process is inhibited by epsilon-aminocaproic acid. These results demonstrate that transglutaminase and carboxypeptidase enzymes are activated simultaneously with Fn formation. The initial clot is a composite of Fn I and Fg already displaying gamma-gamma cross-linking prior to the formation of Fn II with Bbeta-chain remaining mostly intact followed by the selective degradation of FPB to des-Arg FPB.  (+info)

Transglutaminase-catalyzed crosslinking of the Aalpha and gamma constituent chains in fibrinogen. (5/203)

Studies on transglutaminases usually focus on the polymerization of protein substrates by intermolecular N(epsilon)(gamma-glutamyl)lysine bridges, without considering the possibility that the monomeric protein units, themselves, could also become crosslinked internally. Both types of crosslinks are produced in the reaction of fibrinogen with red cell transglutaminase. We isolated the transglutaminase-modified, mostly monomeric form (92-96%) of fibrinogen with a N(epsilon)(gamma-glutamyl)lysine content of approximately 1.6 moles/mole of fibrinogen. The preparation was fully clottable by thrombin, but the rates of release of fibrinopeptides and clotting times were delayed compared with control. Hybrid Aalpha.gamma type of crosslinking, the hallmark of the reaction of the transglutaminase with fibrinogen, occurred by bridging the Aalpha(408-421) chain segment of the protein to that of gamma(392-406). Rotary shadowed electron microscope images showed many monomers to be bent, and the crosslinks seemed to bind the otherwise flexible alphaC domain closer to the backbone of fibrinogen.  (+info)

Hemostatic markers in patients at risk of cerebral ischemia. (6/203)

BACKGROUND: Increased levels of markers of hemostasis may assist in the determination of the extent of carotid occlusive disease and the identification of neurologically intact individuals at increased risk of ischemic events. METHODS: We conducted a prospective study of 304 subjects, including 82 with a recent (< or =7 days) transient ischemic attack (TIA), 157 asymptomatic individuals with a cervical bruit, and 65 control subjects. Baseline evaluation included a neurological assessment, ECG, cervical ultrasonography, and cerebral CT and/or MRI. Levels of markers of coagulation and fibrinolytic activity were also determined. Results were analyzed in relation to the degree of carotid disease and the subsequent occurrence of cerebral and cardiac ischemic events. RESULTS: Over a mean follow-up period of 2.8 years (SD, 1.3 years), 114 ischemic events occurred. Survival analyses showed that prothrombin fragment 1.2 (F(1.2)) was a predictor of time to cerebral and cardiac ischemic events in the combined TIA and asymptomatic bruit group (relative risk [RR], 1.46; 95% CI, 1.18 to 1.81) as well as in the asymptomatic bruit group separately (RR, 1.70; 95% CI, 1.14 to 2.53). In the TIA group, both F(1.2) (RR, 2.36; 95% CI, 1.19 to 4.68) and severe (> or =80%) carotid stenosis (RR, 3.53; 95% CI, 1.19 to 10.51) were predictive of time to ischemic stroke, myocardial infarction, or vascular death. CONCLUSIONS: In patients with TIAs and in asymptomatic individuals with cervical bruits, F(1.2) levels were found to be independent predictors of subsequent cerebral and cardiac ischemic events. Our results are consistent with an active role of the coagulation system through upregulation of thrombin in carotid disease progression and in the pathogenesis of ischemic events in patients at risk.  (+info)

Prospective study correlating fibrinopeptide A, troponin I, myoglobin, and myosin light chain levels with early and late ischemic events in consecutive patients presenting to the emergency department with chest pain. (7/203)

BACKGROUND: Although thrombus formation plays a major role in acute coronary syndromes, few studies have evaluated a thrombus marker in risk stratification of patients with chest pain. Furthermore, the relation between markers that reflect myocardial injury and thrombus formation that may predict events in a heterogeneous patient population is unknown. This study correlated markers of thrombus and myocardial injury with early and late ischemic events in consecutive patients with chest pain. METHODS AND RESULTS: Serum troponin I (TnI), myoglobin, and myosin light chain levels were obtained from 247 patients and urinary fibrinopeptide A (FPA) from 178 of the 247. By multivariate analysis, patients with an elevated FPA level were 4.82 times more likely to die or have myocardial infarction, unstable angina, and coronary revascularization at 1 week (P=0.002, 95% CI 1.78, 13.03), whereas those with an elevated TnI (>0.2 ng/mL) were 9.41 times more likely (P<0.001, 95% CI 2.84, 31.17). At 6 months (excluding the index event), an elevated FPA level was an independent predictor of events, with an odds ratio of 9.57 (P<0.001, C1 3.29, 27.8), and was the only marker to predict a shorter event-free survival (P<0.001). The other markers did not independently correlate with cardiac events, although MLC incrementally increased early predictive accuracy in combination with the FPA and TnI. CONCLUSIONS: Elevated FPA and TnI correlated with cardiac events during the initial week in patients presenting to the Emergency Department with chest pain. FPA predicted adverse events and a shorter event-free survival at 6 months.  (+info)

Analysis of fibrin formation and proteolysis during intravenous administration of ancrod. (8/203)

Ancrod is a purified fraction of venom from the Malayan pit viper, Calloselasma rhodostoma, currently under investigation for treatment of acute ischemic stroke. Treatment with ancrod leads to fibrinogen depletion. The present study investigated the mechanisms leading to the reduction of plasma fibrinogen concentration. Twelve healthy volunteers received an intravenous infusion of 0.17 U/kg body weight of ancrod for 6 hours. Blood samples were drawn and analyzed before and at various time points until 72 hours after start of infusion. Ancrod releases fibrinopeptide A from fibrinogen, leading to the formation of desAA-fibrin monomer. In addition, a considerable proportion of desA-profibrin is formed. Production of desA-profibrin is highest at low concentrations of ancrod, whereas desA-profibrin is rapidly converted to desAA-fibrin at higher concentrations of ancrod. Both desA-profibrin and desAA-fibrin monomers form fibrin complexes. A certain proportion of complexes carries exposed fibrin polymerization sites E(A), indicating that the terminal component of the protofibril is a desAA-fibrin monomer unit. Soluble fibrin complexes potentiate tissue-type plasminogen activator-induced plasminogen activation. Significant amounts of plasmin are formed when soluble fibrin in plasma reaches a threshold concentration, leading to the proteolytic degradation of fibrinogen and fibrin. In the present setting, high concentrations of soluble fibrin are detected after 1 hour of ancrod infusion, whereas a rise in fibrinogen and fibrin degradation products, and plasmin-alpha(2)-plasmin inhibitor complex levels is first detected after 2 hours of ancrod infusion. Ancrod treatment also results in the appearance of cross-inked fibrin degradation product D-dimer in plasma. (Blood. 2000;96:2793-2802)  (+info)

Types of Blood Coagulation Disorders:

1. Hemophilia A: A genetic disorder that affects the blood's ability to clot, leading to prolonged bleeding after injury or surgery.
2. Hemophilia B: Similar to hemophilia A, but caused by a deficiency of factor IX instead of factor VIII.
3. Von Willebrand Disease (VWD): A bleeding disorder caused by a deficiency of von Willebrand factor, which is needed for blood clotting.
4. Platelet Disorders: These include conditions such as low platelet count (thrombocytopenia) or abnormal platelet function, which can increase the risk of bleeding.
5. Coagulopathy: A general term for any disorder that affects the body's blood coagulation process.

Symptoms and Diagnosis:

Blood coagulation disorders can cause a range of symptoms, including easy bruising, frequent nosebleeds, and prolonged bleeding after injury or surgery. Diagnosis is typically made through a combination of physical examination, medical history, and laboratory tests such as blood clotting factor assays and platelet function tests.

Treatment and Management:

Treatment for blood coagulation disorders depends on the specific condition and its severity. Some common treatments include:

1. Infusions of clotting factor concentrates to replace missing or deficient factors.
2. Desmopressin, a medication that stimulates the release of von Willebrand factor and platelets.
3. Platelet transfusions to increase platelet count.
4. Anticoagulation therapy to prevent blood clots from forming.
5. Surgery to repair damaged blood vessels or joints.

Prevention and Prognosis:

Prevention of blood coagulation disorders is often challenging, but some steps can be taken to reduce the risk of developing these conditions. These include:

1. Avoiding trauma or injury that can cause bleeding.
2. Managing underlying medical conditions such as liver disease, vitamin deficiencies, and autoimmune disorders.
3. Avoiding medications that can interfere with blood clotting.

The prognosis for blood coagulation disorders varies depending on the specific condition and its severity. Some conditions, such as mild hemophilia A, may have a good prognosis with appropriate treatment, while others, such as severe hemophilia B, can have a poor prognosis without proper management.

Complications and Comorbidities:

Blood coagulation disorders can lead to a range of complications and comorbidities, including:

1. Joint damage and chronic pain due to repeated bleeding into joints.
2. Infection and sepsis from bacteria entering the body through bleeding sites.
3. Arthritis and other inflammatory conditions.
4. Nerve damage and neuropathy from bleeding into nerve tissue.
5. Increased risk of bleeding during surgery or trauma.
6. Emotional and social challenges due to the impact of the condition on daily life.
7. Financial burden of treatment and management costs.
8. Impaired quality of life, including reduced mobility and activity levels.
9. Increased risk of blood clots and thromboembolic events.
10. Psychological distress and anxiety related to the condition.


Blood coagulation disorders are a group of rare and complex conditions that can significantly impact quality of life, productivity, and longevity. These disorders can be caused by genetic or acquired factors and can lead to a range of complications and comorbidities. Diagnosis is often challenging, but prompt recognition and appropriate treatment can improve outcomes. Management strategies include replacing missing clotting factors, using blood products, and managing underlying conditions. While the prognosis varies depending on the specific condition and its severity, early diagnosis and effective management can improve quality of life and reduce the risk of complications.

In DIC, the body's normal blood coagulation mechanisms become overactive and begin to form clots throughout the circulatory system, including in small blood vessels and organs. This can cause a range of symptoms, including bleeding, fever, and organ failure.

DIC is often seen in sepsis, which is a severe infection that has spread throughout the body. It can also be caused by other conditions such as trauma, cancer, and autoimmune disorders.

Treatment of DIC typically involves addressing the underlying cause, such as treating an infection or injury, as well as supporting the body's natural clotting mechanisms and preventing further bleeding. In severe cases, hospitalization and intensive care may be necessary to monitor and treat the condition.

In summary, Disseminated Intravascular Coagulation (DIC) is a serious medical condition that can cause widespread clotting and damage to the body's organs and tissues. It is often seen in sepsis and other severe conditions, and treatment typically involves addressing the underlying cause and supporting the body's natural clotting mechanisms.

There are several types of thrombosis, including:

1. Deep vein thrombosis (DVT): A clot forms in the deep veins of the legs, which can cause swelling, pain, and skin discoloration.
2. Pulmonary embolism (PE): A clot breaks loose from another location in the body and travels to the lungs, where it can cause shortness of breath, chest pain, and coughing up blood.
3. Cerebral thrombosis: A clot forms in the brain, which can cause stroke or mini-stroke symptoms such as weakness, numbness, or difficulty speaking.
4. Coronary thrombosis: A clot forms in the coronary arteries, which supply blood to the heart muscle, leading to a heart attack.
5. Renal thrombosis: A clot forms in the kidneys, which can cause kidney damage or failure.

The symptoms of thrombosis can vary depending on the location and size of the clot. Some common symptoms include:

1. Swelling or redness in the affected limb
2. Pain or tenderness in the affected area
3. Warmth or discoloration of the skin
4. Shortness of breath or chest pain if the clot has traveled to the lungs
5. Weakness, numbness, or difficulty speaking if the clot has formed in the brain
6. Rapid heart rate or irregular heartbeat
7. Feeling of anxiety or panic

Treatment for thrombosis usually involves medications to dissolve the clot and prevent new ones from forming. In some cases, surgery may be necessary to remove the clot or repair the damaged blood vessel. Prevention measures include maintaining a healthy weight, exercising regularly, avoiding long periods of immobility, and managing chronic conditions such as high blood pressure and diabetes.

The causes of angina pectoris, variant are not well understood, but it is believed to be related to a decrease in blood flow to the heart muscle, particularly during times of rest or low exertion. This can lead to a lack of oxygen and nutrients to the heart muscle, which can cause pain.

The diagnosis of angina pectoris, variant is based on a combination of clinical symptoms, physical examination findings, and results of diagnostic tests such as electrocardiography (ECG), stress test, and echocardiography. Treatment for this condition typically involves medications such as nitrates, calcium channel blockers, and beta-blockers to relieve pain and improve blood flow to the heart muscle. In some cases, surgery may be necessary to improve blood flow or to treat underlying conditions that are contributing to the angina.

Prevention of angina pectoris, variant includes lifestyle modifications such as regular exercise, stress reduction techniques, and avoiding smoking and alcohol consumption. It is important for individuals with this condition to work closely with their healthcare provider to manage their symptoms and prevent complications.

Word origin: Greek "anginos" meaning "pain in the neck".

The fibrinopeptides, fibrinopeptide A (FpA) and fibrinopeptide B (FpB), are peptides which are located in the central region of ...
O'Neil, P. B.; Doolittle, R. F. (1973). "Mammalian Phylogeny Based on Fibrinopeptide Amino Acid Sequences". Systematic Zoology ...
Reptilase also differs from thrombin by releasing fibrinopeptide A, but not fibrinopeptide B, in its cleavage of fibrinogen.[ ...
... is formed after thrombin cleavage of fibrinopeptide A (FPA) from fibrinogen Aalpha-chains, thus initiating fibrin ...
... contains a hydrophobic domain that binds fibrinopeptide A and in the 3-D confirmation looks very similar to the ... This data suggests that cerastocytin has distinct sites for platelet and fibrinopeptide binding because the two functions could ...
Sulfation was first discovered by Bettelheim in bovine fibrinopeptide B in 1954 and later found to be present in animals and ...
... and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme ...
Examples include prothrombin fragment 1+2 (F1+2), thrombin-antithrombin complex (TAT), fibrinopeptide A (FpA), fibrin monomers ...
... it more reliable for measuring ongoing coagulation than other markers like thrombin-antithrombin complexes and fibrinopeptide A ...
... it releases fibrinopeptide A or B. Thrombin acts on two exosites to fibrinogen. Exosite 1 mediates the binding of thrombin to ...
... television station Fast patrol boat Federal Planning Bureau of Belgium Federation of Trade Unions of Belarus Fibrinopeptide B, ...
Fibrinopeptide A is a substance released as blood clots in your body. A test can be done to measure the level of this substance ... Fibrinopeptide A is a substance released as blood clots in your body. A test can be done to measure the level of this substance ... In general, the level of fibrinopeptide A should range from 0.6 to 1.9 (mg/mL). ...
Changes in fibrinopeptide A peptides in the sera of rats chronically exposed to low doses of 2,3,7,8-tetrachlorodibenzo-p- ... Changes in fibrinopeptide A peptides in the sera of rats chronically exposed to low doses of 2,3,7,8-tetrachlorodibenzo-p- ... The MS BLAST homology search engine reported the peptide to be a partial sequence of fibrinopeptide A. Liver fatty degeneration ... Levels of fibrinopeptide A were significantly correlated with liver fatty degeneration and necrosis. ...
Fibrinopeptide A Polyclonal Antibody - Affinity Purified. SAFPA-AP - Sheep anti human Fibrinopeptide A (1-16 specific), ... Fibrinopeptide A Polyclonal Antibody. SAFPA-IG - Sheep anti human Fibrinopeptide A, purified IgG (10.0 mg vial) ... Fibrinopeptide A Polyclonal Antibody - HRP Conjugated. Antibodies Affinitys Fibrinopeptide A Polyclonal Antibody - HRP ...
Pulmonary Embolism: Urine Fibrinopeptide B As Screening Tool. Posted at 15:44h in Blood Clots, General Medicine, UCSD by Marie ... The urine fibrinopeptide B assay at a cut-off of 2.5 ng/ml had a sensitivity of 75.4% for detecting pulmonary embolism. For ... Urine Fibrinopeptide B As A Screening Test For Acute Pulmonary Embolism. Type: Scientific Abstract. Category: 18.08 - Pulmonary ...
Fibrinopeptide 1.2 (pmol/L). 0%(0/58). 1.7% (1/58). Protein C (% activity). 0% (0/59). 0% (0/59). ...
Fibrin Polymerization Studied by Static and Dynamic Light-Scattering as a Function of Fibrinopeptide a Release. P. Wiltzius; G ...
Variations in position Arg-35 (the site of cleavage of fibrinopeptide a by thrombin) leads to alpha-dysfibrinogenemias. ...
The fibrinopeptide Bβ15-42 has a direct protective effect on tubular epithelial cells, which is largely determined by binding ... Binding of Cell Surface Carboxypeptidase M Contributes to Tubulo-Protective Effects of Fibrinopeptide Bß15-42. October 25, 2018 ... Binding of Cell Surface Carboxypeptidase M Contributes to Tubulo-Protective Effects of Fibrinopeptide Bß15-42. Session ...
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... and phosphorylated fibrinopeptide A and decreased fibrinogen in migraine susceptibility, especially for MA, potentially ... fibrinopeptide A, and phosphorylated fibrinopeptide A, which were estimated using inverse variance-weighted (IVW) Mendelian ... When extended to migraine subtypes, FVIII, vWF, and phosphorylated fibrinopeptide A showed slightly stronger effects with MA ... Conclusions: The findings support potential causality of increased FVIII, vWF, and phosphorylated fibrinopeptide A and ...
Studies with human fibrinopeptide B.. Senior RM; Skogen WF; Griffin GL; Wilner GD. J Clin Invest; 1986 Mar; 77(3):1014-9. ...
Fibrinopeptide A Preferred Term Term UI T016316. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1976). ... Fibrinopeptide A. Tree Number(s). D12.644.200. D12.776.124.125.515. D12.776.124.270.310. D12.776.811.300.310. D23.101.340. ... Fibrinopeptide A Preferred Concept UI. M0008435. Registry Number. 25422-31-5. Scope Note. Two small peptide chains removed from ... In vivo, fibrinopeptide A is used as a marker to determine the rate of conversion of fibrinogen to fibrin by thrombin.. Terms. ...
Cell proteins, such as hemoglobin B, fibrinopeptide A, or cytochrome C, can take on a bewildering myriad of forms, and every ...
... fibrinopeptide A, thrombin/antithrombin complexes, and D-dimer), even in steady state; whether this change is in relationship ...
Fibrinopeptide B Preferred Term Term UI T016318. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1976). ... Fibrinopeptide B Preferred Concept UI. M0008436. Registry Number. 36204-23-6. Scope Note. Two small peptide chains removed from ... Fibrinopeptide B. Tree Number(s). D12.644.205. D12.776.124.125.530. D12.776.124.270.320. D12.776.811.300.320. D23.119.510. ...
Identified MWCNT-responsive peptides depicted a mechanism involving aberrant fibrinolysis (fibrinopeptide A), blood-brain ...
RESULTS: Thrombin-catalyzed fibrinopeptide A release was normal, but fibrinopeptide B release was delayed for all variants. The ... uniquely altered polymerization associated with slower fibrinopeptide A than fibrinopeptide B release. ... In contrast to thrombin, which releases fibrinopeptide A and B from the NH2-terminal domains of the Aα- and Bß-chains of ... Different expression of fibrinopeptide A and related fragments in serum of type 1 diabetic patients with nephropathy. ...
fibrinogen -> fibrin monomer + 2 fibrinopeptide A + 2 fibrinopeptide B (Homo sapiens) * Extracellular thrombin inactivating ...
Fibrinopeptide B - Preferred Concept UI. M0008436. Scope note. Two small peptide chains removed from the N-terminal segment of ...
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Fibrinopeptide B, human. 1 mg. F3208. Fibrinopeptide B, human. 2 mg. F3208. Fibrinopeptide B, human. 5 mg. ...
Importance of continued activation of thrombin reflected by fibrinopeptide A to the efficacy of thrombolysis. Eisenberg, P. R. ...
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More sensitive tests quantifying proteolytic cleavage products of coagulation reactions (fibrinopeptide A, F1+2) and ...
Results were compared with measurements of fibrinopeptide A (FPA) and of serum fibrinogen-related antigen (FRA). Plasma TDP ... Results were compared with measurements of fibrinopeptide A (FPA) and of serum fibrinogen-related antigen (FRA). Plasma TDP ...
Abnormal N0000006076 Fibrinolysin N0000171484 Fibrinopeptide A N0000171487 Fibrinopeptide B N0000171006 Fibroblast Growth ...
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Fibrinopeptide Fibrinopeptides are short amino acid sequences located on the. soluble fibrinogen molecule.. Fibrinthrombus Net ...
Fibrinopeptide A. *Genetic Markers. *Oligoclonal Bands. *Environmental Monitoring. *Biological Oxygen Demand Analysis ...
  • In vivo, fibrinopeptide A is used as a marker to determine the rate of conversion of fibrinogen to fibrin by thrombin. (
  • In contrast to thrombin, which releases fibrinopeptide A and B from the NH2-terminal domains of the Aα- and Bß-chains of fibrinogen, respectively, batroxobin only releases fibrinopeptide A. Because the mechanism responsible for these differences is unknown, we compared the interactions of batroxobin and thrombin with the predominant γA/γA isoform of fibrin(ogen) and the γA/γ' variant with an extended γ-chain. (
  • Results were compared with measurements of fibrinopeptide A (FPA) and of serum fibrinogen-related antigen (FRA). (
  • If the mutation is confirmed, we investigate its effect on the structure and function of fibrinogen with specialized methods (fibrin polymerization curves, fibrinolysis, quantification of fibrinopeptide cleavage by HPLC, SEM, LC-MS/MS, structural modeling). (
  • Identified MWCNT-responsive peptides depicted a mechanism involving aberrant fibrinolysis (fibrinopeptide A), blood-brain barrier permeation (homeobox protein A4), neuroinflammation (transmembrane protein 131L) with reactivity by astrocytes and microglia, and a pro-degradative (signal transducing adapter molecule, phosphoglycerate kinase), antiplastic (AF4/FMR2 family member 1, vacuolar protein sorting-associated protein 18) state with the excitation-inhibition balance shifted to a hyperexcited (microtubule-associated protein 1B) phenotype. (
  • The MS BLAST homology search engine reported the peptide to be a partial sequence of fibrinopeptide A. Liver fatty degeneration and necrosis were assessed by hematoxylin and eosin staining. (
  • Studies with human fibrinopeptide B. (
  • The fibrinopeptide Bβ15-42 has a direct protective effect on tubular epithelial cells, which is largely determined by binding to CBPM and inhibition of CBPM enzymatic activity. (
  • A snake venom that directly activates fibrinogen by cleaving fibrinopeptide A is used as a reagent in the reptilase time test. (
  • In contrast to thrombin, reptilase cleaves only fibrinopeptide A (not fibrinopeptide B) during fibrin clot formation. (
  • Fibrinopeptide A is a substance released as blood clots in your body. (
  • The route of administration determines the relative availability of different molecular species that exert the anti-Xa, anti-IIa, fibrinopeptide A generation inhibiting actions and the release of tissue plasminogen activator-like activity from the endothelial cell lining. (