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 deficiency or absence of FIBRINOGEN in the blood.
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.
A protein derived from FIBRINOGEN in the presence of THROMBIN, which forms part of the blood clot.
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.
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.
Non-nucleated disk-shaped cells formed in the megakaryocyte and found in the blood of all mammals. They are mainly involved in blood coagulation.
Surface glycoproteins on platelets which have a key role in hemostasis and thrombosis such as platelet adhesion and aggregation. Many of these are receptors.
The attachment of PLATELETS to one another. This clumping together can be induced by a number of agents (e.g., THROMBIN; COLLAGEN) and is part of the mechanism leading to the formation of a THROMBUS.
The process of the interaction of BLOOD COAGULATION FACTORS that results in an insoluble FIBRIN clot.
An enzyme formed from PROTHROMBIN that converts FIBRINOGEN to FIBRIN.
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.
Receptors that bind FIBRINOGEN through distinct adhesive sequences on the fibrinogen molecule. Although MACROPHAGE-1 ANTIGEN is considered an important signaling molecule for fibrinogen interaction, a variety of INTEGRINS from all three major families, (beta1, beta2, and beta3) have been shown to bind fibrinogen.
Platelet membrane glycoprotein complex important for platelet adhesion and aggregation. It is an integrin complex containing INTEGRIN ALPHAIIB and INTEGRIN BETA3 which recognizes the arginine-glycine-aspartic acid (RGD) sequence present on several adhesive proteins. As such, it is a receptor for FIBRINOGEN; VON WILLEBRAND FACTOR; FIBRONECTIN; VITRONECTIN; and THROMBOSPONDINS. A deficiency of GPIIb-IIIa results in GLANZMANN THROMBASTHENIA.
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.
Laboratory tests for evaluating the individual's clotting mechanism.
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.
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.
The process whereby PLATELETS adhere to something other than platelets, e.g., COLLAGEN; BASEMENT MEMBRANE; MICROFIBRILS; or other "foreign" surfaces.
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.
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.-.
Retraction of a clot resulting from contraction of PLATELET pseudopods attached to FIBRIN strands. The retraction is dependent on the contractile protein thrombosthenin. Clot retraction is used as a measure of platelet function.
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 series of progressive, overlapping events, triggered by exposure of the PLATELETS to subendothelial tissue. These events include shape change, adhesiveness, aggregation, and release reactions. When carried through to completion, these events lead to the formation of a stable hemostatic plug.
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.
Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.
The internal resistance of the BLOOD to shear forces. The in vitro measure of whole blood viscosity is of limited clinical utility because it bears little relationship to the actual viscosity within the circulation, but an increase in the viscosity of circulating blood can contribute to morbidity in patients suffering from disorders such as SICKLE CELL ANEMIA and POLYCYTHEMIA.
Endogenous substances, usually proteins, that are involved in the blood coagulation process.
Precursor of plasmin (FIBRINOLYSIN). It is a single-chain beta-globulin of molecular weight 80-90,000 found mostly in association with fibrinogen in plasma; plasminogen activators change it to fibrinolysin. It is used in wound debriding and has been investigated as a thrombolytic agent.
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.
Peptides composed of between two and twelve amino acids.
A high-molecular-weight plasma protein, produced by endothelial cells and megakaryocytes, that is part of the factor VIII/von Willebrand factor complex. The von Willebrand factor has receptors for collagen, platelets, and ristocetin activity as well as the immunologically distinct antigenic determinants. It functions in adhesion of platelets to collagen and hemostatic plug formation. The prolonged bleeding time in VON WILLEBRAND DISEASES is due to the deficiency of this factor.
Heat- and storage-stable plasma protein that is activated by tissue thromboplastin to form factor VIIa in the extrinsic pathway of blood coagulation. The activated form then catalyzes the activation of factor X to factor Xa.
Formation and development of a thrombus or blood clot in the blood vessel.
A plasma protein that circulates in increased amounts during inflammation and after tissue damage.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A congenital bleeding disorder with prolonged bleeding time, absence of aggregation of platelets in response to most agents, especially ADP, and impaired or absent clot retraction. Platelet membranes are deficient in or have a defect in the glycoprotein IIb-IIIa complex (PLATELET GLYCOPROTEIN GPIIB-IIIA COMPLEX).
Agents acting to arrest the flow of blood. Absorbable hemostatics arrest bleeding either by the formation of an artificial clot or by providing a mechanical matrix that facilitates clotting when applied directly to the bleeding surface. These agents function more at the capillary level and are not effective at stemming arterial or venous bleeding under any significant intravascular pressure.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
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 member of the serpin superfamily found in plasma that inhibits the lysis of fibrin clots which are induced by plasminogen activator. It is a glycoprotein, molecular weight approximately 70,000 that migrates in the alpha 2 region in immunoelectrophoresis. It is the principal plasmin inactivator in blood, rapidly forming a very stable complex with plasmin.
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.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Activated form of FACTOR XIII, a transglutaminase, which stabilizes the formation of the fibrin polymer (clot) culminating the blood coagulation cascade.
Measurable and quantifiable biological parameters (e.g., specific enzyme concentration, specific hormone concentration, specific gene phenotype distribution in a population, presence of biological substances) which serve as indices for health- and physiology-related assessments, such as disease risk, psychiatric disorders, environmental exposure and its effects, disease diagnosis, metabolic processes, substance abuse, pregnancy, cell line development, epidemiologic studies, etc.
Glycoproteins found on the surfaces of cells, particularly in fibrillar structures. The proteins are lost or reduced when these cells undergo viral or chemical transformation. They are highly susceptible to proteolysis and are substrates for activated blood coagulation factor VIII. The forms present in plasma are called cold-insoluble globulins.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
The rate dynamics in chemical or physical systems.
A major protein in the BLOOD. It is important in maintaining the colloidal osmotic pressure and transporting large organic molecules.
Proteins that are present in blood serum, including SERUM ALBUMIN; BLOOD COAGULATION FACTORS; and many other types of proteins.
A measurement of the time needed for FIBRINOLYSIS to occur.
The number of PLATELETS per unit volume in a sample of venous BLOOD.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
Disorders caused by abnormalities in platelet count or function.
Adherence of cells to surfaces or to other cells.
Spontaneous or near spontaneous bleeding caused by a defect in clotting mechanisms (BLOOD COAGULATION DISORDERS) or another abnormality causing a structural flaw in the blood vessels (HEMOSTATIC DISORDERS).
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.
An aspect of personal behavior or lifestyle, environmental exposure, or inborn or inherited characteristic, which, on the basis of epidemiologic evidence, is known to be associated with a health-related condition considered important to prevent.
A proteolytic enzyme in the serine protease family found in many tissues which converts PLASMINOGEN to FIBRINOLYSIN. It has fibrin-binding activity and is immunologically different from UROKINASE-TYPE PLASMINOGEN ACTIVATOR. The primary sequence, composed of 527 amino acids, is identical in both the naturally occurring and synthetic proteases.
Chemical analysis based on the phenomenon whereby light, passing through a medium with dispersed particles of a different refractive index from that of the medium, is attenuated in intensity by scattering. In turbidimetry, the intensity of light transmitted through the medium, the unscattered light, is measured. In nephelometry, the intensity of the scattered light is measured, usually, but not necessarily, at right angles to the incident light beam.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.

Evidence suggesting the regulation of a coagulation factor levels in rabbits by a transferable plasma agent. (1/4604)

New Zealand white rabbits were given 30 ml of goat serum intravenously. This procedure resulted in an immediate decrease in platelet count, fibrinogen, and levels of coagulation factors II, V, VII, and X, due to consumption coagulopathy. These factors returned toward baseline levels approximately 12 hr after the injection. Plasma from rabbits who had received goat serum 48 hr previously (donor rabbits) was injected into recipient rabbits. This procedure resulted in a slight rise in the level of coagulation factor II (range, 20%-30%) and a significant rise in factors V (35%-75%), VII (35%-235%), and X (35%-75%) in the recipients. When plasma from control donor rabbits who had not received goat serum was injected into recipients, there was no change in these coagulation factors. It is postulated that the reduction in coagulation factor levels in donor rabbits induces a "coagulopoietin" for each factor or one "coagulopoietin" for all factors which stimulates increased synthesis and/or release of these factors in recipient rabbits.  (+info)

Effect of intravenous dextran 70 and pneumatic leg compression on incidence of postoperative pulmonary embolism. (2/4604)

The incidence of pulmonary embolism and deep vein thrombosis was measured in 50 matched pairs of patients undergoing common surgical procedures with preoperative and postoperative ventilation-perfusion lung scans and the fibrinogen uptake test. One patient in each pair was treated with intravenous dextran 70 and pneumatic leggings. The incidence of pulmonary embolism among the treated patients was significantly reduced from 24% to 8%, but the incidence of deep vein thrombosis was not significantly reduced (34% to 24%).  (+info)

Constitutional, biochemical and lifestyle correlates of fibrinogen and factor VII activity in Polish urban and rural populations. (3/4604)

BACKGROUND: Fibrinogen and factor VII activity are known to be related to atherosclerosis and coronary heart disease, but population differences in clotting factors and modifiable characteristics that influence their levels have not been widely explored. METHODS: This paper examines correlates of plasma fibrinogen concentration and factor VII activity in 2443 men and women aged 35-64 in random samples selected from the residents in two districts in urban Warsaw (618 men and 651 women) and from rural Tarnobrzeg Province (556 men and 618 women) screened in 1987-1988, and assesses which characteristics might explain urban-rural differences. Fibrinogen and factor VII activity were determined using coagulation methods. RESULTS: Fibrinogen was 12.9 mg/dl higher in men and 14.1 mg/dl higher in women in Tarnobrzeg compared to Warsaw. Factor VII activity was higher in Warsaw (9.2% in men and 15.3% in women). After adjustment for selected characteristics, fibrinogen was higher in smokers compared to non-smokers by 28 mg/dl in men and 22 mg/dl in women. In women, a 15 mg/dl increase in HDL-cholesterol was associated with a 10 mg/dl decrease in fibrinogen (P < 0.01). After adjustment for other variables, a higher factor VII activity in Warsaw remained significant (a difference of 9.4% in men and 14.8% in women). Lower fibrinogen in Warsaw remained significant only in women (15.4 mg/dl difference). CONCLUSIONS: The study confirmed that sex, age, BMI, smoking and blood lipids are related to clotting factors. However, with the exception of gender differences and smoking, associations between clotting factors and other variables were small and of questionable practical importance.  (+info)

Improvement of factor VII clotting activity following long-term NCPAP treatment in obstructive sleep apnoea syndrome. (4/4604)

Obstructive sleep apnoea syndrome (OSAS) is a very common disorder. Patients with OSAS are at an increased risk for cardiovascular events. It has also been reported that a 25% rise in factor VII clotting activity (FVIIc) is associated with a 55% increase in ischaemic heart disease death during the first 5 years. We examined the effects of nasal continuous positive airway pressure (NCPAP) treatment on FVIIc in patients with OSAS. FVIIc was investigated prospectively in 15 patients with OSAS before (mean +/- SEM apnoea and hypopnoea index (AHI) 61.5 +/- 4.2 and after (AHI 3.0 +/- 0.9) NCPAP treatment for immediate relief, at 1 month after treatment and at over 6 months. FVIIc levels gradually decreased after NCPAP treatment. After 6 months of NCPAP treatment, FVIIc levels had decreased significantly (before 141.1 +/- 11.7% vs. after 6 months 110.7 +/- 6.2%; p < 0.01). Six of the seven patients whose FVIIc levels were over 140% before the NCPAP treatment had FVIIc levels below 130% after 6 months or 1 year of NCPAP treatment. This decrease in FVIIc after long-term NCPAP treatment could improve mortality in OSAS patients. If patients, especially obese ones, present with high FVIIc of unknown origin, it would be prudent to check for OSAS.  (+info)

Elevated levels of C-reactive protein at discharge in patients with unstable angina predict recurrent instability. (5/4604)

BACKGROUND: In a group of patients admitted for unstable angina, we investigated whether C-reactive protein (CRP) plasma levels remain elevated at discharge and whether persistent elevation is associated with recurrence of instability. METHODS AND RESULTS: We measured plasma levels of CRP, serum amyloid A protein (SAA), fibrinogen, total cholesterol, and Helicobacter pylori and Chlamydia pneumoniae antibody titers in 53 patients admitted to our coronary care unit for Braunwald class IIIB unstable angina. Blood samples were taken on admission, at discharge, and after 3 months. Patients were followed for 1 year. At discharge, CRP was elevated (>3 mg/L) in 49% of patients; of these, 42% had elevated levels on admission and at 3 months. Only 15% of patients with discharge levels of CRP <3 mg/L but 69% of those with elevated CRP (P<0.001) were readmitted because of recurrence of instability or new myocardial infarction. New phases of instability occurred in 13% of patients in the lower tertile of CRP (/=8.7 mg/L, P<0.001). The prognostic value of SAA was similar to that of CRP; that of fibrinogen was not significant. Chlamydia pneumoniae but not Helicobacter pylori antibody titers significantly correlated with CRP plasma levels. CONCLUSIONS: In unstable angina, CRP may remain elevated for at >/=3 months after the waning of symptoms and is associated with recurrent instability. Elevation of acute-phase reactants in unstable angina could represent a hallmark of subclinical persistent instability or of susceptibility to recurrent instability and, at least in some patients, could be related to chronic Chlamydia pneumoniae infection.  (+info)

Association of plasma fibrinogen concentration with vascular access failure in hemodialysis patients. (6/4604)

BACKGROUND: Elevated plasma fibrinogen is an important risk factor for coronary artery disease in the general population and patients with chronic renal failure. High plasma fibrinogen may trigger thrombus formation in arteriovenous fistulas. We performed a prospective, cohort study to evaluate the association of plasma fibrinogen concentration with vascular access failure in patients undergoing long-term haemodialysis. METHODS: Between September 1989 and October 1995, 144 patients underwent a vascular access operation. In March 1997, 102 patients (56 M, 46 F) who had been followed up for more than 18 months (median; 37 months, range; 18-102 months) were included in the study. The median age of the patients was 52 years (range; 19-78 years). In 35 patients, renal disease was secondary to diabetes mellitus. The type of vascular access was a polytetrafluoroethylene (PTFE) graft in 17 patients. Seventy-seven patients received recombinant human erythropoietin (r-HuEPO) therapy during the follow-up period. Plasma fibrinogen, albumin, total cholesterol, hematocrit, platelets and creatinine were measured at the time of operation. Vascular access failure was defined as the occurrence of complications requiring transluminal angioplasty, thrombolytic therapy or surgical repair. RESULTS: Thirty-eight patients had at least one vascular access failure and the incidence was 0.3 (range; 0-2.4) episodes per patient-year. The survival rate of vascular access was 78% (native fistula; 80%, PTFE graft; 71%) after 12 months and 70% (native fistula; 73%, PTFE graft; 51%) after 24 months. Older age, a PTFE graft, r-HuEPO therapy, higher hematocrit, lower albumin and higher fibrinogen levels were significantly associated with vascular access failure, whereas gender, diabetes mellitus, total cholesterol and platelet count were not. Plasma fibrinogen was inversely correlated with albumin (r=-0.38, P=0.001). The cumulative vascular access survival was significantly lower in patients with high plasma fibrinogen levels (> or = 460 mg/dl) compared with patients with low levels (< 460 mg/dl) (P=0.007). Independent risk factors for vascular access failure analysed by Cox's proportional hazards model were older age (RR; 1.36 by 10-year increment), higher fibrinogen level (RR; 1.20 by 100 mg/dl increment), PTFE graft (RR; 2.28) and r-HuEPO therapy (RR; 3.79). CONCLUSION: High plasma fibrinogen level is an independent risk factor for vascular access failure in haemodialysis patients.  (+info)

Effect of prostanoids and their precursors on the aggregation of rainbow trout thrombocytes. (7/4604)

The role of prostanoids and their precursor fatty acids in the aggregatory response of thrombocytes (platelet equivalents of fish) from the rainbow trout, Oncorhynchus mykiss, was studied. Aggregation of these cells was induced by the thromboxane mimetic U-46619 or arachidonic acid (AA) in the presence of human or trout fibrinogen. The production of TXB2/3 by thrombocytes in response to stimulation with AA was inhibited by aspirin, ibuprofen, and indomethacin. However, thrombocyte aggregation in response to AA stimulation was not significantly altered by these agents at the concentrations tested (10-100 microM), with the exception of indomethacin at 20 and 40 microM. Effects on cytosolic calcium concentration have been suggested as an alternative mechanism for the inhibitory action of indomethacin on human platelet aggregation. The present study, however, failed to identify this as a mechanism for the inhibition of U-46619-induced trout thrombocyte aggregation by indomethacin. The polyunsaturated fatty acids docosahexaenoic acid and eicosapentaenoic acid both exhibited an inhibitory effect on U-46619-induced thrombocyte aggregation similar to that observed with mammalian platelets. Unlike the case in mammalian hemostasis, prostacyclin inhibited thrombocyte aggregation only at high concentrations (>5 microM). Prostaglandin E2, however, inhibited thrombocyte aggregation at much lower concentrations (>0.01 microM), suggesting that it may be the major inhibitory eicosanoid in trout.  (+info)

Socioeconomic status and determinants of hemostatic function in healthy women. (8/4604)

Hemostatic factors are reported to be associated with coronary heart disease (CHD). Socioeconomic status (SES) is 1 of the determinants of the hemostatic profile, but the factors underlying this association are not well known. Our aim was to examine determinants of the socioeconomic differences in hemostatic profile. Between 1991 and 1994, we studied 300 healthy women, aged 30 to 65 years, who were representative of women living in the greater Stockholm area. Fibrinogen, factor VII mass concentration (FVII:Ag), activated factor VII (FVIIa), von Willebrand factor (vWF), and plasminogen activator inhibitor-1 (PAI-1) were measured. Educational attainment was used as a measure of SES. Low educational level and an unfavorable hemostatic profile were both associated with older age, unhealthful life style, psychosocial stress, atherogenic biochemical factors, and hypertension. Levels of hemostatic factors increased with lower educational attainment. Independently of age, the differences between the lowest (mandatory) and highest (college/university) education in FVII:Ag levels were 41 microg/L (95% confidence interval [CI], 15 to 66 microg/L, P=0.001), 0.26 g/L (95% CI, 0.10 to 0.42 g/L, P=0.001) in fibrinogen levels, and 0.11 U/mL (95% CI, 0.09 to 0.12 U/mL, P=0.03) in levels of vWF. The corresponding differences in FVIIa and PAI-1 were not statistically significant. With further adjustment for menopausal status, family history of CHD, marital status, psychosocial stress, lifestyle patterns, biochemical factors, and hypertension, statistically significant differences between mandatory and college/university education were observed in FVII:Ag (difference=34 microg/L; 95% CI, 2 to 65 microg/L, P=0.05) but not in fibrinogen (difference=0.03 g/L; 95% CI, -0.13 to 0.19 g/L, P=0.92) or in vWF (difference=0.06 U/mL; 95% CI, -0.10 to 0.22 U/mL, P=0.45). An educational gradient was most consistent and statistically significant for FVII:Ag, fibrinogen, and vWF. Age, psychosocial stress, unhealthful life style, atherogenic biochemical factors, and hypertension mediated the association of low educational level with elevated levels of fibrinogen and vWF. Psychosocial stress and unhealthful life style were the most important contributing factors. There was an independent association between education and FVII:Ag, which could not be explained by any of these factors.  (+info)

Fibrinogen is a soluble protein present in plasma, synthesized by the liver. It plays an essential role in blood coagulation. When an injury occurs, fibrinogen gets converted into insoluble fibrin by the action of thrombin, forming a fibrin clot that helps to stop bleeding from the injured site. Therefore, fibrinogen is crucial for hemostasis, which is the process of stopping bleeding and starting the healing process after an injury.

Afibrinogenemia is a rare genetic disorder characterized by the complete absence or severely decreased levels of fibrinogen, a protein involved in blood clotting. This condition leads to an increased risk of excessive bleeding due to the inability to form proper blood clots. It is caused by mutations in the genes that provide instructions for making the three chains (Aα, Bβ, and γ) that make up the fibrinogen protein. Inheritance is autosomal recessive, meaning an individual must inherit two copies of the defective gene, one from each parent, to have the condition.

Fibrin(ogen) degradation products (FDPs) are a group of proteins that result from the breakdown of fibrinogen and fibrin, which are key components of blood clots. This process occurs during the normal physiological process of fibrinolysis, where clots are dissolved to maintain blood flow.

FDPs can be measured in the blood as a marker for the activation of the coagulation and fibrinolytic systems. Elevated levels of FDPs may indicate the presence of a disorder that causes abnormal clotting or bleeding, such as disseminated intravascular coagulation (DIC), deep vein thrombosis (DVT), pulmonary embolism (PE), or certain types of cancer.

It is important to note that FDPs are not specific to any particular disorder and their measurement should be interpreted in conjunction with other clinical and laboratory findings.

Fibrin is defined as a protein that is formed from fibrinogen during the clotting of blood. It plays an essential role in the formation of blood clots, also known as a clotting or coagulation cascade. When an injury occurs and bleeding starts, fibrin threads form a net-like structure that entraps platelets and red blood cells to create a stable clot, preventing further loss of blood.

The process of forming fibrin from fibrinogen is initiated by thrombin, another protein involved in the coagulation cascade. Thrombin cleaves fibrinogen into fibrin monomers, which then polymerize to form long strands of fibrin. These strands cross-link with each other through a process catalyzed by factor XIIIa, forming a stable clot that protects the wound and promotes healing.

It is important to note that abnormalities in fibrin formation or breakdown can lead to bleeding disorders or thrombotic conditions, respectively. Proper regulation of fibrin production and degradation is crucial for maintaining healthy hemostasis and preventing excessive clotting or bleeding.

Fibrinopeptide B is a small protein molecule that is cleaved and released from the larger fibrinogen protein during the blood clotting process, also known as coagulation. Fibrinogen is converted to fibrin by the action of thrombin, an enzyme that activates the coagulation cascade. Thrombin cuts specific peptide bonds in fibrinogen, releasing fibrinopeptides A and B from the resulting fibrin monomers.

The release of fibrinopeptide B is a critical step in the formation of a stable blood clot because it allows for the exposure of binding sites on the fibrin molecules that facilitate their polymerization into an insoluble network, trapping platelets and other components to form a clot. The measurement of fibrinopeptide B levels can be used as a marker for thrombin activity and fibrin formation in various clinical settings, such as monitoring the effectiveness of anticoagulant therapy or diagnosing conditions associated with abnormal blood clotting.

Fibrinopeptide A is a small protein molecule that is cleaved and released from the larger fibrinogen protein during the blood clotting process. Specifically, it is removed by the enzyme thrombin as part of the conversion of fibrinogen to fibrin, which is the main structural component of a blood clot. The measurement of Fibrinopeptide A in the blood can be used as a marker for ongoing thrombin activation and fibrin formation, which are key events in coagulation and hemostasis. Increased levels of Fibrinopeptide A may indicate abnormal or excessive blood clotting, such as in disseminated intravascular coagulation (DIC) or deep vein thrombosis (DVT).

Blood platelets, also known as thrombocytes, are small, colorless cell fragments in our blood that play an essential role in normal blood clotting. They are formed in the bone marrow from large cells called megakaryocytes and circulate in the blood in an inactive state until they are needed to help stop bleeding. When a blood vessel is damaged, platelets become activated and change shape, releasing chemicals that attract more platelets to the site of injury. These activated platelets then stick together to form a plug, or clot, that seals the wound and prevents further blood loss. In addition to their role in clotting, platelets also help to promote healing by releasing growth factors that stimulate the growth of new tissue.

Platelet membrane glycoproteins are specialized proteins found on the surface of platelets, which are small blood cells responsible for clotting. These glycoproteins play crucial roles in various processes related to hemostasis and thrombosis, including platelet adhesion, activation, and aggregation.

There are several key platelet membrane glycoproteins, such as:

1. Glycoprotein (GP) Ia/IIa (also known as integrin α2β1): This glycoprotein mediates the binding of platelets to collagen fibers in the extracellular matrix, facilitating platelet adhesion and activation.
2. GP IIb/IIIa (also known as integrin αIIbβ3): This is the most abundant glycoprotein on the platelet surface and functions as a receptor for fibrinogen, von Willebrand factor, and other adhesive proteins. Upon activation, GP IIb/IIIa undergoes conformational changes that enable it to bind these ligands, leading to platelet aggregation and clot formation.
3. GPIb-IX-V: This glycoprotein complex is involved in the initial tethering and adhesion of platelets to von Willebrand factor (vWF) in damaged blood vessels. It consists of four subunits: GPIbα, GPIbβ, GPIX, and GPV.
4. GPVI: This glycoprotein is essential for platelet activation upon contact with collagen. It associates with the Fc receptor γ-chain (FcRγ) to form a signaling complex that triggers intracellular signaling pathways, leading to platelet activation and aggregation.

Abnormalities in these platelet membrane glycoproteins can lead to bleeding disorders or thrombotic conditions. For example, mutations in GPIIb/IIIa can result in Glanzmann's thrombasthenia, a severe bleeding disorder characterized by impaired platelet aggregation. On the other hand, increased expression or activation of these glycoproteins may contribute to the development of arterial thrombosis and cardiovascular diseases.

Platelet aggregation is the clumping together of platelets (thrombocytes) in the blood, which is an essential step in the process of hemostasis (the stopping of bleeding) after injury to a blood vessel. When the inner lining of a blood vessel is damaged, exposure of subendothelial collagen and tissue factor triggers platelet activation. Activated platelets change shape, become sticky, and release the contents of their granules, which include ADP (adenosine diphosphate).

ADP then acts as a chemical mediator to attract and bind additional platelets to the site of injury, leading to platelet aggregation. This forms a plug that seals the damaged vessel and prevents further blood loss. Platelet aggregation is also a crucial component in the formation of blood clots (thrombosis) within blood vessels, which can have pathological consequences such as heart attacks and strokes if they obstruct blood flow to vital organs.

Blood coagulation, also known as blood clotting, is a complex process that occurs in the body to prevent excessive bleeding when a blood vessel is damaged. This process involves several different proteins and chemical reactions that ultimately lead to the formation of a clot.

The coagulation cascade is initiated when blood comes into contact with tissue factor, which is exposed after damage to the blood vessel wall. This triggers a series of enzymatic reactions that activate clotting factors, leading to the formation of a fibrin clot. Fibrin is a protein that forms a mesh-like structure that traps platelets and red blood cells to form a stable clot.

Once the bleeding has stopped, the coagulation process is regulated and inhibited to prevent excessive clotting. The fibrinolytic system degrades the clot over time, allowing for the restoration of normal blood flow.

Abnormalities in the blood coagulation process can lead to bleeding disorders or thrombotic disorders such as deep vein thrombosis and pulmonary embolism.

Thrombin is a serine protease enzyme that plays a crucial role in the coagulation cascade, which is a complex series of biochemical reactions that leads to the formation of a blood clot (thrombus) to prevent excessive bleeding during an injury. Thrombin is formed from its precursor protein, prothrombin, through a process called activation, which involves cleavage by another enzyme called factor Xa.

Once activated, thrombin converts fibrinogen, a soluble plasma protein, into fibrin, an insoluble protein that forms the structural framework of a blood clot. Thrombin also activates other components of the coagulation cascade, such as factor XIII, which crosslinks and stabilizes the fibrin network, and platelets, which contribute to the formation and growth of the clot.

Thrombin has several regulatory mechanisms that control its activity, including feedback inhibition by antithrombin III, a plasma protein that inactivates thrombin and other serine proteases, and tissue factor pathway inhibitor (TFPI), which inhibits the activation of factor Xa, thereby preventing further thrombin formation.

Overall, thrombin is an essential enzyme in hemostasis, the process that maintains the balance between bleeding and clotting in the body. However, excessive or uncontrolled thrombin activity can lead to pathological conditions such as thrombosis, atherosclerosis, and disseminated intravascular coagulation (DIC).

Thrombin time (TT) is a medical laboratory test that measures the time it takes for a clot to form after thrombin, an enzyme that converts fibrinogen to fibrin in the final step of the coagulation cascade, is added to a plasma sample. This test is used to evaluate the efficiency of the conversion of fibrinogen to fibrin and can be used to detect the presence of abnormalities in the coagulation system, such as the presence of heparin or dysfibrinogenemia. Increased thrombin time may indicate the presence of a systemic anticoagulant or a deficiency in fibrinogen.

Fibrinogen receptors are specialized proteins found on the surface of certain cells, particularly platelets and some types of immune cells. These receptors bind to fibrinogen, a protein involved in blood clotting, under specific conditions such as injury or inflammation. The binding of fibrinogen to its receptors plays a crucial role in the process of platelet activation, aggregation, and clot formation, which are essential for hemostasis (the stoppage of bleeding) after injury. Disorders affecting fibrinogen receptor function can lead to abnormal bleeding or clotting tendencies.

The platelet glycoprotein GPIIb-IIIa complex, also known as integrin αIIbβ3 or CD41/CD61, is a heterodimeric transmembrane receptor found on the surface of platelets and megakaryocytes. It plays a crucial role in platelet aggregation and thrombus formation during hemostasis and pathological conditions such as arterial thrombosis.

The GPIIb-IIIa complex is composed of two non-covalently associated subunits, GPIIb (αIIb or CD41) and IIIa (β3 or CD61). Upon platelet activation by various agonists like ADP, thrombin, or collagen, the GPIIb-IIIa complex undergoes a conformational change that allows it to bind fibrinogen, von Willebrand factor, and other adhesive proteins. This binding event leads to platelet aggregation and the formation of a hemostatic plug or pathological thrombus.

Inhibition of the GPIIb-IIIa complex has been a target for antiplatelet therapy in the prevention and treatment of arterial thrombosis, such as myocardial infarction and stroke. Several pharmacological agents, including monoclonal antibodies and small molecule antagonists, have been developed to block this complex and reduce platelet aggregation.

Blood coagulation disorders, also known as bleeding disorders or clotting disorders, refer to a group of medical conditions that affect the body's ability to form blood clots properly. Normally, when a blood vessel is injured, the body's coagulation system works to form a clot to stop the bleeding and promote healing.

In blood coagulation disorders, there can be either an increased tendency to bleed due to problems with the formation of clots (hemorrhagic disorder), or an increased tendency for clots to form inappropriately even without injury, leading to blockages in the blood vessels (thrombotic disorder).

Examples of hemorrhagic disorders include:

1. Hemophilia - a genetic disorder that affects the ability to form clots due to deficiencies in clotting factors VIII or IX.
2. Von Willebrand disease - another genetic disorder caused by a deficiency or abnormality of the von Willebrand factor, which helps platelets stick together to form a clot.
3. Liver diseases - can lead to decreased production of coagulation factors, increasing the risk of bleeding.
4. Disseminated intravascular coagulation (DIC) - a serious condition where clotting and bleeding occur simultaneously due to widespread activation of the coagulation system.

Examples of thrombotic disorders include:

1. Factor V Leiden mutation - a genetic disorder that increases the risk of inappropriate blood clot formation.
2. Antithrombin III deficiency - a genetic disorder that impairs the body's ability to break down clots, increasing the risk of thrombosis.
3. Protein C or S deficiencies - genetic disorders that lead to an increased risk of thrombosis due to impaired regulation of the coagulation system.
4. Antiphospholipid syndrome (APS) - an autoimmune disorder where the body produces antibodies against its own clotting factors, increasing the risk of thrombosis.

Treatment for blood coagulation disorders depends on the specific diagnosis and may include medications to manage bleeding or prevent clots, as well as lifestyle changes and monitoring to reduce the risk of complications.

Fibrinolysis is the natural process in the body that leads to the dissolution of blood clots. It is a vital part of hemostasis, the process that regulates bleeding and wound healing. Fibrinolysis occurs when plasminogen activators convert plasminogen to plasmin, an enzyme that breaks down fibrin, the insoluble protein mesh that forms the structure of a blood clot. This process helps to prevent excessive clotting and maintains the fluidity of the blood. In medical settings, fibrinolysis can also refer to the therapeutic use of drugs that stimulate this process to dissolve unwanted or harmful blood clots, such as those that cause deep vein thrombosis or pulmonary embolism.

Blood coagulation tests, also known as coagulation studies or clotting tests, are a series of medical tests used to evaluate the blood's ability to clot. These tests measure the functioning of various clotting factors and regulatory proteins involved in the coagulation cascade, which is a complex process that leads to the formation of a blood clot to prevent excessive bleeding.

The most commonly performed coagulation tests include:

1. Prothrombin Time (PT): Measures the time it takes for a sample of plasma to clot after the addition of calcium and tissue factor, which activates the extrinsic pathway of coagulation. The PT is reported in seconds and can be converted to an International Normalized Ratio (INR) to monitor anticoagulant therapy.
2. Activated Partial Thromboplastin Time (aPTT): Measures the time it takes for a sample of plasma to clot after the addition of calcium, phospholipid, and a contact activator, which activates the intrinsic pathway of coagulation. The aPTT is reported in seconds and is used to monitor heparin therapy.
3. Thrombin Time (TT): Measures the time it takes for a sample of plasma to clot after the addition of thrombin, which directly converts fibrinogen to fibrin. The TT is reported in seconds and can be used to detect the presence of fibrin degradation products or abnormalities in fibrinogen function.
4. Fibrinogen Level: Measures the amount of fibrinogen, a protein involved in clot formation, present in the blood. The level is reported in grams per liter (g/L) and can be used to assess bleeding risk or the effectiveness of fibrinogen replacement therapy.
5. D-dimer Level: Measures the amount of D-dimer, a protein fragment produced during the breakdown of a blood clot, present in the blood. The level is reported in micrograms per milliliter (µg/mL) and can be used to diagnose or exclude venous thromboembolism (VTE), such as deep vein thrombosis (DVT) or pulmonary embolism (PE).

These tests are important for the diagnosis, management, and monitoring of various bleeding and clotting disorders. They can help identify the underlying cause of abnormal bleeding or clotting, guide appropriate treatment decisions, and monitor the effectiveness of therapy. It is essential to interpret these test results in conjunction with a patient's clinical presentation and medical history.

Fibrinolysin is defined as a proteolytic enzyme that dissolves or breaks down fibrin, a protein involved in the clotting of blood. This enzyme is produced by certain cells, such as endothelial cells that line the interior surface of blood vessels, and is an important component of the body's natural mechanism for preventing excessive blood clotting and maintaining blood flow.

Fibrinolysin works by cleaving specific bonds in the fibrin molecule, converting it into soluble degradation products that can be safely removed from the body. This process is known as fibrinolysis, and it helps to maintain the balance between clotting and bleeding in the body.

In medical contexts, fibrinolysin may be used as a therapeutic agent to dissolve blood clots that have formed in the blood vessels, such as those that can occur in deep vein thrombosis or pulmonary embolism. It is often administered in combination with other medications that help to enhance its activity and specificity for fibrin.

Hemostasis is the physiological process that occurs to stop bleeding (bleeding control) when a blood vessel is damaged. This involves the interaction of platelets, vasoconstriction, and blood clotting factors leading to the formation of a clot. The ultimate goal of hemostasis is to maintain the integrity of the vascular system while preventing excessive blood loss.

Platelet adhesiveness refers to the ability of platelets, which are small blood cells that help your body form clots to prevent excessive bleeding, to stick to other cells or surfaces. This process is crucial in hemostasis, the process of stopping bleeding after injury to a blood vessel.

When the endothelium (the lining of blood vessels) is damaged, subendothelial structures are exposed, which can trigger platelet adhesion. Platelets then change shape and release chemical signals that cause other platelets to clump together, forming a platelet plug. This plug helps to seal the damaged vessel and prevent further bleeding.

Platelet adhesiveness is influenced by several factors, including the presence of von Willebrand factor (vWF), a protein in the blood that helps platelets bind to damaged vessels, and the expression of glycoprotein receptors on the surface of platelets. Abnormalities in platelet adhesiveness can lead to bleeding disorders or thrombotic conditions.

Factor XIII, also known as fibrin stabilizing factor, is a protein involved in the clotting process of blood. It is a transglutaminase enzyme that cross-links fibrin molecules to form a stable clot. Factor XIII becomes activated during the coagulation cascade, and its activity helps strengthen the clot and protect it from premature degradation by proteolytic enzymes. A deficiency in Factor XIII can lead to a bleeding disorder characterized by prolonged bleeding after injury or surgery.

Ancrod is a thrombin-like enzyme that is derived from the venom of the Malayan pit viper (Calloselasma rhodostoma). It has been used in clinical settings as an anticoagulant and for the treatment of cerebral thrombosis, although its use is not widespread due to the availability of other effective treatments and potential side effects.

Ancrod works by selectively cleaving fibrinogen, a protein involved in blood clotting, into fibrin degradation products. This action reduces the formation of blood clots and increases the bleeding time, making it useful as an anticoagulant. However, ancrod also has potential side effects such as bleeding complications, allergic reactions, and anaphylaxis, which limit its use in clinical practice.

It is important to note that the use of ancrod and other snake venom-derived enzymes for medical purposes should only be done under the supervision of a qualified healthcare professional, and with careful monitoring of potential side effects.

Clot retraction is the process that occurs during blood clotting where the platelets in the blood contract and pull together the edges of the clot, causing it to shrink. This process helps to seal off injured blood vessels and prevent further bleeding. Clot retraction also aids in the healing process by helping to remove damaged tissue and debris from the wound site. The proteins in the blood, called fibrin, form a mesh that traps red and white blood cells and platelets, creating a clot. As the platelets contract, they pull on the fibrin mesh, causing it to tighten and the clot to shrink. This process is an important part of the body's natural healing response to injury.

Batroxobin is a serine protease enzyme that is isolated from the venom of Bothrops atrox, also known as the South American fer-de-lance snake. It has thrombin-like activity and can induce fibrinogen to form fibrin, which is an important step in blood clotting. Batroxobin is used medically as a defibrinating agent to treat conditions such as snake envenomation, cerebral infarction, and arterial thrombosis. It may also be used for research purposes to study hemostasis and coagulation.

Platelet activation is the process by which platelets (also known as thrombocytes) become biologically active and change from their inactive discoid shape to a spherical shape with pseudopodia, resulting in the release of chemical mediators that are involved in hemostasis and thrombosis. This process is initiated by various stimuli such as exposure to subendothelial collagen, von Willebrand factor, or thrombin during vascular injury, leading to platelet aggregation and the formation of a platelet plug to stop bleeding. Platelet activation also plays a role in inflammation, immune response, and wound healing.

Prothrombin time (PT) is a medical laboratory test that measures the time it takes for blood to clot. It's often used to evaluate the functioning of the extrinsic and common pathways of the coagulation system, which is responsible for blood clotting. Specifically, PT measures how long it takes for prothrombin (a protein produced by the liver) to be converted into thrombin, an enzyme that converts fibrinogen into fibrin and helps form a clot.

Prolonged PT may indicate a bleeding disorder or a deficiency in coagulation factors, such as vitamin K deficiency or the use of anticoagulant medications like warfarin. It's important to note that PT is often reported with an international normalized ratio (INR), which allows for standardization and comparison of results across different laboratories and reagent types.

Adenosine diphosphate (ADP) is a chemical compound that plays a crucial role in energy transfer within cells. It is a nucleotide, which consists of a adenosine molecule (a sugar molecule called ribose attached to a nitrogenous base called adenine) and two phosphate groups.

In the cell, ADP functions as an intermediate in the conversion of energy from one form to another. When a high-energy phosphate bond in ADP is broken, energy is released and ADP is converted to adenosine triphosphate (ATP), which serves as the main energy currency of the cell. Conversely, when ATP donates a phosphate group to another molecule, it is converted back to ADP, releasing energy for the cell to use.

ADP also plays a role in blood clotting and other physiological processes. In the coagulation cascade, ADP released from damaged red blood cells can help activate platelets and initiate the formation of a blood clot.

Blood viscosity is a measure of the thickness or flow resistance of blood. It is defined as the ratio of shear stress to shear rate within the flowing blood, which reflects the internal friction or resistance to flow. Blood viscosity is primarily determined by the concentration and size of red blood cells (hematocrit), plasma proteins, and other blood constituents. An increase in any of these components can raise blood viscosity, leading to impaired blood flow, reduced oxygen delivery to tissues, and potential cardiovascular complications if not managed appropriately.

Blood coagulation factors, also known as clotting factors, are a group of proteins that play a crucial role in the blood coagulation process. They are essential for maintaining hemostasis, which is the body's ability to stop bleeding after injury.

There are 13 known blood coagulation factors, and they are designated by Roman numerals I through XIII. These factors are produced in the liver and are normally present in an inactive form in the blood. When there is an injury to a blood vessel, the coagulation process is initiated, leading to the activation of these factors in a specific order.

The coagulation cascade involves two pathways: the intrinsic and extrinsic pathways. The intrinsic pathway is activated when there is damage to the blood vessel itself, while the extrinsic pathway is activated by tissue factor released from damaged tissues. Both pathways converge at the common pathway, leading to the formation of a fibrin clot.

Blood coagulation factors work together in a complex series of reactions that involve activation, binding, and proteolysis. When one factor is activated, it activates the next factor in the cascade, and so on. This process continues until a stable fibrin clot is formed.

Deficiencies or abnormalities in blood coagulation factors can lead to bleeding disorders such as hemophilia or thrombosis. Hemophilia is a genetic disorder that affects one or more of the coagulation factors, leading to excessive bleeding and difficulty forming clots. Thrombosis, on the other hand, occurs when there is an abnormal formation of blood clots in the blood vessels, which can lead to serious complications such as stroke or pulmonary embolism.

Plasminogen is a glycoprotein that is present in human plasma, and it is the inactive precursor of the enzyme plasmin. Plasmin is a serine protease that plays a crucial role in the dissolution of blood clots by degrading fibrin, one of the major components of a blood clot.

Plasminogen can be activated to form plasmin through the action of various activators, such as tissue plasminogen activator (tPA) and urokinase-type plasminogen activator (uPA). Once activated, plasmin can break down fibrin and other proteins, helping to prevent excessive clotting and promoting the normal turnover of extracellular matrix components.

Abnormalities in plasminogen activation have been implicated in various diseases, including thrombosis, fibrosis, and cancer. Therefore, understanding the regulation and function of plasminogen is important for developing therapies to treat these conditions.

Disseminated Intravascular Coagulation (DIC) is a complex medical condition characterized by the abnormal activation of the coagulation cascade, leading to the formation of blood clots in small blood vessels throughout the body. This process can result in the consumption of clotting factors and platelets, which can then lead to bleeding complications. DIC can be caused by a variety of underlying conditions, including sepsis, trauma, cancer, and obstetric emergencies.

The term "disseminated" refers to the widespread nature of the clotting activation, while "intravascular" indicates that the clotting is occurring within the blood vessels. The condition can manifest as both bleeding and clotting complications, which can make it challenging to diagnose and manage.

The diagnosis of DIC typically involves laboratory tests that evaluate coagulation factors, platelet count, fibrin degradation products, and other markers of coagulation activation. Treatment is focused on addressing the underlying cause of the condition while also managing any bleeding or clotting complications that may arise.

Oligopeptides are defined in medicine and biochemistry as short chains of amino acids, typically containing fewer than 20 amino acid residues. These small peptides are important components in various biological processes, such as serving as signaling molecules, enzyme inhibitors, or structural elements in some proteins. They can be found naturally in foods and may also be synthesized for use in medical research and therapeutic applications.

Von Willebrand factor (vWF) is a large multimeric glycoprotein that plays a crucial role in hemostasis, the process which leads to the cessation of bleeding and the formation of a blood clot. It was named after Erik Adolf von Willebrand, a Finnish physician who first described the disorder associated with its deficiency, known as von Willebrand disease (vWD).

The primary functions of vWF include:

1. Platelet adhesion and aggregation: vWF mediates the initial attachment of platelets to damaged blood vessel walls by binding to exposed collagen fibers and then interacting with glycoprotein Ib (GPIb) receptors on the surface of platelets, facilitating platelet adhesion. Subsequently, vWF also promotes platelet-platelet interactions (aggregation) through its interaction with platelet glycoprotein IIb/IIIa (GPIIb/IIIa) receptors under high shear stress conditions found in areas of turbulent blood flow, such as arterioles and the capillary bed.

2. Transport and stabilization of coagulation factor VIII: vWF serves as a carrier protein for coagulation factor VIII (FVIII), protecting it from proteolytic degradation and maintaining its stability in circulation. This interaction between vWF and FVIII is essential for the proper functioning of the coagulation cascade, particularly in the context of vWD, where impaired FVIII function can lead to bleeding disorders.

3. Wound healing: vWF contributes to wound healing by promoting platelet adhesion and aggregation at the site of injury, which facilitates the formation of a provisional fibrin-based clot that serves as a scaffold for tissue repair and regeneration.

In summary, von Willebrand factor is a vital hemostatic protein involved in platelet adhesion, aggregation, coagulation factor VIII stabilization, and wound healing. Deficiencies or dysfunctions in vWF can lead to bleeding disorders such as von Willebrand disease.

Factor VII, also known as proconvertin, is a protein involved in the coagulation cascade, which is a series of chemical reactions that leads to the formation of a blood clot. Factor VII is synthesized in the liver and is activated when it comes into contact with tissue factor, which is exposed when blood vessels are damaged. Activated Factor VII then activates Factor X, leading to the formation of thrombin and ultimately a fibrin clot.

Inherited deficiencies or dysfunctions of Factor VII can lead to an increased risk of bleeding, while elevated levels of Factor VII have been associated with an increased risk of thrombosis (blood clots).

Thrombosis is the formation of a blood clot (thrombus) inside a blood vessel, obstructing the flow of blood through the circulatory system. When a clot forms in an artery, it can cut off the supply of oxygen and nutrients to the tissues served by that artery, leading to damage or tissue death. If a thrombus forms in the heart, it can cause a heart attack. If a thrombus breaks off and travels through the bloodstream, it can lodge in a smaller vessel, causing blockage and potentially leading to damage in the organ that the vessel supplies. This is known as an embolism.

Thrombosis can occur due to various factors such as injury to the blood vessel wall, abnormalities in blood flow, or changes in the composition of the blood. Certain medical conditions, medications, and lifestyle factors can increase the risk of thrombosis. Treatment typically involves anticoagulant or thrombolytic therapy to dissolve or prevent further growth of the clot, as well as addressing any underlying causes.

C-reactive protein (CRP) is a protein produced by the liver in response to inflammation or infection in the body. It is named after its ability to bind to the C-polysaccharide of pneumococcus, a type of bacteria. CRP levels can be measured with a simple blood test and are often used as a marker of inflammation or infection. Elevated CRP levels may indicate a variety of conditions, including infections, tissue damage, and chronic diseases such as rheumatoid arthritis and cancer. However, it is important to note that CRP is not specific to any particular condition, so additional tests are usually needed to make a definitive diagnosis.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Thrombasthenia is a rare bleeding disorder that is inherited and caused by a deficiency or dysfunction of the platelet glycoprotein IIb/IIIa complex. This complex plays a crucial role in platelet aggregation, which is necessary for blood clotting. When it's defective or absent, platelets are unable to aggregate properly, leading to prolonged bleeding times and symptoms such as easy bruising, nosebleeds, and excessive bleeding following injury or surgery. There are two main types of thrombasthenia: Glanzmann's thrombasthenia and pseudo-thrombasthenia.

Hemostatics are substances or agents that promote bleeding cessation or prevent the spread of bleeding. They can act in various ways, such as by stimulating the body's natural clotting mechanisms, constricting blood vessels to reduce blood flow, or forming a physical barrier to block the bleeding site.

Hemostatics are often used in medical settings to manage wounds, injuries, and surgical procedures. They can be applied directly to the wound as a powder, paste, or gauze, or they can be administered systemically through intravenous injection. Examples of hemostatic agents include fibrin sealants, collagen-based products, thrombin, and oxidized regenerated cellulose.

It's important to note that while hemostatics can be effective in controlling bleeding, they should be used with caution and only under the guidance of a healthcare professional. Inappropriate use or overuse of hemostatic agents can lead to complications such as excessive clotting, thrombosis, or tissue damage.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Partial Thromboplastin Time (PTT) is a medical laboratory test that measures the time it takes for blood to clot. It's more specifically a measure of the intrinsic and common pathways of the coagulation cascade, which are the series of chemical reactions that lead to the formation of a clot.

The test involves adding a partial thromboplastin reagent (an activator of the intrinsic pathway) and calcium to plasma, and then measuring the time it takes for a fibrin clot to form. This is compared to a control sample, and the ratio of the two times is calculated.

The PTT test is often used to help diagnose bleeding disorders or abnormal blood clotting, such as hemophilia or disseminated intravascular coagulation (DIC). It can also be used to monitor the effectiveness of anticoagulant therapy, such as heparin. Prolonged PTT results may indicate a bleeding disorder or an increased risk of bleeding, while shortened PTT results may indicate a hypercoagulable state and an increased risk of thrombosis.

Alpha-2-antiplasmin (α2AP) is a protein found in the blood plasma that inhibits fibrinolysis, the process by which blood clots are broken down. It does this by irreversibly binding to and inhibiting plasmin, an enzyme that degrades fibrin clots.

Alpha-2-antiplasmin is one of the most important regulators of fibrinolysis, helping to maintain a balance between clot formation and breakdown. Deficiencies or dysfunction in alpha-2-antiplasmin can lead to an increased risk of bleeding due to uncontrolled plasmin activity.

Antithrombin III is a protein that inhibits the formation of blood clots (thrombi) in the body. It does this by inactivating several enzymes involved in coagulation, including thrombin and factor Xa. Antithrombin III is produced naturally by the liver and is also available as a medication for the prevention and treatment of thromboembolic disorders, such as deep vein thrombosis and pulmonary embolism. It works by binding to and neutralizing excess clotting factors in the bloodstream, thereby reducing the risk of clot formation.

A peptide fragment is a short chain of amino acids that is derived from a larger peptide or protein through various biological or chemical processes. These fragments can result from the natural breakdown of proteins in the body during regular physiological processes, such as digestion, or they can be produced experimentally in a laboratory setting for research or therapeutic purposes.

Peptide fragments are often used in research to map the structure and function of larger peptides and proteins, as well as to study their interactions with other molecules. In some cases, peptide fragments may also have biological activity of their own and can be developed into drugs or diagnostic tools. For example, certain peptide fragments derived from hormones or neurotransmitters may bind to receptors in the body and mimic or block the effects of the full-length molecule.

Factor XIIIa is a protein involved in the blood clotting process. It is a activated form of Factor XIII, which is a protransglutaminase enzyme that plays a role in stabilizing blood clots. Factor XIIIa cross-links fibrin molecules in the clot to form a more stable and insoluble clot. This action helps prevent further bleeding from the site of injury.

Factor XIIIa is formed when thrombin, another protein involved in blood clotting, cleaves and activates Factor XIII. Once activated, Factor XIIIa catalyzes the formation of covalent bonds between fibrin molecules, creating a mesh-like structure that strengthens the clot.

Deficiencies or dysfunctions in Factor XIIIa can lead to bleeding disorders, including factor XIII deficiency, which is a rare but serious condition characterized by prolonged bleeding and an increased risk of spontaneous hemorrhage.

A biological marker, often referred to as a biomarker, is a measurable indicator that reflects the presence or severity of a disease state, or a response to a therapeutic intervention. Biomarkers can be found in various materials such as blood, tissues, or bodily fluids, and they can take many forms, including molecular, histologic, radiographic, or physiological measurements.

In the context of medical research and clinical practice, biomarkers are used for a variety of purposes, such as:

1. Diagnosis: Biomarkers can help diagnose a disease by indicating the presence or absence of a particular condition. For example, prostate-specific antigen (PSA) is a biomarker used to detect prostate cancer.
2. Monitoring: Biomarkers can be used to monitor the progression or regression of a disease over time. For instance, hemoglobin A1c (HbA1c) levels are monitored in diabetes patients to assess long-term blood glucose control.
3. Predicting: Biomarkers can help predict the likelihood of developing a particular disease or the risk of a negative outcome. For example, the presence of certain genetic mutations can indicate an increased risk for breast cancer.
4. Response to treatment: Biomarkers can be used to evaluate the effectiveness of a specific treatment by measuring changes in the biomarker levels before and after the intervention. This is particularly useful in personalized medicine, where treatments are tailored to individual patients based on their unique biomarker profiles.

It's important to note that for a biomarker to be considered clinically valid and useful, it must undergo rigorous validation through well-designed studies, including demonstrating sensitivity, specificity, reproducibility, and clinical relevance.

Fibronectin is a high molecular weight glycoprotein that is found in many tissues and body fluids, including plasma, connective tissue, and the extracellular matrix. It is composed of two similar subunits that are held together by disulfide bonds. Fibronectin plays an important role in cell adhesion, migration, and differentiation by binding to various cell surface receptors, such as integrins, and other extracellular matrix components, such as collagen and heparan sulfate proteoglycans.

Fibronectin has several isoforms that are produced by alternative splicing of a single gene transcript. These isoforms differ in their biological activities and can be found in different tissues and developmental stages. Fibronectin is involved in various physiological processes, such as wound healing, tissue repair, and embryonic development, and has been implicated in several pathological conditions, including fibrosis, tumor metastasis, and thrombosis.

Electrophoresis, polyacrylamide gel (EPG) is a laboratory technique used to separate and analyze complex mixtures of proteins or nucleic acids (DNA or RNA) based on their size and electrical charge. This technique utilizes a matrix made of cross-linked polyacrylamide, a type of gel, which provides a stable and uniform environment for the separation of molecules.

In this process:

1. The polyacrylamide gel is prepared by mixing acrylamide monomers with a cross-linking agent (bis-acrylamide) and a catalyst (ammonium persulfate) in the presence of a buffer solution.
2. The gel is then poured into a mold and allowed to polymerize, forming a solid matrix with uniform pore sizes that depend on the concentration of acrylamide used. Higher concentrations result in smaller pores, providing better resolution for separating smaller molecules.
3. Once the gel has set, it is placed in an electrophoresis apparatus containing a buffer solution. Samples containing the mixture of proteins or nucleic acids are loaded into wells on the top of the gel.
4. An electric field is applied across the gel, causing the negatively charged molecules to migrate towards the positive electrode (anode) while positively charged molecules move toward the negative electrode (cathode). The rate of migration depends on the size, charge, and shape of the molecules.
5. Smaller molecules move faster through the gel matrix and will migrate farther from the origin compared to larger molecules, resulting in separation based on size. Proteins and nucleic acids can be selectively stained after electrophoresis to visualize the separated bands.

EPG is widely used in various research fields, including molecular biology, genetics, proteomics, and forensic science, for applications such as protein characterization, DNA fragment analysis, cloning, mutation detection, and quality control of nucleic acid or protein samples.

In the context of medicine and pharmacology, "kinetics" refers to the study of how a drug moves throughout the body, including its absorption, distribution, metabolism, and excretion (often abbreviated as ADME). This field is called "pharmacokinetics."

1. Absorption: This is the process of a drug moving from its site of administration into the bloodstream. Factors such as the route of administration (e.g., oral, intravenous, etc.), formulation, and individual physiological differences can affect absorption.

2. Distribution: Once a drug is in the bloodstream, it gets distributed throughout the body to various tissues and organs. This process is influenced by factors like blood flow, protein binding, and lipid solubility of the drug.

3. Metabolism: Drugs are often chemically modified in the body, typically in the liver, through processes known as metabolism. These changes can lead to the formation of active or inactive metabolites, which may then be further distributed, excreted, or undergo additional metabolic transformations.

4. Excretion: This is the process by which drugs and their metabolites are eliminated from the body, primarily through the kidneys (urine) and the liver (bile).

Understanding the kinetics of a drug is crucial for determining its optimal dosing regimen, potential interactions with other medications or foods, and any necessary adjustments for special populations like pediatric or geriatric patients, or those with impaired renal or hepatic function.

Serum albumin is the most abundant protein in human blood plasma, synthesized by the liver. It plays a crucial role in maintaining the oncotic pressure or colloid osmotic pressure of blood, which helps to regulate the fluid balance between the intravascular and extravascular spaces.

Serum albumin has a molecular weight of around 66 kDa and is composed of a single polypeptide chain. It contains several binding sites for various endogenous and exogenous substances, such as bilirubin, fatty acids, hormones, and drugs, facilitating their transport throughout the body. Additionally, albumin possesses antioxidant properties, protecting against oxidative damage.

Albumin levels in the blood are often used as a clinical indicator of liver function, nutritional status, and overall health. Low serum albumin levels may suggest liver disease, malnutrition, inflammation, or kidney dysfunction.

Blood proteins, also known as serum proteins, are a group of complex molecules present in the blood that are essential for various physiological functions. These proteins include albumin, globulins (alpha, beta, and gamma), and fibrinogen. They play crucial roles in maintaining oncotic pressure, transporting hormones, enzymes, vitamins, and minerals, providing immune defense, and contributing to blood clotting.

Albumin is the most abundant protein in the blood, accounting for about 60% of the total protein mass. It functions as a transporter of various substances, such as hormones, fatty acids, and drugs, and helps maintain oncotic pressure, which is essential for fluid balance between the blood vessels and surrounding tissues.

Globulins are divided into three main categories: alpha, beta, and gamma globulins. Alpha and beta globulins consist of transport proteins like lipoproteins, hormone-binding proteins, and enzymes. Gamma globulins, also known as immunoglobulins or antibodies, are essential for the immune system's defense against pathogens.

Fibrinogen is a protein involved in blood clotting. When an injury occurs, fibrinogen is converted into fibrin, which forms a mesh to trap platelets and form a clot, preventing excessive bleeding.

Abnormal levels of these proteins can indicate various medical conditions, such as liver or kidney disease, malnutrition, infections, inflammation, or autoimmune disorders. Blood protein levels are typically measured through laboratory tests like serum protein electrophoresis (SPE) and immunoelectrophoresis (IEP).

Fibrin clot lysis time, also known as fibrinolytic time, is the measurement of the amount of time it takes for a blood clot to dissolve or lyse. This is typically measured in a laboratory setting using specialized tests such as the thromboelastography (TEG) or rotational thromboelastometry (ROTEM) assays. These tests measure the viscoelastic properties of a clot and can provide information about the rate of fibrinolysis, which is the natural process by which the body breaks down and removes blood clots.

Increased fibrin clot lysis time may indicate an impaired fibrinolytic system, which can lead to an increased risk of thrombosis or blood clot formation. Decreased fibrin clot lysis time may indicate an overactive fibrinolytic system, which can lead to an increased risk of bleeding.

It's important to note that the fibrin clot lysis time is just one factor among many that are considered when evaluating a patient's coagulation status and risk of thrombosis or bleeding. Other factors, such as platelet function, coagulation factor levels, and the presence of inhibitors or anticoagulants, must also be taken into account.

A platelet count is a laboratory test that measures the number of platelets, also known as thrombocytes, in a sample of blood. Platelets are small, colorless cell fragments that circulate in the blood and play a crucial role in blood clotting. They help to stop bleeding by sticking together to form a plug at the site of an injured blood vessel.

A normal platelet count ranges from 150,000 to 450,000 platelets per microliter (µL) of blood. A lower than normal platelet count is called thrombocytopenia, while a higher than normal platelet count is known as thrombocytosis.

Abnormal platelet counts can be a sign of various medical conditions, including bleeding disorders, infections, certain medications, and some types of cancer. It is important to consult with a healthcare provider if you have any concerns about your platelet count or if you experience symptoms such as easy bruising, prolonged bleeding, or excessive menstrual flow.

In the context of medical and biological sciences, a "binding site" refers to a specific location on a protein, molecule, or cell where another molecule can attach or bind. This binding interaction can lead to various functional changes in the original protein or molecule. The other molecule that binds to the binding site is often referred to as a ligand, which can be a small molecule, ion, or even another protein.

The binding between a ligand and its target binding site can be specific and selective, meaning that only certain ligands can bind to particular binding sites with high affinity. This specificity plays a crucial role in various biological processes, such as signal transduction, enzyme catalysis, or drug action.

In the case of drug development, understanding the location and properties of binding sites on target proteins is essential for designing drugs that can selectively bind to these sites and modulate protein function. This knowledge can help create more effective and safer therapeutic options for various diseases.

Blood platelet disorders are conditions that affect the number and/or function of platelets, which are small blood cells that help your body form clots to stop bleeding. Normal platelet count ranges from 150,000 to 450,000 platelets per microliter of blood. A lower-than-normal platelet count is called thrombocytopenia, while a higher-than-normal platelet count is called thrombocytosis.

There are several types of platelet disorders, including:

1. Immune thrombocytopenia (ITP): A condition in which the immune system mistakenly attacks and destroys platelets, leading to a low platelet count. ITP can be acute (lasting less than six months) or chronic (lasting longer than six months).
2. Thrombotic thrombocytopenic purpura (TTP): A rare but serious condition that causes blood clots to form in small blood vessels throughout the body, leading to a low platelet count, anemia, and other symptoms.
3. Hemolytic uremic syndrome (HUS): A condition that is often caused by a bacterial infection, which can lead to the formation of blood clots in the small blood vessels of the kidneys, resulting in kidney damage and a low platelet count.
4. Hereditary platelet disorders: Some people inherit genetic mutations that can affect the number or function of their platelets, leading to bleeding disorders such as von Willebrand disease or Bernard-Soulier syndrome.
5. Medication-induced thrombocytopenia: Certain medications can cause a decrease in platelet count as a side effect.
6. Platelet dysfunction disorders: Some conditions can affect the ability of platelets to function properly, leading to bleeding disorders such as von Willebrand disease or storage pool deficiency.

Symptoms of platelet disorders may include easy bruising, prolonged bleeding from cuts or injuries, nosebleeds, blood in urine or stools, and in severe cases, internal bleeding. Treatment for platelet disorders depends on the underlying cause and may include medications, surgery, or other therapies.

Cell adhesion refers to the binding of cells to extracellular matrices or to other cells, a process that is fundamental to the development, function, and maintenance of multicellular organisms. Cell adhesion is mediated by various cell surface receptors, such as integrins, cadherins, and immunoglobulin-like cell adhesion molecules (Ig-CAMs), which interact with specific ligands in the extracellular environment. These interactions lead to the formation of specialized junctions, such as tight junctions, adherens junctions, and desmosomes, that help to maintain tissue architecture and regulate various cellular processes, including proliferation, differentiation, migration, and survival. Disruptions in cell adhesion can contribute to a variety of diseases, including cancer, inflammation, and degenerative disorders.

Hemorrhagic disorders are medical conditions characterized by abnormal bleeding due to impaired blood clotting. This can result from deficiencies in coagulation factors, platelet dysfunction, or the use of medications that interfere with normal clotting processes. Examples include hemophilia, von Willebrand disease, and disseminated intravascular coagulation (DIC). Treatment often involves replacing the missing clotting factor or administering medications to help control bleeding.

Hirudin is not a medical term itself, but it is a specific substance with medical relevance. Hirudin is a naturally occurring anticoagulant that is found in the saliva of certain species of leeches (such as Hirudo medicinalis). This compound works by inhibiting the activity of thrombin, a key enzyme in the coagulation cascade, which ultimately results in preventing blood clot formation.

Medically, hirudin has been used in some research and therapeutic settings for its anticoagulant properties. For instance, recombinant hirudin (also known as lepirudin) is available for clinical use as an injectable anticoagulant to treat or prevent blood clots in specific medical conditions, such as heparin-induced thrombocytopenia (HIT).

In summary, Hirudins are a group of anticoagulant substances, primarily derived from leeches, that inhibit the activity of thrombin and have potential medical applications in preventing or treating blood clots.

Medical Definition:

"Risk factors" are any attribute, characteristic or exposure of an individual that increases the likelihood of developing a disease or injury. They can be divided into modifiable and non-modifiable risk factors. Modifiable risk factors are those that can be changed through lifestyle choices or medical treatment, while non-modifiable risk factors are inherent traits such as age, gender, or genetic predisposition. Examples of modifiable risk factors include smoking, alcohol consumption, physical inactivity, and unhealthy diet, while non-modifiable risk factors include age, sex, and family history. It is important to note that having a risk factor does not guarantee that a person will develop the disease, but rather indicates an increased susceptibility.

Tissue Plasminogen Activator (tPA) is a thrombolytic enzyme, which means it dissolves blood clots. It is naturally produced by the endothelial cells that line the interior surface of blood vessels. tPA activates plasminogen, a zymogen, to convert it into plasmin, a protease that breaks down fibrin, the structural protein in blood clots. This enzyme is used medically as a thrombolytic drug under various brand names, such as Activase and Alteplase, to treat conditions like acute ischemic stroke, pulmonary embolism, and deep vein thrombosis by dissolving the clots and restoring blood flow.

Nephelometry and turbidimetry are methods used in clinical laboratories to measure the amount of particles, such as proteins or cells, present in a liquid sample. The main difference between these two techniques lies in how they detect and quantify the particles.

1. Nephelometry: This is a laboratory method that measures the amount of light scattered by suspended particles in a liquid medium at a 90-degree angle to the path of the incident light. When light passes through a sample containing particles, some of the light is absorbed, while some is scattered in various directions. In nephelometry, a light beam is shone into the sample, and a detector measures the intensity of the scattered light at a right angle to the light source. The more particles present in the sample, the higher the intensity of scattered light, which correlates with the concentration of particles in the sample. Nephelometry is often used to measure the levels of immunoglobulins, complement components, and other proteins in serum or plasma.

2. Turbidimetry: This is another laboratory method that measures the amount of light blocked or absorbed by suspended particles in a liquid medium. In turbidimetry, a light beam is shone through the sample, and the intensity of the transmitted light is measured. The more particles present in the sample, the more light is absorbed or scattered, resulting in lower transmitted light intensity. Turbidimetric measurements are typically reported as percent transmittance, which is the ratio of the intensity of transmitted light to that of the incident light expressed as a percentage. Turbidimetry can be used to measure various substances, such as proteins, cells, and crystals, in body fluids like urine, serum, or plasma.

In summary, nephelometry measures the amount of scattered light at a 90-degree angle, while turbidimetry quantifies the reduction in transmitted light intensity due to particle presence. Both methods are useful for determining the concentration of particles in liquid samples and are commonly used in clinical laboratories for diagnostic purposes.

Macromolecular substances, also known as macromolecules, are large, complex molecules made up of repeating subunits called monomers. These substances are formed through polymerization, a process in which many small molecules combine to form a larger one. Macromolecular substances can be naturally occurring, such as proteins, DNA, and carbohydrates, or synthetic, such as plastics and synthetic fibers.

In the context of medicine, macromolecular substances are often used in the development of drugs and medical devices. For example, some drugs are designed to bind to specific macromolecules in the body, such as proteins or DNA, in order to alter their function and produce a therapeutic effect. Additionally, macromolecular substances may be used in the creation of medical implants, such as artificial joints and heart valves, due to their strength and durability.

It is important for healthcare professionals to have an understanding of macromolecular substances and how they function in the body, as this knowledge can inform the development and use of medical treatments.

The plasma fibrinogen levels (generally 50 mg/dl) detected in this disorder reflect the fibrinogen made by the normal gene. ... Plasma fibrinogen levels are similar to that seen in other forms of congenital dysfibrinogenemia. Fibrinogen Aα-Chain ... Low fibrinogen levels and dysfunctional fibrinogens usually prolong these times, whereas the lack of fibrinogen (i.e. ... Endothelium cells are also reported to make small amounts of fibrinogen, but this fibrinogen has not been fully characterized; ...
... , also known as fibrinogen gamma gene (FGG), is a human gene found on chromosome 4. The protein encoded ... Approximately 10% of the total plasma fibrinogen consists of γA/γ' fibrinogen, with ... 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 ...
A fibrinogen uptake test is a test that was formerly used to detect deep vein thrombosis. Radioactive labeled fibrinogen is ... Iodine 125-labeled fibrinogen scanning is a very sensitive method for detecting subclinical leg vein thrombi. Fibrinogen ... The technique is safe if fibrinogen is obtained from carefully screened donors. The limitations of the method include its ... Screening for these major thrombi may be improved by combining fibrinogen scanning with impedance plethysmography or ultrasonic ...
... has been shown to interact with Lipoprotein(a). Fibrin Fibrinogen alpha chain Fibrinogen gamma chain ... Berg K, Kierulf P (1989). "DNA polymorphisms at fibrinogen loci and plasma fibrinogen concentration". Clin. Genet. 36 (4): 229- ... Fibrinogen beta chain, also known as FGB, is a gene found in humans and most other vertebrates with a similar system of blood ... "Entrez Gene: FGB fibrinogen beta chain". Klose, R; Fresser F; Kochl S; Parson W; Kapetanopoulos A; Fruchart-Najib J; Baier G; ...
... has been shown to interact with tissue plasminogen activator. Fibrinogen gamma chain GRCh38: Ensembl ... Fibrinogen alpha chain is a protein that in humans is encoded by the FGA gene. The protein encoded by this gene is the alpha ... Following vascular injury, fibrinogen is cleaved by thrombin to form fibrin, which is the most abundant component of blood ... "Entrez Gene: FGA fibrinogen alpha chain". Tsurupa G, Medved L (Jan 2001). "Identification and characterization of novel tPA- ...
Hereditary fibrinogen Aα-Chain amyloidosis, a form of dysfibrinogenemia in which certain fibrinogen mutations cause blood ... Fibrinogen#Fibrinogen disorders Casini A, de Moerloose P, Neerman-Arbez M (2016). "Clinical Features and Management of ... Fibrinogen storage disease, a form of congenital hypofibrinogenemia in which specific hereditary mutations in fibrinogen cause ... a disorder in which normal levels of fibrinogen are composed at least in part of a dysfunctional fibrinogen due to an acquired ...
"Crystal Structure of the Tetrameric Fibrinogen-like Recognition Domain of Fibrinogen C Domain Containing 1 (FIBCD1) Protein". ... Fibrinogen C domain containing 1 (FIBCD1) is a protein that in humans is encoded by the FIBCD1 gene localized on chromosome ... "Entrez Gene: Fibrinogen C domain containing 1". Retrieved 2016-03-08. Shrive, Annette K.; Moeller, Jesper B.; Burns, Ian; ... and a C-terminal fibrinogen-like recognition domain, otherwise known as the FReD. (Shrive, et al., 2014) GRCm38: Ensembl ...
also describe a molecular mechanism for fibrinogen displacement involving pH cycling. Here the αC domains of fibrinogen change ... A typical example of this occurs when fibrinogen displaces earlier adsorbed proteins on a biopolymer surface and is later ... The process is delayed in narrow spaces and on hydrophobic surfaces, fibrinogen is usually not displaced. Under stagnant ... Horbett, Thomas A (October 2018). "Fibrinogen adsorption to biomaterials". Journal of Biomedical Materials Research. Part A. ...
The N-terminal FpA is cleaved from the Aα chains of fibrinogen and FpB from the Bβ chains of fibrinogen, with FpA released ... Weisel JW (2005). "Fibrinogen and fibrin". Adv Protein Chem. Advances in Protein Chemistry. 70: 247-99. doi:10.1016/S0065-3233( ... are peptides which are located in the central region of the fibrous glycoprotein fibrinogen (factor I) and are cleaved by the ... enzyme thrombin (factor IIa) to convert fibrinogen into covalently-linked fibrin (factor IA) monomers. ...
... of fibrinogen and fibrin subunit chains from four different genetic dysfibrinogen variants. In: Fibrinogen-Structure. Eds. ... He described the multifaceted Stormorken syndrome, a mutations in f. VII, f. IX, Fibrinogen Oslo IV and V, all with clinical ... Stormorken, H; Brosstad, F; Seim, H (28 April 1983). "A new dysfibrinogenemia: fibrinogen Oslo IV". Thrombosis and Haemostasis ... "Characterisation of Fibrinogen Oslo IV by electrospray mass spectrometry". Thrombosis and Haemostasis. 77 (5): 1040-1. doi: ...
Bennett JS (2001). "Platelet-fibrinogen interactions". Ann. N. Y. Acad. Sci. 936 (1): 340-54. Bibcode:2001NYASA.936..340B. doi: ... 2004). "Relationship of the platelet glycoprotein PlA and fibrinogen T/G+1689 polymorphisms with peripheral arterial disease ...
Bennett JS (2001). "Platelet-fibrinogen interactions". Ann. N. Y. Acad. Sci. 936 (1): 340-54. Bibcode:2001NYASA.936..340B. doi: ... post-translational cleavage to yield disulfide-linked light and heavy chains that join with beta 3 to form a fibrinogen ...
Dysfunction or disease of the liver can lead to a decrease in the production of fibrin's inactive precursor, fibrinogen, or to ... It is formed by the action of the protease thrombin on fibrinogen, which causes it to polymerize. The polymerized fibrin, ... Winston-Salem: International Fibrinogen Research Society. 23 June 2016. Retrieved 25 November 2022. Pabst M, Bondili JS, ... Fibrin is formed after thrombin cleavage of fibrinopeptide A (FPA) from fibrinogen Aalpha-chains, thus initiating fibrin ...
It was noticed that liver tissue obtained from patients aged 60 to 80 years had an increased level of fibrinogen. However, when ... Pilgeram, L; Pickart, L (1968). "Control of fibrinogen biosynthesis; the role of free fatty acids". Journal of Atherosclerosis ... Pilgeram, L (2010). "Control of fibrinogen biosynthesis; role of FFA/Albumin Ratio". Cardiovascular Engineering. 10 (2): 78-83 ...
"Fibrin/Fibrinogen Degradation Products". Archived from the original on 2008-08-21. Retrieved 2007-10-28. "510(k) summary: AMDL- ... Fibrin and fibrinogen degradation product (FDP) testing is commonly used to diagnose disseminated intravascular coagulation. A ...
... subunit of fibrinogen. Computation of the distance between the charged Arg and Asp sites in fibrinogen provided guidance ... Tirofiban is a synthetic, non-peptide inhibitor of the interaction of fibrinogen with the integrin glycoprotein IIb/IIIa on ... Tirofiban is a small molecule inhibitor of the protein-protein interaction between fibrinogen and the platelet integrin ... November 1992). "Non-peptide fibrinogen receptor antagonists. 1. Discovery and design of exosite inhibitors". Journal of ...
Thrombin is an enzyme that splits fibrinogen into fibrin monomers in 10 to 60 seconds, which aggregate to form a three- ... It contains separately packaged human fibrinogen and human thrombin. This glue is used as a supportive treatment in surgery ( ... "AusPAR: Human Fibrinogen / Human Thrombin". Therapeutic Goods Administration (TGA). 29 June 2022. Retrieved 17 July 2022. " ... KEGG drug: Factor XIII with fibrinogen. Accessed 2020-07-09. "Evicel". U.S. Food and Drug Administration (FDA). 5 June 2017. ...
Fibrinogen level was initially thought to be useful in the diagnosis of DIC but because it is an acute phase reactant, it will ... The breakdown of fibrinogen and fibrin results in polypeptides called fibrin degradation products (FDPs) or fibrin split ... Findings may include low platelets, low fibrinogen, high INR, or high D-dimer. Treatment is mainly directed towards the ... The activation of the coagulation cascade yields thrombin that converts fibrinogen to fibrin; the stable fibrin clot being the ...
... is also capable of segregating platelets by cleaving the fibrinogen cross-link amongst the platelets. Fibrinogen acts ... Cleavage of fibrinogen in its native conformation at AαAsn102-Asn103, BβLys130-Gln131, and ϓPro76-Asn77 yield three sets of ... It is capable of disrupting the function of fibrinogen, a glycoprotein responsible for blood clotting, by cleaving three ... Hementin is an anticoagulant protease (fibrinogen lytic enzyme) from the salivary glands of the giant Amazon leech (Haementeria ...
Ugarova TP, Yakubenko VP (2001). "Recognition of fibrinogen by leukocyte integrins". Ann. N. Y. Acad. Sci. 936 (1): 368-85. ...
Fibrinogen-like protein 1 is a member of the fibrinogen family of proteins, which also includes fibrinogen, fibrinogen-like ... "Entrez Gene: FGL1 fibrinogen-like 1". Wang J, Sanmamed MF, Datar I, Su TT, Ji L, Sun J, et al. (January 2019). "Fibrinogen-like ... Fibrinogen-like protein 1 (FGL-1) is a protein that is structurally related to fibrinogen. In humans, FGL-1 is encoded by the ... FGL-1 is homologous to the carboxy terminus of the fibrinogen beta- and gamma- subunits which contains the four conserved ...
Fibrinogen comprises 7% of blood proteins; conversion of fibrinogen to insoluble fibrin is essential for blood clotting. The ...
It cleaves fibrinogen, similarly to thrombin. Batroxobin from B atrox is used as a drug called "Reptilase" that is used to stop ...
Fibrinogen-like protein 2, also known as FGL2, is a protein which in humans is encoded by the FGL2 gene. FGL2 is a 439 amino ... "Entrez Gene: FGL2 fibrinogen-like 2". Rüegg C, Pytela R (July 1995). "Sequence of a human transcript expressed in T-lymphocytes ... 2005). "Role of fibrinogen-like protein 2 prothrombinase/fibroleukin in experimental and human allograft rejection". J. Immunol ... 2006). "Fibrinogen-like protein 2 fibroleukin expression and its correlation with disease progression in murine hepatitis virus ...
1996). "A novel human serum lectin with collagen- and fibrinogen-like domains that functions as an opsonin". J. Biol. Chem. 271 ... "Entrez Gene: FCN2 ficolin (collagen/fibrinogen domain containing lectin) 2 (hucolin)". Lu J, Le Y (1999). "Ficolins and the ... and a C-terminal fibrinogen-like domain. This gene is predominantly expressed in the liver, and has been shown to have ... purification and preliminary crystallographic analysis of human M-ficolin fibrinogen-like domain". Acta Crystallographica ...
... is an equine collagen sponge coated with the human plasma-derived coagulation factors fibrinogen and thrombin. It is ... "Tachosil- thrombin human and fibrinogen patch". DailyMed. 2 November 2022. Archived from the original on 19 May 2023. Retrieved ... "Tachosil- thrombin human and fibrinogen patch". DailyMed. 16 February 2023. Archived from the original on 19 May 2023. ...
It also cleaves and therefore inactivates a significant part of circulating plasma fibrinogen. Fibrinogen is often found in ... Hao Z, Liu M, Counsell C, Wardlaw JM, Lin S, Zhao X (March 2012). "Fibrinogen depleting agents for acute ischaemic stroke". The ... If systemic bleeding is severe enough to warrant fast reversal of ancrod action, fibrinogen should be substituted (please refer ... One of the cleavage fibrinogen products, termed 'desAA-Fibrin', acts as cofactor for the tPA-induced plasminogen activation and ...
Venombin A from snake venom were used in stokes to deplete fibrinogen by forming very weak clots that can be easily dissolved. ... Hao Z, Liu M, Counsell C, Wardlaw JM, Lin S, Zhao X (March 2012). "Fibrinogen depleting agents for acute ischaemic stroke". The ...
It can often refer more specifically to mean: a part of the T-cell receptor, the fibrinogen alpha chain, the integrin alpha ... Fibrinogen Peptide Lesieur, Claire (2014-06-18). Oligomerization of Chemical and Biological Compounds. BoD - Books on Demand. ...
They are thought to act as an antithrombotic by depletion of fibrinogen. They are different from thrombin in that they only ... Hao Z, Liu M, Counsell C, Wardlaw JM, Lin S, Zhao X (March 2012). "Fibrinogen depleting agents for acute ischaemic stroke". The ... This enzyme catalyses the following chemical reaction Selective cleavage of Arg- bond in fibrinogen, to form fibrin, and ... a snake venom enzyme that clots fibrinogen". Proceedings of the National Academy of Sciences of the United States of America. ...
The plasma fibrinogen levels (generally 50 mg/dl) detected in this disorder reflect the fibrinogen made by the normal gene. ... Plasma fibrinogen levels are similar to that seen in other forms of congenital dysfibrinogenemia. Fibrinogen Aα-Chain ... Low fibrinogen levels and dysfunctional fibrinogens usually prolong these times, whereas the lack of fibrinogen (i.e. ... Endothelium cells are also reported to make small amounts of fibrinogen, but this fibrinogen has not been fully characterized; ...
Afibrinogenemia and hypofibrinogenemia are quantitative defects in fibrinogen (type I), which result from muta... ... Congenital abnormalities of fibrinogen are divided into 2 types: type I, or quantitative abnormalities (afibrinogenemia and ... Management of fibrinogen abnormalities. Medical care in fibrinogen abnormalities can include the following:. * Hemorrhage - ... The primary physiologic role of fibrinogen is in hemostasis. In the final step of the coagulation cascade, fibrinogen is ...
1. The preferred method of specimen collection for coagulation studies is a properly performed VENIPUNCTURE. The specimen may be collected directly into 1.8 or 2.7 mL vacutainer or into a syringe and then transferred immediately into a 1.8 or 2.7 mL vacutainer. 2. The vacutainer tube MUST contain the EXACT amount of blood. It is essential that LT blue top tubes are PROPERLY FILLED. Volume is CRITICAL and the blood (9 parts) to liquid anticoagulant (1 part) must remain intact for correct results. 3. The specimen should be transported to the Laboratory within one hour of collection. 4. SPECIAL INSTRUCTIONS FOR SPECIMENS COLLECTED FROM A LINE: If collecting specimens for coagulation studies from an indwelling line that may contain heparin, it is recommended that the line should be flushed with 5 mL of saline and the first 5 mL of blood or 6-times the line volume (dead space volume of the catheter) be drawn off and discarded before the coagulation tube is filled. For those samples collected from a ...
Although this is fibrinogens main job, it also forms bridges between platelets. Fibrinogen is a protein made by the liver. It ... Fibrinogen is the clotting element present in blood. When blood comes out of a wound in a vessel, the fibrinogen is activated ... When fibrinogen is activated to form fibrin, an enzyme called thrombin cleaves the fibrinopeptides off of the alpha and beta ... It is possible to examine a small sample of a persons blood to find out how much fibrinogen is in the blood. This helps ...
Fibrinogen results in cognitive decline in Alzheimers disease, finds study. *Download PDF Copy ... The team showed that fibrinogen can have this effect even in brains that lack amyloid plaques, which are the focus of diverse ... In their study, published in the scientific journal Neuron, the researchers found that fibrinogen, after leaking from the blood ... The researchers showed that injecting even extremely small quantities of fibrinogen into a healthy brain caused the same kind ...
Therefore, Fibrinogen and Thrombin are not expected to pose a risk to the environment in accordance with the Guideline on ... Fass environmental information for fibrinogen (Fibryga, Riastap and Tachosil) from Octapharma, CSL Behring and Takeda Pharma ... This summary information comes from the assessment report for VeraSeal (fibrinogen, thrombin) and Fass environmental ...
Blood fibrinogen as a biomarker of chronic obstructive pulmonary disease Message subject: (Your Name) has forwarded a page to ...
LBDFBSI - Fibrinogen (g/L). Variable Name: LBDFBSI. SAS Label: Fibrinogen (g/L). English Text: Fibrinogen (g/L). Target: Both ... LBXFB - Fibrinogen (mg/dL). Variable Name: LBXFB. SAS Label: Fibrinogen (mg/dL). English Text: Fibrinogen (mg/dL). Target: Both ... Fibrinogen Fibrinogen is an essential blood-clotting factor and is involved in a range of other functions, including platelet ... Fibrinogen On the STA-Compact, the Clauss clotting method determined the fibrinogen concentration in plasma quantitatively. ...
If you wish to reuse any or all of this article please use the link below which will take you to the Copyright Clearance Centers RightsLink service. You will be able to get a quick price and instant permission to reuse the content in many different ways.. ...
Plasma fibrinogen is increasingly recognized as an independent risk factor for stroke and ischemic heart disease (Ann NY Acad ... A randomized, double-blind, placebo-controlled trial showed a statistically significant reduction in fibrinogen levels using ...
Previous studies showed that fibrinogen-to-albumin ratio (FAR) regarded as a novel inflammatory and thrombotic biomarker was ... Relation of Fibrinogen-to-Albumin Ratio to Severity of Coronary Artery Disease and Long-Term Prognosis in Patients with Non-ST ... B. L. Walton, J. R. Byrnes, and A. S. Wolberg, "Fibrinogen, red blood cells, and factor XIII in venous thrombosis," Journal of ... Fibrinogen is a serum glycoprotein with a dimeric molecular structure synthesized by the liver [16], which plays an important ...
Exercise, fibrinogen, and other risk factors for ischaemic heart disease. Caerphilly Prospective Heart Disease Study. ... Exercise, fibrinogen, and other risk factors for ischaemic heart disease. Caerphilly Prospective Heart Disease Study. ... Risk factors for heart disease examined included blood pressure, lipids, fibrinogen, and plasma viscosity. Possible confounding ... Fibrinogen concentration was lower by 0.24 g/l and viscosity by 0.026 cP in the third of men who were most active in leisure ...
... they refer to the finding that plasma fibrinogen concentrations are related to a polymorphism in the β-fibrinogen gene, with ... this finding is in keeping with the evidence from controlled trials that suggests that drugs lowering fibrinogen do not ... particularly the association of fibrinogen with socioeconomic status, and its interpretation is not correct, and runs contrary ...
FGG / Fibrinogen Gamma. fibrinogen gamma chain. Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to ... FGG, Fibrinogen gamma-b chain, Fibrinogen gamma chain, Fibrinogen, gamma polypeptide. Target Sequences:. NM_021870 NP_068656.2 ... Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it ... FGG / Fibrinogen Gamma Antibody (aa166-416, clone IgG1,k, Biotin) LS-C418055 ...
The affinity of fibrinogen to integrin receptors has been studied in B16F0 tumors. Fibrinogen nanoparticles and liposomes were ... Fibrinogen-bound methotrexate therapy in vivo was described for Gardner lymphosarcoma in mice. Fibrinogen-methotrexate ... Thermo-responsive Fibrinogen Nanogels: a Viable Thermo-responsive Drug Delivery Agent for Breast Cancer Therapy?. Publication ... Fibrinogen coating has significantly reduced the toxicity induced by the bare QDs which make it more cytocompatible and also ...
... the story of Octapharmas high-purity human fibrinogen concentrate ... Reduced or dysfunctional fibrinogen occurs in various congenital fibrinogen-related disorders. However, unlike in congenital ... Today, scientific progress allows us to produce high-purity human fibrinogen concentrate to treat acquired fibrinogen ... The 2011 launch of the clinical trial to investigate the use of our high-purity human fibrinogen concentrate in congenital ...
Anti-human fibrinogen antibody bound to ADP-, PAF-, and A23817- activated platelets, but binding was not dependent on platelet ... The extent of binding of anti-fibrinogen antibody was less in equine platelets, compared with that for human platelets, despite ... anti-human fibrinogen antibody, and anti-thrombospondin antibody to unactivated and ADP-, collagen-, platelet activating factor ... labeled annexin V and anti-human fibrinogen antibody but not by use of anti-human thrombospondin antibody. These flow ...
Massive Hemorrhage Protocol: Blood Products (TXA, Fibrinogen, PCC) Substitutions. Presented by Dr. Michelle Sholzberg, St. ... Massive Hemorrhage Protocol: Blood Products (TXA, Fibrinogen, PCC) Substitutions. *Massive Hemorrhage Protocol: Temperature/ ...
We provide biomedical researchers with the best tools available for the analysis of Oxidative Stress and Chronic Inflammation - two of the most important risk factors that play key roles in the development of a wide range of human illness, including cancer, cardiovascular disease, diabetes and neurodegeneration.. ...
Fibrinogen Gamma in Plasma, Serum. It is a Sandwich assay which can detect FGG / Fibrinogen Gamma down to 15.625 ng/ml. For ... Fibrinogen Gamma ELISA Kit LS-F40146 is a 96-Well enzyme-linked immunosorbent assay for the Quantitative detection of Human FGG ... Human FGG / Fibrinogen Gamma (Sandwich ELISA) ELISA Kit - LS-F40146 Human FGG / Fibrinogen Gamma (Sandwich ELISA) ELISA Kit - ... It is based upon a Sandwich assay principle and can be used to detect levels of FGG / Fibrinogen Gamma as low as 9.375 ...
In the RT group with low fibrinogen levels, OS rates after 2 and 3 years were 74 and 53 %, and in the high-fibrinogen group 40 ... Fibrinogen and thrombotic disease. J Thromb Haemost. 2013;11 Suppl 1:294-305. CrossRefPubMed Ariëns RA. Fibrinogen and ... Plasma fibrinogen and serum C-reactive protein are associated with non-small cell lung cancer. Lung Cancer. 2006;53:1. CrossRef ... Fibrinogen levels correlate with stage of disease in patients with oesophageal cancer. Br J Surg. 1997;84:2. CrossRef ...
This is an ELISA for the quantitative analysis of total fibrinogen levels in rat plasma and serum. This test operates on the ... basis of sandwich ELISA where the fibrinogen binds to a capture antibody on the plate and is quantified with the use of a ...
Fibrin/Fibrinogen & Fibrin(ogen) Degradation Products. By Technical Data. Fibrin/Fibrinogen & Fibrin(ogen) Degradation Products ... Fibrin/Fibrinogen & Fibrin(ogen) Degradation Products - from Mouse - Antibodies. Fibrin/Fibrinogen & Fibrin(ogen) Degradation ... Fibrin/Fibrinogen & Fibrin(ogen) Degradation Products - Monoclonal Antibody - Antibodies. Human - Fibrin/Fibrinogen & Fibrin( ... Fibrinogen alpha (FGA), fibrinogen beta (FGB), and fibrinogen gamma (FGG) polymerize to form an insoluble fibrin matrix. Fibrin ...
Human Fibrinogen and product number, FIB.Human Fibrinogen Purified from Innovative Research has been purified from human plasma ... Keep fibrinogen at 25-37C, aliquot and flash-freeze unused portion.. This product can be used as a control in applications like ... Human Fibrinogen Purified from Innovative Research has been purified from human plasma by a propritetary process that combines ... Select this product for Molecular Innovations name, Human Fibrinogen and product number, FIB. ...
As a result of this interaction, fibrinogen is converted to fibrin and fibrinogen-derived peptides, termed fibrinopeptides, are ... As a result of this interaction, fibrinogen is converted to fibrin and fibrinogen-derived peptides, termed fibrinopeptides, are ... As a result of this interaction, fibrinogen is converted to fibrin and fibrinogen-derived peptides, termed fibrinopeptides, are ... The conversion of fibrinogen to fibrin at the surface of curliated E. coli bacteria leads to the generation of proinflammatory ...
... fibrinogen. These findings demonstrate that, in fully hydrated conditions, thrombin and fibrinogen γ have dramatic effects on ... Thrombin and fibrinogen γ impact clot structure by marked effects on intrafibrillar structure and protofibril packing ... Fibers produced with fibrinogen γ showed reduced protofibril packing over a range of thrombin concentrations. High- ... Our aim was to investigate the role of thrombin and fibrinogen γ in modulating fibrin structure under fully hydrated ...
Dive into the research topics of SARS-CoV-2 spike protein S1 induces fibrin(ogen) resistant to fibrinolysis: Implications for ... SARS-CoV-2 spike protein S1 induces fibrin(ogen) resistant to fibrinolysis: Implications for microclot formation in COVID-19. ...
Launch Diagnostics is a licensed reseller and distributor of Duplica RealTime Beta-Fibrinogen 455G>A Genotyping Kit. Launch ... PCR kit for the detection of the 455G,A polymorphism in the promoter region of the Beta-Fibrinogen gene. ...
Fibrinogen as a key regulator of inflammation in disease. Davalos D, Akassoglou K. Fibrinogen as a key regulator of ... Fibrinogen in neurological diseases: mechanisms, imaging and therapeutics. Petersen MA, Ryu JK, Akassoglou K. Fibrinogen in ... Fibrinogen Induces Microglia-Mediated Spine Elimination and Cognitive Impairment in an Alzheimers Disease Model. Merlini M, ...
  • Although the primary function of fibrinogen is in fibrin clot formation, it has a multitude of other functions, including nonsubstrate thrombin binding, platelet aggregation, and fibrinolysis. (medscape.com)
  • Exposure of its nonsubstrate thrombin-binding sites after fibrin clot formation promotes the antithrombotic properties of fibrinogen. (medscape.com)
  • Thrombin time is more sensitive than PT or aPTT for quantitative and qualitative defects in fibrinogen. (medscape.com)
  • When fibrinogen is activated to form fibrin, an enzyme called thrombin cleaves the fibrinopeptides off of the alpha and beta chains. (wikipedia.org)
  • This summary information comes from the assessment report for VeraSeal (fibrinogen, thrombin) and Fass environmental information for various drugs with fibrinogen. (janusinfo.se)
  • Therefore, Fibrinogen and Thrombin are not expected to pose a risk to the environment in accordance with the Guideline on environmental risk assessment of medicinal products for human use (EMEA/CHMP/SWP/4447/00). (janusinfo.se)
  • This test method involves measuring the rate of fibrinogen to fibrin conversion in diluted sample under the influence of excess thrombin. (cdc.gov)
  • Previous studies have shown effects of thrombin and fibrinogen γ' on clot structure. (whiterose.ac.uk)
  • Our aim was to investigate the role of thrombin and fibrinogen γ' in modulating fibrin structure under fully hydrated conditions. (whiterose.ac.uk)
  • Fibers produced with fibrinogen γ' showed reduced protofibril packing over a range of thrombin concentrations. (whiterose.ac.uk)
  • Decreased protofibril packing was confirmed in plasma for high thrombin concentrations and fibrinogendeficient plasma reconstituted with γ' fibrinogen. (whiterose.ac.uk)
  • These findings demonstrate that, in fully hydrated conditions, thrombin and fibrinogen γ' have dramatic effects on protofibril content and that protein density within fibers correlates with strength of the fibrin network. (whiterose.ac.uk)
  • We conclude that regulation of protofibril content of fibers is an important mechanism by which thrombin and fibrinogen γ' modulate fibrin clot structure and strength. (whiterose.ac.uk)
  • 3. Thrombin converts fibrinogen into fibrin. (safalta.com)
  • The thrombin (IIa) catalyzed cleavage of soluble fibrinogen (Fbg) to form fibrin (Fbn) is the terminal proteolytic event in the coagulation cascade. (cellsystems.eu)
  • Download Citation on ResearchGate \textbar Arachidonate induced fibrinogen binding to thrombin degranulated platelets is independent of released ADP \textbar When human or rabbit platelets are stimulated with ADP, fibrinogen (Fbg) binding sites are revealed, the platelets bind Fbg and aggregate. (mcmaster.ca)
  • The assay measures the ability of fibrinogen to form fibrin clot after being exposed to a high concentration of purified thrombin. (yycnewcentrallibrary.com)
  • Fibrinogen, the substrate of thrombin, provides the major meshwork of arterial thrombi. (yycnewcentrallibrary.com)
  • Fibrinogen is a soluble protein in the plasma that is broken down to fibrin by the enzyme thrombin to form clots. (medscape.com)
  • For coagulation to occur, another protein called thrombin removes a piece from the Aα and the Bβ subunits of the functional fibrinogen protein (the pieces are called the A and B fibrinopeptides). (medlineplus.gov)
  • Two small peptide chains removed from the N-terminal segment of the beta chains of fibrinogen by the action of thrombin. (bvsalud.org)
  • Fibrinogen is a "positive" acute-phase protein, i.e. its blood levels rise in response to systemic inflammation, tissue injury, and certain other events. (wikipedia.org)
  • Mature fibrinogen is arranged as a long flexible protein array of three nodules held together by a very thin thread which is estimated to have a diameter between 8 and 15 Ã…ngstrom (Ã…). (wikipedia.org)
  • Fibrinogen is a protein made by the liver . (wikipedia.org)
  • Scientists at the Gladstone Institutes, led by Senior Investigator Katerina Akassoglou, PhD, showed for the first time that a blood-clotting protein called fibrinogen is responsible for a series of molecular and cellular events that can destroy connections between neurons in the brain and result in cognitive decline. (news-medical.net)
  • 1) Fibrinogen and its end product fibrin are the only known coagulable protein in the blood of vertebrates. (truthwiki.org)
  • Fibrinogen, the protein of the blood plasma, is converted into the insoluble protein fibrin during the clotting process. (britannica.com)
  • Fibrinogen is a protein found in blood plasma which plays a vital role in blood clotting. (yycnewcentrallibrary.com)
  • Fibrinogen (feye-BRIN-oh jen) is a protein needed for blood to clot. (yycnewcentrallibrary.com)
  • Fibrinogen is a soluble protein that is produced in the liver and released into the bloodstream. (medscape.com)
  • The FGG gene provides instructions for making the fibrinogen gamma (γ) chain, one piece (subunit) of the fibrinogen protein. (medlineplus.gov)
  • Two sets of this three-protein complex combine to form functional fibrinogen. (medlineplus.gov)
  • This process converts fibrinogen to fibrin, the main protein in blood clots. (medlineplus.gov)
  • Mutations in the FGG gene can lead to congenital afibrinogenemia, a condition that causes excessive bleeding due to the absence of fibrinogen protein in the blood. (medlineplus.gov)
  • Without the γ subunit, the fibrinogen protein is not assembled, which results in the absence of fibrin. (medlineplus.gov)
  • Dysfibrinogenemia is a condition characterized by abnormally functioning fibrinogen, although the protein is present at normal levels. (medlineplus.gov)
  • This condition is usually caused by mutations that change a single protein building block (amino acid) in the fibrinogen γ chain. (medlineplus.gov)
  • These mutations alter the function of the fibrinogen protein and, depending on the functional change, can lead to excessive bleeding or abnormal blood clotting (thrombosis). (medlineplus.gov)
  • Hypodysfibrinogenemia is a condition characterized by low levels of abnormally functioning fibrinogen protein in the blood. (medlineplus.gov)
  • C-reactive protein, fibrinogen, and procalcitonin levels as early markers of staple line leak after laparoscopic sleeve gastrectomy in morbidly obese patients within an Enhanced Recovery After Surgery (ERAS) program. (bvsalud.org)
  • Acute-phase parameters ( C-reactive protein , procalcitonin , fibrinogen , and White Blood Cell count ) were investigated. (bvsalud.org)
  • Novel biomarkers of risk, such as apolipoprotein (Apo) A1 and ApoB (2), and the inflammatory markers C-reactive protein (CRP), fibrinogen, and homocysteine (3-5), have been proposed. (cdc.gov)
  • Markers of systemic inflammation, including C-reactive protein (CRP), fibrinogen, and white blood cell (WBC) levels, were determined in peripheral blood samples collected at baseline and after 5.3 (SD 1.0) hours of exposure. (cdc.gov)
  • In the final step of the coagulation cascade, fibrinogen is converted to fibrin, with formation of a fibrin clot. (medscape.com)
  • As a result of this interaction, fibrinogen is converted to fibrin and fibrinogen-derived peptides, termed fibrinopeptides, are generated. (lu.se)
  • At the end of the cascade, fibrinogen is converted to fibrin. (medscape.com)
  • Interestingly, Akassoglou and her colleagues recently developed an antibody that blocks the interaction between fibrinogen and a molecule on the brain's immune cells. (news-medical.net)
  • The remainder of the fibrinogen molecule, a monomer , is soluble and stable at pH values less than 6 (i.e., in acid solutions). (britannica.com)
  • Reduced and/or dysfunctional fibrinogens occur in various congenital and acquired human fibrinogen-related disorders. (wikipedia.org)
  • Congenital abnormalities of fibrinogen are divided into two types: type I, or quantitative abnormalities (afibrinogenemia and hypofibrinogenemia), and type II, or qualitative abnormalities (dysfibrinogenemia and hypodysfibrinogenemia). (medscape.com)
  • The 2011 launch of the clinical trial to investigate the use of our high-purity human fibrinogen concentrate in congenital fibrinogen deficiency was the start of a clinical development programme in a very rare disease. (octapharma.com)
  • This approval extends the original 2017 marketing authorisation for Octapharma's high-purity human fibrinogen concentrate for use in congenital fibrinogen deficiency. (octapharma.com)
  • Reduced or dysfunctional fibrinogen occurs in various congenital fibrinogen-related disorders. (octapharma.com)
  • However, unlike in congenital fibrinogen deficiencies, AFD arises due to consumption of fibrinogen after excessive blood loss. (octapharma.com)
  • After Octapharma's high-purity human fibrinogen concentrate obtained regulatory approval in the USA, Canada and the EU in 2017 for the treatment of very rare congenital fibrinogen deficiencies (with further approval obtained in Switzerland in 2018 for both acquired and congenital fibrinogen deficiencies), clinical initiatives continued with FORMA-05, the first new clinical study in AFD. (octapharma.com)
  • Some of the genetic disorders associated with fibrinogen include congenital afibrogenmia and familial renal amyloidosis. (yycnewcentrallibrary.com)
  • Molecular analysis of the fibrinogen gene cluster in 16 patients with congenital afibrinogenemia: novel truncating mutations in the FGA and FGG genes. (medlineplus.gov)
  • Afibrinogenemia and hypofibrinogenemia are quantitative defects in fibrinogen (type I), which result from mutations that affect plasma fibrinogen concentration inherited on both chromosomal alleles and are frequently associated with a bleeding diathesis but occasionally a thrombotic event. (medscape.com)
  • LS-F40146 is a 96-well enzyme-linked immunosorbent assay (ELISA) for the Quantitative detection of Human FGG / Fibrinogen Gamma in samples of Plasma and Serum. (lsbio.com)
  • This is an ELISA for the quantitative analysis of total fibrinogen levels in rat plasma and serum. (oxfordbiomed.com)
  • Description: A competitive ELISA for quantitative measurement of Rabbit Fibrinogen in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (gentaur-online.com)
  • The Clauss fibrinogen assay is a quantitative, clot-based, functional assay. (yycnewcentrallibrary.com)
  • The fibrinogen-free fluid obtained after removal of the clot, called blood serum, is blood plasma minus fibrinogen. (britannica.com)
  • Fibrinogen deficiency is caused by a mutation (change) on the FGA, FGB or FGG gene all of which play a role in causing blood to clot. (yycnewcentrallibrary.com)
  • Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. (lsbio.com)
  • Since under these conditions the fibrinogen content was rate limiting, the clotting time can be used as a measure of the concentration of the fibrinogen and in fact, the clotting time is inversely proportional to the level of fibrinogen in the plasma. (cdc.gov)
  • The normal level of fibrinogen in human blood plasma is 200-400 mg/dL. (yycnewcentrallibrary.com)
  • Using receiver operating characteristic analysis at 24 h postoperatively, a cutoff level of CRP at 9 mg/dL achieved 85% sensitivity and 90% specificity for predicting staple line leak, a cutoff level of procalcitonin at 0.85 ng/mL achieved 70% sensitivity and 90% specificity , and a cutoff level of fibrinogen at 600 mg/dL achieved 80% sensitivity and 87.5% specificity . (bvsalud.org)
  • Normal amounts of fibrinogen in blood vary from 100 mg to 700 mg per 100 ml of blood. (truthwiki.org)
  • The final secreted, hepatocyte-derived glycoprotein is composed of two trimers, with each trimer composed of three different polypeptide chains, the fibrinogen alpha chain (also termed the Aα or α chain) encoded by the FGA gene, the fibrinogen beta chain (also termed the Bβ or β chain) encoded by the FGB gene, and the fibrinogen gamma chain (also termed the γ chain) encoded by the FGG gene. (wikipedia.org)
  • As the evidence, they refer to the finding that plasma fibrinogen concentrations are related to a polymorphism in the β-fibrinogen gene, with presence of the "T" allele being associated with higher levels. (bmj.com)
  • A polymorphism in the promoter region of the Beta-Fibrinogen gene. (launchdiagnostics.com)
  • Whole exome sequencing identified a heterozygous missense mutation at codon 35 of the fibrinogen α (FGA) gene. (escholarship.org)
  • 9: Fuller GM, Zhang Z. Transcriptional control mechanism of fibrinogen gene expression Ann N Y Acad Sci. (moleculardepot.com)
  • Because this condition occurs when both copies of the FGG gene are altered, there is a complete absence of functional fibrinogen γ chain. (medlineplus.gov)
  • However, these tests have a poor sensitivity to mild fibrinogen deficiency or dysfunction. (medscape.com)
  • Today, scientific progress allows us to produce high-purity human fibrinogen concentrate to treat acquired fibrinogen deficiency (AFD). (octapharma.com)
  • But it also became an early step in one of the most audacious clinical programmes which Octapharma has conducted, targeting acquired fibrinogen deficiency (AFD). (octapharma.com)
  • What causes fibrinogen deficiency? (yycnewcentrallibrary.com)
  • Neerman-Arbez M. Molecular basis of fibrinogen deficiency. (medlineplus.gov)
  • In the low-fibrinogen (below 411 mg/dL) postoperatively irradiated group, OS rates at 2 and 3 years were 86 and 83 %, and in the high-fibrinogen group 66 and 51 %, respectively. (springermedizin.at)
  • In the RT group with low fibrinogen levels, OS rates after 2 and 3 years were 74 and 53 %, and in the high-fibrinogen group 40 and 22 %, respectively. (springermedizin.at)
  • What does a high fibrinogen level mean? (yycnewcentrallibrary.com)
  • High fibrinogen is associated with higher rates of heart disease, blood vessel dysfunction, and stroke. (yycnewcentrallibrary.com)
  • The conversion of soluble fibrinogen to insoluble fibrin. (medscape.com)
  • Procedure -Flow cytometry was used to assess platelet activation as indicated by detection of binding of fluorescent-labeled annexin V, anti-human fibrinogen antibody, and anti-thrombospondin antibody to unactivated and ADP-, collagen-, platelet activating factor (PAF)-, and A23187-activated equine platelets. (avma.org)
  • Anti-human fibrinogen antibody bound to ADP-, PAF-, and A23817- activated platelets, but binding was not dependent on platelet secretion. (avma.org)
  • The extent of binding of anti-fibrinogen antibody was less in equine platelets, compared with that for human platelets, despite maximal stimulation. (avma.org)
  • Conclusions and Clinical Relevance -Activation of equine platelets can be detected by use of fluorescent- labeled annexin V and anti-human fibrinogen antibody but not by use of anti-human thrombospondin antibody. (avma.org)
  • This test operates on the basis of sandwich ELISA where the fibrinogen binds to a capture antibody on the plate and is quantified with the use of a biotin labeled primary antibody and an avidin-HRP conjugate. (oxfordbiomed.com)
  • ProductData": { "ID": "RTD000911", "ProductType": "Others", "BrandName": "FITC anti-Fibrinogen Primary Antibody", "ProductNameAddition": "", "RegulatoryDisclaimer1": "For in vitro diagnostic use. (roche.com)
  • contains a goat polyclonal antibody directed against human fibrinogen approximately 1.4 µg/mL. (roche.com)
  • Language": "en", "Country": "XG", "Code": "Content" }, { "Name": "Intended Use", "Value": "This antibody is intended for in vitro diagnostic (IVD) use. (roche.com)
  • Ventana ® Medical Systems' (Ventana) FITC anti-Fibrinogen Primary Antibody is a goat derived polyclonal antibody labeled with fluorescein and specifically directed against human fibrinogen. (roche.com)
  • FITC anti-Fibrinogen contains a goat polyclonal antibody raised against purified human fibrinogen. (roche.com)
  • Language": "en", "Country": "XG", "Code": "Background Information" }, { "Name": "Principle", "Value": "FITC anti-Fibrinogen may be used as the primary antibody for immunohistochemical staining of frozen tissue sections. (roche.com)
  • The normal concentration of fibrinogen in blood plasma is 150-400 mg/dl, with levels appreciably below or above this range associated with pathological bleeding and/or thrombosis. (wikipedia.org)
  • Fibrinogen is a 340-kD glycoprotein that is synthesized in the liver and circulates in plasma at a concentration of 2-4 g/L, with a half-life of 4 days. (medscape.com)
  • On the STA-Compact, the Clauss clotting method determined the fibrinogen concentration in plasma quantitatively. (cdc.gov)
  • The time was translated into fibrinogen concentration from a fibrinogen standard curve, stored on the STA Compact. (cdc.gov)
  • OBJECTIVE--To examine the associations between physical activity and a wide range of risk factors for ischaemic heart disease including fibrinogen concentration and viscosity. (bmj.com)
  • RESULTS--Fibrinogen concentration was lower by 0.24 g/l and viscosity by 0.026 cP in the third of men who were most active in leisure activities (about 0.25 x 1 SD). (bmj.com)
  • Plasma fibrinogen is large glycoprotein (Mr = 340,000) synthesized in the liver and circulating at a concentration of 2.6 mg/ml. (cellsystems.eu)
  • RÉSUMÉ Les polymorphismes du gène du facteur VII peuvent contribuer à l'élévation de la concentration en activité coagulante du facteur VII (FVIIc) qui a été associée au risque cardio-vasculaire. (who.int)
  • Les sujets ayant un génotype R/R avaient une concentration en FVIIc significativement plus élevée que les sujets hétérozy- gotes et homozygotes porteurs de l'allèle Q353 (96,36 vs 59,52). (who.int)
  • La concentration en FVIIc avec le polymor- phisme d'insertion de 10 pb n'était pas significativement différente. (who.int)
  • Fibrinogen (factor I) is a glycoprotein complex, produced in the liver, that circulates in the blood of all vertebrates. (wikipedia.org)
  • blood platelets and their precursors, bone marrow megakaryocytes, while once thought to make fibrinogen, are now known to take up and store but not make the glycoprotein. (wikipedia.org)
  • The heximer is transferred to the Golgi where it is glycosylated, hydroxylated, sulfated, and phosphorylated to form the mature fibrinogen glycoprotein that is secreted into the blood. (wikipedia.org)
  • Fibrinogen, also known as factor I, is a naturally occurring blood plasma glycoprotein. (octapharma.com)
  • Fibrinogen is a high molecular weight soluble glycoprotein that is produced by the liver. (truthwiki.org)
  • A growing body of evidence has identified fibrinogen as an important risk factor for cardiovascular disease, the major cause of death in the U.S. The objective of including this measure was to provide data on laboratory, clinical, and socio-demographic correlates of fibrinogen levels. (cdc.gov)
  • Numerous studies have shown that elevated levels of fibrinogen are a significant risk factor for cardiovascular disease. (truthwiki.org)
  • Elevated fibrinogen levels are considered to be as much of a serious a risk factor for cardiovascular disease as hypertension, cigarette smoking, and diabetes. (truthwiki.org)
  • Fibrinogen concentrations has also been shown to enable a more precise diagnosis of the severity of an inflammation than that based simply on clinical conditions in respiratory diseases, particularly bacterial pneumonia. (quickvet.net)
  • these conditions are treated by supplementing blood fibrinogen levels and inhibiting blood clotting, respectively. (wikipedia.org)
  • Elevated levels of fibrinogen in inflammation as well as cancer and other conditions have been suggested to be the cause of thrombosis and vascular injury that accompanies these conditions. (wikipedia.org)
  • Of particular importance in NHANES, the data can be used to study the relationship between fibrinogen levels and clinically measured lower extremity arterial blood flow as assessed by the Ankle-Brachial Index in the Lower Extremity Disease component. (cdc.gov)
  • A randomized, double-blind, placebo-controlled trial showed a statistically significant reduction in fibrinogen levels using ticlopidine (Ticlid) in 37 patients suffering from polycythemia vera and related hyperfibrinogenemia ( Acta Haematol . (clinicaladvisor.com)
  • It is based upon a Sandwich assay principle and can be used to detect levels of FGG / Fibrinogen Gamma as low as 9.375 nanograms per millilter. (lsbio.com)
  • The objective of this retrospective study was to clarify the potential prognostic significance of pre-therapeutic fibrinogen levels in head and neck squamous cell carcinoma (HNSCC) patients treated with curative intent by primary radiotherapy (RT) or with postoperative radiotherapy (PORT). (springermedizin.at)
  • The most relevant observation was that plasma fibrinogen levels were significantly associated with a reduction of overall survival rates. (springermedizin.at)
  • His plasma fibrinogen levels were found to be decreased to 85 mg/dL (normal range 215-464). (escholarship.org)
  • Despite the extensive research there is still some debate among experts as to whether or not elevated levels of fibrinogen actually cause health problems. (truthwiki.org)
  • Because elevated levels of fibrinogen could also be the result of other pathological conditions, it is unclear as to exactly how harmful excessive fibrinogen is to the body. (truthwiki.org)
  • Fibrinogen levels are elevated in times of stress. (truthwiki.org)
  • Unfortunately chronic stress tends to promote excessive fibrinogen levels. (truthwiki.org)
  • Excessive fibrinogen levels are likely to lead to a number of health problems, though this has yet to be proven irrefutably. (truthwiki.org)
  • However when people are subject to chronic stress the resulting excessive fibrinogen levels are likely to cause serious harm to the body's cardiovascular system, and possibly disrupt the normal function of other important physiological systems. (truthwiki.org)
  • It is not uncommon in horses to have increased plasma fibrinogen levels as the sole indicator of inflammation. (quickvet.net)
  • Levels of serum amyloid A, fibrinogen and iron reflects the intensity of the surgical trauma, where as WBC do not do this. (quickvet.net)
  • Horses with equine influenza and herpes virus 2 has been proven to show elevated fibrinogen levels 3 days post infection. (quickvet.net)
  • Parasitized (Strongelus Vulgaris) ponies showed in a study to have significantly elevated fibrinogen levels compared to a control group 9, 14, 21 and 45 days after infection. (quickvet.net)
  • Elevated fibrinogen levels increase the risk of blood clots, which can, in turn, contribute to an increased risk of heart disease. (yycnewcentrallibrary.com)
  • Fibrinogen levels drop as a result of traumatic injuries and blood loss, liver disease, leukemia, certain medications, or genetic disorders. (yycnewcentrallibrary.com)
  • Levels of fibrinogen increase in inflammatory states as part of the acute-phase response. (yycnewcentrallibrary.com)
  • A consistent body of observational evidence links elevated levels of fibrinogen with cardiovascular risk. (yycnewcentrallibrary.com)
  • Levels of fibrinogen in the blood can be detected with the use of a blood test which can also be used to look at levels of other clotting agents and substances in the blood. (yycnewcentrallibrary.com)
  • Low levels of fibrinogen are associated with bleeding most commonly secondary to liver disease or Disseminated Intravascular Coagulation (DIC). (yycnewcentrallibrary.com)
  • Fibrinogen is an acute phase reactant and thus elevated levels may be associated with inflammation. (yycnewcentrallibrary.com)
  • Fibrinogen levels are typically also tested as part of the DIC panel ( fibrin , fibrin monomer, platelet, prothrombin time [PT], partial thromboplastin time [PTT], international normalized ratio for prothrombin time, D-dimer ). (medscape.com)
  • Hypofibrinogenemia is a condition characterized by decreased levels of fibrinogen in the blood. (medlineplus.gov)
  • Compared to non-smokers, smokers had a significantly higher baseline WBC count, but comparable levels of CRP and fibrinogen. (cdc.gov)
  • A significant decrease in fibrinogen levels was observed in non-smokers (-32 mg/dl, 95% CI -63 to -1). (cdc.gov)
  • No significant changes in WBC, neutrophil, and fibrinogen levels were found in smokers. (cdc.gov)
  • fibrinogen levels. (cdc.gov)
  • QZBFBY18-4, a specific fibrinogen degradation product ELISA can be made. (biovendor.com)
  • Stimulation of fibrinogen synthesis in cultured rat hepatocytes by fibrinogen degradation product fragment D Proc Natl Acad Sci U S A. 1989 Nov;86(22):8788-92. (moleculardepot.com)
  • The conversion of fibrinogen to fibrin at the surface of curliated E. coli bacteria leads to the generation of proinflammatory fibrinopeptides. (lu.se)
  • A snake venom that directly activates fibrinogen by cleaving fibrinopeptide A is used as a reagent in the reptilase time test. (medscape.com)
  • Language": "en", "Country": "XG", "Code": "Storage Conditions (Product)" }, { "Name": "Content", "Value": "FITC anti-Fibrinogen contains sufficient reagent for 50 tests. (roche.com)
  • This reagent should be used in conjunction with a panel of antibodies to aid in the identification of fibrinogen in target tissue (e.g., in the diagnosis of renal or dermal pathologies). (roche.com)
  • The Fibrinogen Elisa Macfa reagent is RUO (Research Use Only) to test human serum or cell culture lab samples. (gentaur-online.com)
  • Previous studies showed that fibrinogen-to-albumin ratio (FAR) regarded as a novel inflammatory and thrombotic biomarker was the risk factor for coronary artery disease (CAD). (hindawi.com)
  • We conclude from these results that elevated pre-therapeutic fibrinogen may serve as a biomarker associated with worsened prognosis in locally advanced head and neck cancer patients treated by either RT or surgery followed by adjuvant radiotherapy. (springermedizin.at)
  • The Fibrinogen Antigen, Nephelometry test contains 1 test with 1 biomarker. (yycnewcentrallibrary.com)
  • Although a coagulation profile (prothrombin time [PT], activated partial thromboplastin time [aPTT], and fibrinogen) should also be evaluated, its clinical value is unclear when the platelet count is 100,000/mm 3 or more with no evidence of bleeding. (medscape.com)
  • Hence, the final fibrinogen product is composed principally of Aα, Bβ, and γ chains with a small percentage of it containing AαE and/or γ' chains in place of Aα and/or γ chains, respectively. (wikipedia.org)
  • 7: Van Ruijven-Vermeer IA, Nieuwenhuizen W. Purification of rat_fibrinogen and its constituent chains Biochem J. 1978 Mar 1;169(3):653-8. (moleculardepot.com)
  • To form fibrinogen, the γ chain attaches to the fibrinogen A alpha (Aα) and fibrinogen B beta (Bβ) chains, each produced from different genes. (medlineplus.gov)
  • The coordinated transcription of these three fibrinogen genes is rapidly and greatly increased by systemic conditions such as inflammation and tissue injury. (wikipedia.org)
  • Experimentally induced aseptically inflammation showed a significant increase in fibrinogen with a maximum level 3 - 6 days post-injections. (quickvet.net)
  • Why fibrinogen is high in inflammation? (yycnewcentrallibrary.com)
  • 3: Uzan G, Courtois G, Stanckovic Z, Crabtree GR, Marguerie G. Expression of the fibrinogen_ genes in rat megakaryocytes Biochem Biophys Res Commun. (moleculardepot.com)
  • 5: Kant JA, Crabtree GR. The rat fibrinogen genes. (moleculardepot.com)
  • Fibrinogen is made and secreted into the blood primarily by liver hepatocyte cells. (wikipedia.org)
  • In patient news, I became aware of two more families affected by fibrinogen amyloidosis in 2020, and I know of one combined liver and kidney transplant that occurred in the US. (fibrinogenamyloidosis.com)
  • Recently, numerous studies have shown that the fibrinogen-to-albumin ratio (FAR) does not only have a high prognostic value in certain types of cancer including gastric, colorectal, and gallbladder cancer [ 8 - 10 ] but also have an association with the presence and poor clinical outcome of cardiovascular disease [ 11 - 14 ]. (hindawi.com)
  • Greetings, loyal readers of the Fibrinogen Amyloidosis blog. (fibrinogenamyloidosis.com)
  • There have been a few articles published in the past couple of years specifically about fibrinogen amyloidosis, although at a glance they do not seem to have any significant developments with regard to treatment. (fibrinogenamyloidosis.com)
  • Fass environmental information for fibrinogen (Fibryga, Riastap and Tachosil) from Octapharma, CSL Behring and Takeda Pharma respectively. (janusinfo.se)
  • Select this product for Molecular Innovations name, Human Fibrinogen and product number, FIB . (innov-research.com)
  • Fibrinogen Elisa Laboratories manufactures the fibrinogen elisa macfa reagents distributed by Genprice. (gentaur-online.com)
  • Startseite Dialine Hemostasis Reagents CNBr Fibrinogen fragments, lyo. (dialine.ch)
  • In their study, published in the scientific journal Neuron , the researchers found that fibrinogen, after leaking from the blood into the brain, activates the brain's immune cells and triggers them to destroy important connections between neurons. (news-medical.net)
  • 6 FITC anti-Fibrinogen binds specifically with human fibrinogen and its degradation products. (roche.com)
  • [ 1 ] Dysfibrinogenemia is a qualitative defect in fibrinogen (type II) marked by functional abnormalities of fibrinogen who carry one abnormal allele that may result in either bleeding or thrombosis. (medscape.com)
  • [ 6 ] Therefore, disorders of fibrinogen may be associated with either a bleeding or a thrombotic predisposition. (medscape.com)
  • Fibrinogen and thrombotic disease. (springermedizin.at)
  • The primary physiologic role of fibrinogen is in hemostasis. (medscape.com)
  • In 2017, Octapharma started discussing another study using Octapharma's high-purity human fibrinogen concentrate in cardiac surgery with a group of Canadian physicians led by Dr Keyvan Karkouti in Toronto. (octapharma.com)
  • 2017. https://nursing.unboundmedicine.com/nursingcentral/view/Davis-Lab-and-Diagnostic-Tests/425342/all/Fibrinogen_Degradation_Products. (unboundmedicine.com)
  • 5 Immunofluorescent detection of fibrinogen in human renal tissue has been previously documented. (roche.com)
  • Fibrinogen is the clotting element present in blood . (wikipedia.org)
  • When blood comes out of a wound in a vessel, the fibrinogen is activated and forms fibrin , which clots the blood. (wikipedia.org)
  • It is possible to examine a small sample of a person's blood to find out how much fibrinogen is in the blood. (wikipedia.org)
  • Fibrinogen is an essential blood-clotting factor and is involved in a range of other functions, including platelet aggregation and smooth muscle proliferation. (cdc.gov)
  • Risk factors for heart disease examined included blood pressure, lipids, fibrinogen, and plasma viscosity. (bmj.com)
  • Fibrinogen is necessary for normal blood platelet functions and it is also needed in order to heal wounds. (truthwiki.org)
  • Fibrinogen plays an important role in blood clotting, and without a doubt some amount of Fibrinogen is necessary to form blood clots. (truthwiki.org)
  • Fibrinogen increases blood viscosity and coaguability. (truthwiki.org)
  • Fibrinogen serves a survival purpose of inhibiting blood loss from minor injuries in dangerous situations. (truthwiki.org)
  • The fibrinogen content of the blood plasma is 0.2 to 0.4 percent. (britannica.com)
  • Fibrinogen can be precipitated from the blood plasma by half-saturation with sodium chloride . (britannica.com)
  • When your fibrinogen is low, your body can't create blood clots and heal injuries. (yycnewcentrallibrary.com)
  • Blood transfusions within the past month may affect fibrinogen test results. (yycnewcentrallibrary.com)
  • This test measures the amount of fibrinogen in the blood. (yycnewcentrallibrary.com)
  • Normal fibrinogen activity results usually reflect normal blood-clotting ability. (medscape.com)
  • Generally, the less fibrinogen in the blood, the more severe the bleeding problems are. (medlineplus.gov)
  • The ambitious goal of this programme was to show that our high-purity human fibrinogen concentrate is at least as effective as cryoprecipitate for AFD - and is a more practical and reliable alternative to it. (octapharma.com)
  • Eight years on, and after the detailed design, planning and conduct of clinical trials by a dedicated Octapharma team, our high-purity human fibrinogen concentrate has now been approved for use in AFD in 15 countries of the EU. (octapharma.com)
  • Members of the dedicated Octapharma human fibrinogen concentrate team. (octapharma.com)
  • The FORMA-05 clinical study was a prospective, randomised, single-blind, controlled, non-inferiority study which compared the efficacy of Octapharma's high-purity human fibrinogen concentrate to that of cryoprecipitate during cytoreductive surgery to treat pseudomyxoma peritonei, a rare cancer that usually starts in the appendix. (octapharma.com)
  • Human Fibrinogen Purified from Innovative Research has been purified from human plasma by a propritetary process that combines multiple conventional chromatographic methods. (innov-research.com)
  • Fibrinogen in rat gastrointestinal lymph before, during and after intraduodenal administration of emulsified triglyceride: fibrinogen bound to chylomicrons in gastrointestinal lymph is functional Thromb Res. (moleculardepot.com)
  • 6: Hirose S, Oda K, Ikehara Y. Biosynthesis, assembly and secretion of fibrinogen_ in cultured rat hepatocytes Biochem J. 1988 Apr 15;251(2):373-7. (moleculardepot.com)
  • Determining the fibrinogen level of a horse quantitatively with high precision is now possible directly at the patient side or in your clinic. (quickvet.net)