Antithrombin iii. Medical search

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.

An absence or reduced level of Antithrombin III leading to an increased risk for thrombosis.

Endogenous factors and drugs that directly inhibit the action of THROMBIN, usually by blocking its enzymatic activity. They are distinguished from INDIRECT THROMBIN INHIBITORS, such as HEPARIN, which act by enhancing the inhibitory effects of antithrombins.

A highly acidic mucopolysaccharide formed of equal parts of sulfated D-glucosamine and D-glucuronic acid with sulfaminic bridges. The molecular weight ranges from six to twenty thousand. Heparin occurs in and is obtained from liver, lung, mast cells, etc., of vertebrates. Its function is unknown, but it is used to prevent blood clotting in vivo and vitro, in the form of many different salts.

An endogenous family of proteins belonging to the serpin superfamily that neutralizes the action of thrombin. Six naturally occurring antithrombins have been identified and are designated by Roman numerals I to VI. Of these, Antithrombin I (see FIBRIN) and ANTITHROMBIN III appear to be of major importance.

An enzyme formed from PROTHROMBIN that converts FIBRINOGEN to FIBRIN.

Activated form of factor X that participates in both the intrinsic and extrinsic pathways of blood coagulation. It catalyzes the conversion of prothrombin to thrombin in conjunction with other cofactors.

Storage-stable glycoprotein blood coagulation factor that can be activated to factor Xa by both the intrinsic and extrinsic pathways. A deficiency of factor X, sometimes called Stuart-Prower factor deficiency, may lead to a systemic coagulation disorder.

The process of the interaction of BLOOD COAGULATION FACTORS that results in an insoluble FIBRIN clot.

A sulfated plasma protein with a MW of approximately 66kDa that resembles ANTITHROMBIN III. The protein is an inhibitor of thrombin in plasma and is activated by dermatan sulfate or heparin. It is a member of the serpin superfamily.

A plasma protein that is the inactive precursor of thrombin. It is converted to thrombin by a prothrombin activator complex consisting of factor Xa, factor V, phospholipid, and calcium ions. Deficiency of prothrombin leads to hypoprothrombinemia.

Exogenous or endogenous compounds which inhibit SERINE ENDOPEPTIDASES.

A vitamin-K dependent zymogen present in the blood, which, upon activation by thrombin and thrombomodulin exerts anticoagulant properties by inactivating factors Va and VIIIa at the rate-limiting steps of thrombin formation.

Laboratory tests for evaluating the individual's clotting mechanism.

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.

Agents that prevent clotting.

Endogenous substances, usually proteins, that are involved in the blood coagulation process.

Inflammation of a vein associated with a blood clot (THROMBUS).

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.

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.

An absence or deficiency in PROTEIN C which leads to impaired regulation of blood coagulation. It is associated with an increased risk of severe or premature thrombosis. (Stedman's Med. Dict., 26th ed.)

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.

A disorder of HEMOSTASIS in which there is a tendency for the occurrence of THROMBOSIS.

An autosomal dominant disorder showing decreased levels of plasma protein S antigen or activity, associated with venous thrombosis and pulmonary embolism. PROTEIN S is a vitamin K-dependent plasma protein that inhibits blood clotting by serving as a cofactor for activated PROTEIN C (also a vitamin K-dependent protein), and the clinical manifestations of its deficiency are virtually identical to those of protein C deficiency. Treatment with heparin for acute thrombotic processes is usually followed by maintenance administration of coumarin drugs for the prevention of recurrent thrombosis. (From Harrison's Principles of Internal Medicine, 12th ed, p1511; Wintrobe's Clinical Hematology, 9th ed, p1523)

Single-chain polypeptides of about 65 amino acids (7 kDa) from LEECHES that have a neutral hydrophobic N terminus, an acidic hydrophilic C terminus, and a compact, hydrophobic core region. Recombinant hirudins lack tyr-63 sulfation and are referred to as 'desulfato-hirudins'. They form a stable non-covalent complex with ALPHA-THROMBIN, thereby abolishing its ability to cleave FIBRINOGEN.

A reagent used mainly to induce experimental liver cancer. According to the Fourth Annual Report on Carcinogens (NTP 85-002, p. 89) published in 1985, this compound "may reasonably be anticipated to be a carcinogen." (Merck, 11th ed)

The vitamin K-dependent cofactor of activated PROTEIN C. Together with protein C, it inhibits the action of factors VIIIa and Va. A deficiency in protein S; (PROTEIN S DEFICIENCY); can lead to recurrent venous and arterial thrombosis.

Activated form of factor IX. This activation can take place via the intrinsic pathway by the action of factor XIa and calcium, or via the extrinsic pathway by the action of factor VIIa, thromboplastin, and calcium. Factor IXa serves to activate factor X to Xa by cleaving the arginyl-leucine peptide bond in factor X.

Formation and development of a thrombus or blood clot in the blood vessel.

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.

The rate dynamics in chemical or physical systems.

An enzyme of the isomerase class that catalyzes the eliminative cleavage of polysaccharides containing 1,4-linked D-glucuronate or L-iduronate residues and 1,4-alpha-linked 2-sulfoamino-2-deoxy-6-sulfo-D-glucose residues to give oligosaccharides with terminal 4-deoxy-alpha-D-gluc-4-enuronosyl groups at their non-reducing ends. (From Enzyme Nomenclature, 1992) EC 4.2.2.7.

Plasma glycoprotein member of the serpin superfamily which inhibits TRYPSIN; NEUTROPHIL ELASTASE; and other PROTEOLYTIC ENZYMES.

Immunoelectrophoresis in which a second electrophoretic transport is performed on the initially separated antigen fragments into an antibody-containing medium in a direction perpendicular to the first electrophoresis.

Colorless, endogenous or exogenous pigment precursors that may be transformed by biological mechanisms into colored compounds; used in biochemical assays and in diagnosis as indicators, especially in the form of enzyme substrates. Synonym: chromogens (not to be confused with pigment-synthesizing bacteria also called chromogens).

A sulfated pentosyl polysaccharide with heparin-like properties.

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 naturally occurring glycosaminoglycan found mostly in the skin and in connective tissue. It differs from CHONDROITIN SULFATE A (see CHONDROITIN SULFATES) by containing IDURONIC ACID in place of glucuronic acid, its epimer, at carbon atom 5. (from Merck, 12th ed)

Heat- and storage-labile plasma glycoprotein which accelerates the conversion of prothrombin to thrombin in blood coagulation. Factor V accomplishes this by forming a complex with factor Xa, phospholipid, and calcium (prothrombinase complex). Deficiency of factor V leads to Owren's disease.

Coagulant substances inhibiting the anticoagulant action of heparin.

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.

A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)

Carbohydrates consisting of between two (DISACCHARIDES) and ten MONOSACCHARIDES connected by either an alpha- or beta-glycosidic link. They are found throughout nature in both the free and bound form.

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.

Activated form of factor XI. In the intrinsic pathway, Factor XI is activated to XIa by factor XIIa in the presence of cofactor HMWK; (HIGH MOLECULAR WEIGHT KININOGEN). Factor XIa then activates factor IX to factor IXa in the presence of calcium.

The parts of a macromolecule that directly participate in its specific combination with another molecule.

Serum proteins that inhibit, antagonize, or inactivate COMPLEMENT C1 or its subunits.

Glycoproteins with a molecular weight of approximately 620,000 to 680,000. Precipitation by electrophoresis is in the alpha region. They include alpha 1-macroglobulins and alpha 2-macroglobulins. These proteins exhibit trypsin-, chymotrypsin-, thrombin-, and plasmin-binding activity and function as hormonal transporters.

A heteropolysaccharide that is similar in structure to HEPARIN. It accumulates in individuals with MUCOPOLYSACCHARIDOSIS.

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 natural enzymatic dissolution of FIBRIN.

Compounds which inhibit or antagonize biosynthesis or actions of proteases (ENDOPEPTIDASES).

An order of wholly aquatic MAMMALS occurring in all the OCEANS and adjoining seas of the world, as well as in certain river systems. They feed generally on FISHES, cephalopods, and crustaceans. Most are gregarious and most have a relatively long period of parental care and maturation. Included are DOLPHINS; PORPOISES; and WHALES. (From Walker's Mammals of the World, 5th ed, pp969-70)

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.

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.

Extracellular protease inhibitors that are secreted from FIBROBLASTS. They form a covalent complex with SERINE PROTEASES and can mediate their cellular internalization and degradation.

A family of serine proteinase inhibitors which are similar in amino acid sequence and mechanism of inhibition, but differ in their specificity toward proteolytic enzymes. This family includes alpha 1-antitrypsin, angiotensinogen, ovalbumin, antiplasmin, alpha 1-antichymotrypsin, thyroxine-binding protein, complement 1 inactivators, antithrombin III, heparin cofactor II, plasminogen inactivators, gene Y protein, placental plasminogen activator inhibitor, and barley Z protein. Some members of the serpin family may be substrates rather than inhibitors of SERINE ENDOPEPTIDASES, and some serpins occur in plants where their function is not known.

Heteropolysaccharides which contain an N-acetylated hexosamine in a characteristic repeating disaccharide unit. The repeating structure of each disaccharide involves alternate 1,4- and 1,3-linkages consisting of either N-acetylglucosamine or N-acetylgalactosamine.

Stable blood coagulation factor involved in the intrinsic pathway. The activated form XIa activates factor IX to IXa. Deficiency of factor XI is often called hemophilia C.

Storage-stable blood coagulation factor acting in the intrinsic pathway. Its activated form, IXa, forms a complex with factor VIII and calcium on platelet factor 3 to activate factor X to Xa. Deficiency of factor IX results in HEMOPHILIA B (Christmas Disease).

Activated form of factor VII. Factor VIIa activates factor X in the extrinsic pathway of blood coagulation.

Heparin derivatives. The term has also been used more loosely to include naturally occurring and synthetic highly-sulphated polysaccharides of similar structure. Heparinoid preparations have been used for a wide range of applications including as anticoagulants and anti-inflammatories and they have been claimed to have hypolipidemic properties. (From Martindale, The Extra Pharmacopoeia, 30th, p232)

Inflammation of a vein, often a vein in the leg. Phlebitis associated with a blood clot is called (THROMBOPHLEBITIS).

Amidines substituted with a benzene group. Benzamidine and its derivatives are known as peptidase inhibitors.

7-Hydroxycoumarins. Substances present in many plants, especially umbelliferae. Umbelliferones are used in sunscreen preparations and may be mutagenic. Their derivatives are used in liver therapy, as reagents, plant growth factors, sunscreens, insecticides, parasiticides, choleretics, spasmolytics, etc.

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.

Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.

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.

Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).

A protein derived from FIBRINOGEN in the presence of THROMBIN, which forms part of the blood clot.

A hemostatic disorder characterized by a poor anticoagulant response to activated protein C (APC). The activated form of Factor V (Factor Va) is more slowly degraded by activated protein C. Factor V Leiden mutation (R506Q) is the most common cause of APC resistance.

The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).

The sum of the weight of all the atoms in a molecule.

Obstruction of a blood vessel (embolism) by a blood clot (THROMBUS) in the blood stream.

Compounds that contain a 1-dimethylaminonaphthalene-5-sulfonyl group.

A family of proteinase-activated receptors that are specific for THROMBIN. They are found primarily on PLATELETS and on ENDOTHELIAL CELLS. Activation of thrombin receptors occurs through the proteolytic action of THROMBIN, which cleaves the N-terminal peptide from the receptor to reveal a new N-terminal peptide that is a cryptic ligand for the receptor. The receptors signal through HETEROTRIMERIC GTP-BINDING PROTEINS. Small synthetic peptides that contain the unmasked N-terminal peptide sequence can also activate the receptor in the absence of proteolytic activity.

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.

Constituent composed of protein and phospholipid that is widely distributed in many tissues. It serves as a cofactor with factor VIIa to activate factor X in the extrinsic pathway of blood coagulation.

Pregnane derivatives containing two double bonds anywhere within the ring structures.

The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.

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.

Any member of the group of ENDOPEPTIDASES containing at the active site a serine residue involved in catalysis.

Proteins prepared by recombinant DNA technology.

Sperm chemotaxis. (1/874)

Communication between spermatozoa and egg before contact by chemotaxis appears to be prevalent throughout the animal kingdom. In non-mammalian species, sperm chemotaxis to factors secreted from the egg is well documented. In mammals, sperm chemotaxis to follicular factors in vitro has been established in humans and mice. The attractants of female origin in non-mammalian species are heat-stable peptides or proteins of various sizes, or other small molecules, depending on the species. Species specificity of the attractants in non-mammalian species may vary from high species specificity, through specificity to families with no specificity within a family, to absence of specificity. The mammalian sperm attractants have not been identified but they appear to be heat-stable peptides. The claim that progesterone is the attractant for human spermatozoa has failed to be substantiated, neither have claims for other mammalian sperm attractants been verified. The molecular mechanism of sperm chemotaxis is not known. Models involving modulation of the intracellular Ca2+ concentration have been proposed for both mammalian and non-mammalian sperm chemotaxis. The physiological role of sperm chemotaxis in non-mammalian species appears to differ from that in mammals. In non-mammalian species, sperm chemotaxis strives to bring as many spermatozoa as possible to the egg. However, in mammals, the role appears to be recruitment of a selective population of capacitated ('ripe') spermatozoa to fertilize the egg. (+info)

Age-related changes in blood coagulation and fibrinolysis in mice fed on a high-cholesterol diet. (2/874)

To investigate the pathogenesis of hyperlipidemia-induced atherosclerosis, we examined age-dependent changes in platelet activity, blood coagulation and fibrinolysis in susceptibility to a high cholesterol diet (HCD) feeding in male ICR mice. Pretreatment of platelet-rich-plasma from HCD feeding mice for 3 days with epinephrine (300 microM) resulted in a marked enhancement of adenosine 5'-diphosphate (ADP: 0.1 microM) or collagen (0.7 microgram/ml)-stimulated aggregation compared with the same in control mice. Yohimbine as alpha 2-adrenergic blocker antagonized these aggregations in a dose-dependent manner. A significant increase in plasma total cholesterol and VLDL (very low-density lipoprotein)-LDL (low-density lipoprotein)-cholesterol and the liver/body weight ratio was observed in mice fed on HCD for 3 months (3-month HCD mice). In the early phase of this experiment, a significant increase in fibrinogen was observed. In the middle phase, increases in the activity of antithrombin III (ATIII) and alpha 2-plasmin inhibitor (alpha 2-Pl) followed. Plasminogen content gradually decreased in both normal diet and HCD mice throughout the experiment. The activity of plasminogen activator inhibitor (PAI) decreased in 3-month HCD mice. Morphological observation of the aortic arch from 3-month HCD mice revealed apparent atheromatous plaques not seen in control mice. These results suggest that 3-month HCD mice can be a convenient hyperlipidemia-induced atherosclerotic model and the changes in platelet activity, coagulation and fibrinolysis in the early phase may be a cause of pathologic changes in this model. (+info)

Single and combined prothrombotic factors in patients with idiopathic venous thromboembolism: prevalence and risk assessment. (3/874)

The inherited thrombophilias--deficiencies of protein C, protein S, and antithrombin III--and the prothrombotic polymorphisms factor V G1691A and factor II G20210A predispose patients toward venous thromboembolism (VTE). The aim of this study was to determine the prevalence of single and combined prothrombotic factors in patients with idiopathic VTE and to estimate the associated risks. The study group consisted of 162 patients referred for work-up of thrombophilia after documented VTE. The controls were 336 consecutively admitted patients. In all subjects factor V G1691A, factor II G20210A, and methylenetetrahydrofolate reductase (MTHFR) C677T were analyzed by specific polymerase chain reactions and restriction enzymes. Activities of antithrombin III and protein C, free protein S antigen, and lupus anticoagulant were determined in a subset of 109 patients who were not receiving oral anticoagulants. The prevalences of heterozygotes and homozygotes for factor V G1691A and factor II G20210A among patients and controls were 40.1% versus 3.9% and 18.5% versus 5.4%, respectively (P=0.0001). The prevalence of homozygotes for MTHFR C677T in patients was 22.8% and in controls, 14.3% (P=0.025). Heterozygous and homozygous factor V G1691A, factor II G20210A, and homozygous MTHFR C677T were found to be independent risk factors for VTE, with odds ratios of 16.3, 3.6, and 2.1, respectively. Two or more polymorphisms were detected in 27 of 162 patients (16.7%) and in 3 of 336 controls (0.9%). Logistic regression analysis disclosed odds ratios of 58.6 (confidence interval [CI], 22.1 to 155.2) for joint occurrence of factor V and factor II polymorphisms, of 35.0 (CI, 14.5 to 84.7) for factor V and MTHFR polymorphisms, and of 7.7 (CI, 3.0 to 19.6) for factor II and MTHFR polymorphisms. Among 109 patients in whom a complete thrombophilic work-up was performed, 74% had at least 1 underlying defect. These data indicate that in most patients referred for evaluation of thrombophilia due to idiopathic VTE, 1 or more underlying genetic predispositions were discernible. The presence of >1 of the prothrombotic polymorphisms was associated with a substantial risk of VTE. (+info)

Oxidation of methionine residues in antithrombin. Effects on biological activity and heparin binding. (4/874)

Commercially available human plasma-derived preparations of the serine protease inhibitor antithrombin (AT) were shown to contain low levels of oxidation, and we sought to determine whether oxidation might be a means of regulating the protein's inhibitory activity. A recombinant form of AT, with similarly low levels of oxidation as purified, was treated with hydrogen peroxide in order to study the effect of oxidation, specifically methionine oxidation, on the biochemical properties of this protein. AT contains two adjacent methionine residues near the reactive site loop cleaved by thrombin (Met314 and Met315) and two exposed methionines that border on the heparin binding region of AT (Met17 and Met20). In forced oxidations with hydrogen peroxide, the methionines at 314 and 315 were found to be the most susceptible to oxidation, but their oxidation did not affect either thrombin-inhibitory activity or heparin binding. Methionines at positions 17 and 20 were significantly oxidized only at higher concentrations of peroxide, at which point heparin affinity was decreased. However at saturating heparin concentrations, activity was only marginally decreased for these highly oxidized samples of AT. Structural studies indicate that highly oxidized AT is less able to undergo the complete conformational change induced by heparin, most probably due to oxidation of Met17. Since this does not occur in less oxidized, and presumably more physiologically relevant, forms of AT such as those found in plasma preparations, oxidation does not appear to be a means of controlling AT activity. (+info)

Dose response of intravenous heparin on markers of thrombosis during primary total hip replacement. (5/874)

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

Effect of thrombin inhibition in vascular dementia and silent cerebrovascular disease. An MR spectroscopy study. (6/874)

BACKGROUND AND PURPOSE: Silent cerebrovascular disease (CVD) has been proposed as a predisposing condition for clinically overt stroke and vascular dementia. Recently, we found increased thrombin generation in silent CVD patients. Here, we report the effect of thrombin inhibition using a potent selective thrombin inhibitor on the cerebral metabolism and function in peripheral arterial occlusive disease (PAOD) patients with or without silent CVD. METHODS: We examined 17 mild chronic PAOD patients, including 2 cases of vascular dementia. We divided the patients into 2 groups: 1 was the advanced CVD group with multiple lacunar infarction and/or advanced periventricular hyperintensity detected by brain MRI (n=12), and the other was the no CVD group that had none of these abnormalities (n=5). We assessed the cerebral biochemical compounds in the deep white matter area and cerebellar hemisphere (8 cm3) by proton MR spectroscopy before and after infusion of argatroban (10 mg/d IV) over 2 hours for 7 days. RESULTS: The ratio of N-acetylasparate (NAA) to total creatine (Cre) in the deep white matter area was significantly lower in the advanced CVD group than in the no CVD group, whereas there were no significant differences in this ratio in the cerebellar hemisphere between the 2 groups. In the former group, this decreased NAA/Cre ratio significantly increased after argatroban therapy, whereas there was no change in the latter group. The 2 patients with vascular dementia showed clinical improvement with marked increases in the NAA/Cre ratio and mini-mental score. CONCLUSIONS: These results suggest that increased thrombin generation may have some pathophysiological roles in developing vascular dementia and its chronic predisposing conditions. Thrombin inhibition may break this vicious cycle and lead to clinical improvement. (+info)

Comparison of the antithrombotic effect of PEG-hirudin and heparin in a human ex vivo model of arterial thrombosis. (7/874)

Polyethylene glycol (PEG)-hirudin is a derivative of hirudin with a long plasma half-life. We have compared the efficacy of PEG-hirudin with unfractionated heparin (UH) in preventing arterial thrombosis. Arterial thrombus formation was induced ex vivo in 12 healthy human volunteers by exposing a tissue factor-coated coverslip positioned in a parallel-plate perfusion chamber to flowing nonanticoagulated human blood drawn directly from an antecubital vein at an arterial wall shear rate of 2600 s-1 for 3.5 minutes. PEG-hirudin, UH, or saline (as control) were administered ex vivo through a heparin-coated mixing device positioned proximal to the perfusion chamber. Platelet and fibrin deposition was quantified by immunoenzymatic measure of the P-selectin and D-dimer content of dissolved plasmin-digested thrombi, respectively. UH was administered to a plasma concentration of 0.35 IU/mL. This concentration prolonged the activated partial thromboplastin time from 32+/-1 seconds to 79+/-4 seconds (P<0.01). UH did not significantly prevent platelet deposition. However, fibrin deposition was reduced by 39% (P<0.05). PEG-hirudin in plasma concentrations of 0.5, 2.5, and 5 microg/mL prolonged the activated partial thromboplastin time to 48+/-2, 87+/-4, and 118+/-4 seconds, respectively. In contrast to UH, PEG-hirudin prevented both platelet and fibrin deposition in a dose-dependent manner with a >80% reduction at 5 microg/mL (P<0.01). Furthermore, the plasma level of PEG-hirudin required to significantly prevent fibrin deposition (0.5 microg/mL) corresponded to a much shorter prolongation of activated partial thromboplastin time (48+/-2 seconds) than that needed for UH (79+/-4 seconds). Thus, our results are compatible with the view that thrombin is greatly involved in recruitment of platelets in evolving thrombi, and that PEG-hirudin is an effective agent for preventing arterial thrombosis in a human ex vivo experimental model. (+info)

Prognostic significance of elevated hemostatic markers in patients with acute myocardial infarction. (8/874)

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

Some examples of heparin binding proteins include antithrombin III. It is thought that much protein interaction with heparin is ... 3 (5984): 614-6. doi:10.1136/bmj.3.5984.614. JSTOR 20406780. PMC 1674425. PMID 51664. Rutjes, Anne W.S.; Jüni, Peter; Da Costa ... 157 (3): 180-91. doi:10.7326/0003-4819-157-3-201208070-00473. PMID 22868835. S2CID 5660398. Linhardt, Robert J.; Toida, ... ISBN 0-8247-9982-8. {{U.S. Pharmacopeia Heparin Stage Two Monograph Revisions Open Microphone Web Meeting March 3, 2009 ...

https://en.wikipedia.org/wiki/Heparinoid

After the antithrombin III binds to Factor Xa, the Fondaparinux is released and can activate another antithrombin. Another drug ... Fondaparinux binds to antithrombin III and activates the molecule for Factor Xa inhibition. In fact, Fondaparinux imparts an ... Idraparinux also binds antithrombin III, however with a 30-fold increase in affinity as compared to Fondaparinux. Idraparinux ... Factor Xa is inhibited by the antithrombin III/heparin system, which also acts to inhibit thrombin. Deficiencies of either ...

https://en.wikipedia.org/wiki/Prothrombinase

Kiehl R, Hellstern P, Wenzel E (January 1987). "Hereditary antithrombin III (AT III) deficiency and atypical localization of a ... and antithrombin III deficiency. Although the above hypothesis is the most commonly accepted, others believe that it is a ... Warfarin necrosis usually occurs three to five days after drug therapy is begun, and a high initial dose increases the risk of ... which usually occurs three to eight weeks after the start of anticoagulation therapy. No report has described this disorder in ...

https://en.wikipedia.org/wiki/Warfarin_necrosis

Dalteparin acts by potentiating the activity of antithrombin III, inhibiting formation of both Factor Xa and thrombin. It is ...

https://en.wikipedia.org/wiki/Dalteparin_sodium

Use in antithrombin III deficiency FFP can be used as a source of antithrombin III in patients who are deficient of this ... There are purified, human derived, as well as recombinant forms of antithrombin III available in the US. Treatment of ... 31 (3): 149-338. doi:10.1002/jca.21470. ISSN 0733-2459. PMID 27322218. S2CID 866923. Sikka, Paul K.; Beaman, Shawn T.; Street, ... 154 (3): 311-324. doi:10.1111/j.1365-2141.2011.08753.x. ISSN 1365-2141. PMID 21671894. S2CID 14749058. "Society for the ...

https://en.wikipedia.org/wiki/Fresh_frozen_plasma

Antithrombin-III. *Lipoprotein lipase. *Apolipoproteins. *Growth factors. *Chemokines. The enzymes and proteins listed above ... 3. p. 345-359 *^ Ebong, Eno; Macaluso FP; Spray DC; Tarbell JM (August 2011). "Imaging the Endothelial Glycocalyx In Vitro By ...

https://en.wikipedia.org/wiki/Glycocalyx

primary: Antithrombin III deficiency. *Protein C deficiency/Activated protein C resistance/Protein S deficiency/Factor V Leiden ... Levels of protein C, free and total protein S, factor VIII, antithrombin, plasminogen, tissue plasminogen activator (TPA) and ... a) Vascular thrombosis in three or more organs or tissues and. *b) Development of manifestations simultaneously or in less than ... and two antibody blood tests spaced at least three months apart that confirm the presence of either lupus anticoagulant or anti ...

https://en.wikipedia.org/wiki/Antiphospholipid_syndrome

prothrombin (kringle domain-2), antithrombin III fragment. inhibit cell proliferation of endothelial cells. ... 4 (3): 275-81. PMID 7606203.. *^ Lee, Jong-Suk; Park, Byung Chul; Ko, Yu Jin; Choi, Mi Kyoung; Choi, Han Gon; Yong, Chul Soon; ... 22 (3): 1737-1754. ISSN 0250-7005. PMID 12168863.. *^ Oba K, Teramukai S, Kobayashi M, Matsui T, Kodera Y, Sakamoto J (June ... epigallocatechin-3-gallate, inhibits vascular endothelial growth factor angiogenic signaling by disrupting the formation of a ...

https://en.wikipedia.org/wiki/Angiogenesis_inhibitor

primary: Antithrombin III deficiency. *Protein C deficiency/Activated protein C resistance/Protein S deficiency/Factor V Leiden ... 3] There are several possible risks to treating coagulopathies, such as transfusion-related acute lung injury, acute ...

https://en.wikipedia.org/wiki/Coagulopathy

Antithrombin III deficiency. altered coagulation. [14] Falls and hip fracture. related to immobility. [17] ... Three factors are important in the formation of a blood clot within a deep vein-these are the rate of blood flow, the thickness ... "Virchow's triad" has been suggested to describe the three factors necessary for the formation of thrombosis: stasis of blood, ... four hours of ischemia resulted in less injury than three hours of ischemia followed by one hour of reperfusion.[32] In ST- ...

https://en.wikipedia.org/wiki/Thrombosis

... namely antithrombin III levels.[2] Small early pilot studies of PEP for prostate cancer in men found no cardiovascular toxicity ... 8 Suppl 1: 3-63. doi:10.1080/13697130500148875. PMID 16112947.. *^ a b c d e f g h i j k l m n o p Stege R, Gunnarsson PO, ... 3 (10): 552-63. doi:10.1038/ncponc0602. PMID 17019433.. *^ a b c d e f g h i j k Lycette JL, Bland LB, Garzotto M, Beer TM ( ... 978-3-642-72110-6. .. *^ a b c d e f g h i j k Ockrim J, Lalani EN, Abel P (October 2006). "Therapy Insight: parenteral ...

https://en.wikipedia.org/wiki/Polyestradiol_phosphate

primary: Antithrombin III deficiency. *Protein C deficiency/Activated protein C resistance/Protein S deficiency/Factor V Leiden ... doi:10.1016/s0140-6736(97)06356-3.. *^ Gando, S (1999). "Disseminated intravascular coagulation and sustained systemic ... Laboratory markers consistent with DIC include:[3][7][12] *Characteristic history (this is important because severe liver ... Treatment is mainly directed towards the underlying condition.[2][3] Other measures may include giving platelets, ...

https://en.wikipedia.org/wiki/Disseminated_intravascular_coagulation

Decrease antithrombin III. *Increase platelet adhesiveness. *Lipid *Increase HDL, triglyceride. *Decrease LDL, fat deposition ... There are three major endogenous estrogens in females that have estrogenic hormonal activity: estrone, estradiol, and estriol. ... The three major naturally occurring forms of estrogen in females are estrone (E1), estradiol (E2), and estriol (E3). Another ... Note the hydroxyl (-OH) groups: estrone (E1) has one, estradiol (E2) has two, estriol (E3) has three, and estetrol (E4) has ...

https://en.wikipedia.org/wiki/Oestrogen

primary: Antithrombin III deficiency. *Protein C deficiency/Activated protein C resistance/Protein S deficiency/Factor V Leiden ... Factor VIII medication may be used to treat and prevent bleeding in people with haemophilia A.[3] ... This page was last edited on 3 September 2018, at 00:29 (UTC). ... Other: Charcot-Marie-Tooth disease (CMTX2-3). *Pelizaeus- ...

https://en.wikipedia.org/wiki/Hemophilia_A

Antithrombin III deficiency. altered coagulation. [14]. Falls and hip fracture. related to immobility. [17]. ... Three factors are important in the formation of a blood clot within a deep vein-these are the rate of blood flow, the thickness ... "Virchow's triad" has been suggested to describe the three factors necessary for the formation of thrombosis: stasis of blood, ... 28 (3): 398-9. doi:10.1161/ATVBAHA.108.162586. PMID 18296598.. *^ National Institute for Health and Clinical Excellence. ...

https://en.wikipedia.org/wiki/Vascular_thrombosis

B01AB02 Antithrombin III. B01AB04 Dalteparin. B01AB05 Enoxaparin. B01AB06 Nadroparin. B01AB07 Parnaparin. B01AB08 Reviparin. ...

https://en.wikipedia.org/wiki/ATC_code_B01

primary: Antithrombin III deficiency. *Protein C deficiency/Activated protein C resistance/Protein S deficiency/Factor V Leiden ... Usually the mutation leads to an early stop in the production of the protein.[3] Due to the problem being genetically based, ... Individuals with the disorder have a mutation to their fibrinogen gene that prevents the formation of the protein.[3] In normal ...

https://en.wikipedia.org/wiki/Congenital_afibrinogenemia

... particularly those caused by a decrease in blood antithrombin III levels due to leakage. Antithrombin III counteracts the ... is a greater predisposition for the formation of blood clots that is caused by a decrease in the levels of antithrombin III in ... Treatment is with oral anticoagulants (not heparin as heparin acts via anti-thrombin 3 which is lost in the proteinuria so it ... antithrombin or the immunoglobulins to pass through the cell membrane and appear in urine.[16] ...

https://en.wikipedia.org/wiki/Nephrotic_syndrome

antithrombin III. Inhibits IIa, Xa, and other proteases. Antithrombin III deficiency heparin cofactor II. Inhibits IIa, ... AntithrombinEdit. Antithrombin is a serine protease inhibitor (serpin) that degrades the serine proteases: thrombin, FIXa, FXa ... III (tissue factor or tissue thromboplastin). Co-factor of VIIa (formerly known as factor III). ... Factors III[citation needed] and VI[citation needed] are unassigned, as thromboplastin was never identified, and actually ...

https://en.m.wikipedia.org/wiki/Blood_coagulation

antithrombin III. Inhibits IIa, Xa, and other proteases. Antithrombin III deficiency. heparin cofactor II. Inhibits IIa, ... AntithrombinEdit. Antithrombin is a serine protease inhibitor (serpin) that degrades the serine proteases: thrombin, FIXa, FXa ... III (tissue factor or tissue thromboplastin ). Co-factor of VIIa (formerly known as factor III). ... The three main forms are hemophilia A (factor VIII deficiency), hemophilia B (factor IX deficiency or "Christmas disease") and ...

https://en.m.wikipedia.org/wiki/Coagulation

... freeze-dried human antithrombin III concentrate Streptase, freeze-dried streptokinase Wound healing Beriplast P Combi-Set, ...

https://en.wikipedia.org/wiki/CSL_Behring

... antithrombin III, homocysteine levels) The diagnosis of pulmonary heart disease is not easy as both lung and heart disease can ... 3 (1): 5-19. doi:10.4103/2045-8932.109910. ISSN 2045-8932. PMC 3641739. PMID 23662171. Taussig, Lynn M.; Landau, Louis I. (2008 ... 3 (1): 137-143. doi:10.4103/2045-8932.109957. ISSN 2045-8932. PMC 3641721. PMID 23662190. "Cor Pulmonale: Introduction to Cor ...

https://en.wikipedia.org/wiki/Pulmonary_heart_disease

The lower risk of VTE may be related to the fact tamoxifen decreases levels of the antithrombin III to a significantly greater ... This study used toremifene as an early prophylactic, which differentiates it from the phase III human studies. Taras TL, Wurz ... a pivotal Phase III clinical trial for the prevention of prostate cancer in high risk men with high grade prostatic ... "GTx's Phase III Clinical Development of ACAPODENE on Course Following Planned Safety Review" (Press release). GTx Inc. 2007-07- ...

https://en.wikipedia.org/wiki/Toremifene

Acquired deficiencies in antithrombin III and C protein during treatment with L-asparaginase]. „Arch Fr Pediatr". 44 (3), s. ... Expert Opin Pharmacother". 2 (3), s. 431-9, Mar 2001. DOI: 10.1517/14656566.2.3.431. PMID: 11336597. ... 3][4]. Mutacja Leiden genu czynnika V prowadzi do powstania białka odpornego na działanie białka C[5] co zwiększa ryzyko ... Crit Care". 10 (3), s. 145, 2006. DOI: 10.1186/cc4947. PMID: 16762040. ...

https://pl.wikipedia.org/wiki/Białko_C

primary: Antithrombin III deficiency. *Protein C deficiency/Activated protein C resistance/Protein S deficiency/Factor V Leiden ... 62 (3): 247-62. doi:10.1111/j.1574-695X.2011.00819.x. PMID 21585562.. Unknown parameter ,month=. ignored (tulong)CS1 maint: ... 3] Ang Sickle-cell anaemia ay isang anyo ng sakit na sickle-cell kung saan may homozygosity para sa mutasyon na nagsasanhi ng ... 39 (3): 176-82. doi:10.1002/ajh.2830390305. PMID 1546714.. Unknown parameter ,month=. ignored (tulong)CS1 maint: multiple names ...

https://tl.wikipedia.org/wiki/Sakit_na_sickle-cell

ആന്റിത്രോംബിൻ(antithrombin) III. IIa, Xa, മറ്റ് പ്രോട്ടിയേയ്സുകൾ എന്നിവയെ തടയുന്നു.. ആന്റിത്രോംബിൻ III യുടെ അഭാവം ... III ടിഷ്യൂ ഘടകം (Tissue factor). VIIa യുടെ കോഫാക്ടർ (factor III എന്ന് മുമ്പ് അറിയപ്പെട്ടിരുന്നത്). ... പാരമ്പര്യ ആൻജിയോഈഡിമ(Hereditary angioedema) type III. ഘടകം XIII, ഫൈബ്രിൻ സ്റ്റെബിലൈസിംഗ് ഘടകം (fibrin-stabilizing factor). ... IIa, ഹെപ്പാരിൻ കോഫാക്ടർ, ഡെർമറ്റാൻ സൾഫേറ്റ് (dermatan sulfate= minor antithrombin) എന്നിവയെ തടയുന്നു.. ഹെപ്പാരിൻ കോഫാക്ടർ II ...

https://ml.wikipedia.org/wiki/രക്തം_കട്ടപിടിക്കൽ

"Antithrombin III for critically ill patients: a systematic review with meta-analysis and trial sequential analysis". Intensive ... Antithrombin protein therapeuticsEdit. The antithrombin protein itself is used as a protein therapeutic that can be purified ... UFH binds to the enzyme inhibitor antithrombin III (AT), causing a conformational change that results in its activation.[83] ... "Thrombate III label" (PDF). Archived from the original (PDF) on 2012-11-15.. ...

https://en.m.wikipedia.org/wiki/Anticoagulants

It works by activating antithrombin III, which blocks thrombin from clotting blood. Heparin can be used in vivo (by injection ... Antithrombin protein therapeuticsEdit. The antithrombin protein itself is used as a protein therapeutic that can be purified ... "Thrombate III label" (PDF). Archived from the original (PDF) on 2012-11-15.. ... Antithrombin is approved by the FDA as an anticoagulant for the prevention of clots before, during, or after surgery or ...

https://en.m.wikipedia.org/wiki/Anticoagulant

However, the Nepalese do not consider it a choice mushroom for eating; of the three grades given to edible mushrooms, it was ... "The nontoxic mushroom Auricularia auricula contains a polysaccharide with anticoagulant activity mediated by antithrombin". ... 7 (3): 373-4. doi:10.1615/intjmedmushr.v7.i3.270.. *^ a b Hobbs, Christopher. (1995). Medicinal Mushrooms: An Exploration of ... 31 (3): 374-6. doi:10.1007/BF02866890.. *^ a b Oei, Peter (2005). "Small-scale mushroom cultivation" (PDF). Agromisa Foundation ...

https://en.wikipedia.org/wiki/Jew's_ear

... and anti-thrombin III, can manifest as iron-resistant microcytic anemia. Reference ranges[edit]. An example reference range for ... III) binding sites. The affinity of transferrin for Fe(III) is extremely high (association constant is 1020 M−1 at pH 7.4)[7] ... The shape of a transferrin receptor resembles a butterfly based on the intersection of three clearly shaped domains.[8] ... Each monomer consists of three domains: the protease, the helical, and the apical domains. ...

https://en.wikipedia.org/wiki/Transferrin

The three N-linked glycosylations sites are mainly equipped with so-called diantennary N-glycans. However, one particular site ... An extremely rare form of Pi, termed PiPittsburgh, functions as an antithrombin (a related serpin), due to a mutation ( ... All three products showed minor differences compared to the normal human plasma A1AT, and are introduced during the specific ... A recent study analyzed and compared the three FDA-approved products regarding their primary structure and glycosylation. ...

https://en.wikipedia.org/wiki/Alpha-1_antitrypsin

Antithrombin (inhibits II, IX, X, XI, XII). *Protein C (inhibits V, VIII)/Protein S (cofactor for protein C) ... Tissue plasminogen activator (t-PA)[3] and urokinase are the agents that convert plasminogen to the active plasmin, thus ...

https://en.wikipedia.org/wiki/Fibrinolysis

Barrett, Mary F. Three common species of Auricularia. Mycologia. 1910, 2 (1): 12-8. ISSN 0027-5514. JSTOR 3753627. doi:10.2307/ ... The nontoxic mushroom Auricularia auricula contains a polysaccharide with anticoagulant activity mediated by antithrombin. ... 黑木耳（學名：Auricularia auricula-judae "猶大的耳朵"），又稱雲耳、木耳、木檽[1]、光木耳、木蕊[2]、木菌[3]、樹雞[4]、䓴（音同「軟」），是木耳科木耳屬一種食用菌。 ... 2011: 90-3. ISBN 81-85041-73-3.. *^ 8.0 8.1 Sterry, Paul; Hughes, Barry. Complete

https://zh.wikipedia.org/zh-tw/黑木耳

Evidence for an exosite determinant of factor Xa specificity in heparin-activated antithrombin»։ J. Biol. Chem. 276 (18): 14961 ... Հեպարինազ III GlcNS/Ac(±6S)-GlcA/IdoA (with a preference for GlcA) ... և III (Կաղապար:EC number) յուրաքանչյուրի առանձին հատկությունները նկարագրված են ներքևում[50][51]: Հեպարինազ ֆերմենտ Սուբստրատի ... Chuang YJ, Swanson R. (2001)։ «Heparin enhances the specificity of antithrombin for thrombin and factor Xa independent of the ...

https://hy.wikipedia.org/wiki/Հեպարին

The La antigen is a 48kDa transcription termination factor of RNA polymerase III, which associates with the Ro-RNP complex.[15] ... 25 (3): 480-6. PMC 1541410. PMID 786521.. *^ Shapiro, TA; Englund, PT (1995). "The structure and replication of kinetoplast DNA ... 15 (3): 132-7. doi:10.1191/0961203306lu2283rr. PMID 16634365. S2CID 25736411.. *^ Jimenez, SA; Derk, CT (Jan 6, 2004). " ... Anti-thrombin. *Lupus anticoagulant. *Coeliac disease: *Anti-transglutaminase. *Anti-gliadin not autoantibody. *RA *Rheumatoid ...

https://en.wikipedia.org/wiki/Anti-nuclear_antibody

Although patients at high risk of bleeding were excluded from the phase III clinical study (PROWESS), 25% of patients treated ... Eli Lilly has recently issued 3 important additional warnings:[citation needed]. *Patients with single organ dysfunction due to ... withdrew Xigris from the market after a major study showed no efficacy for the treatment of sepsis.[2][3] ... Recent administration (within 3 days) of thrombolytic therapy. *Recent administration (within 7 days) of oral anticoagulants or ...

https://en.wikipedia.org/wiki/Drotrecogin_alfa

This model has three stages: 1) initiation of coagulation on TF-bearing cells, 2) amplification of the procoagulant signal by ... antithrombin (AT) to inactivate several coagulation factors IIa, Xa, XIa and XIIa. The affinity of unfractionated heparin and ... The S4 sub-pocket has three ligand binding domains: the "hydrophobic box", the "cationic hole" and the water site. Factor Xa ... Factor Xa plays a key role in all three of these stages.[10] ... Antithrombin (inhibits II, IX, X, XI, XII). *Protein C ( ...

https://en.wikipedia.org/wiki/Factor_X

William III lost his mother to the disease when he was only ten years old in 1660, and she named his uncle Charles II as legal ... Some in the late stage also showed increased antithrombin.[24] This form of smallpox occurred in anywhere from 3 to 25 percent ... 978-3-642-76200-0. .. *^ a b c d e f g h Fenner, F. (1988). "The History of Smallpox and its Spread Around the World" (PDF). ... If successful, a red and itchy bump develops at the vaccine site in three or four days. In the first week, the bump becomes a ...

https://en.wikipedia.org/wiki/Smallpox

Within the first three hours of suspected sepsis, diagnostic studies should include white blood cell counts, measuring serum ... the use of antithrombin to treat disseminated intravascular coagulation is also not useful. Meanwhile, the blood purification ... Within the first three hours, someone with sepsis should have received antibiotics and, intravenous fluids if there is evidence ... The Surviving Sepsis Campaign has recommended 30 ml/kg of fluid to be given in adults in the first three hours followed by ...

https://en.wikipedia.org/wiki/Sepsis

Of these, 93% reported being ill in the three weeks preceding the onset of Reye's syndrome, most commonly with a respiratory ... ISBN 978-3-527-32669-3.. *^ a b c d e f g h i j Jeffreys D (2008). Aspirin the remarkable story of a wonder drug. Bloomsbury ... Aspirin has been shown to have at least three additional modes of action. It uncouples oxidative phosphorylation in ... Retrieved 3 April 2014.. *^ a b c Haynes, William M., ed. (2011). CRC Handbook of Chemistry and Physics (92nd ed.). Boca Raton ...

https://en.wikipedia.org/wiki/Acetylsalicylic_acid

primary: Antithrombin III deficiency · Protein C deficiency/Activated protein C resistance/Protein S deficiency/Factor V Leiden ...

https://bn.wikipedia.org/wiki/থ্যালাসেমিয়া

... heparan sulfate which acts as a cofactor for activating antithrombin, a protease that inactivates several factors in the ...

https://en.wikipedia.org/wiki/Endothelium

Mangel an Inhibiters för't Stollen, sünners Protein C, Protein S un Antithrombin (fröher ok Antithrombin III nöömt) ... Thromboplastin (ok: Tissue Factor, TF oder Fakter III) is en Membranprotein, dat ünner annern in de Adventitia vun Bloodfatten ... Dorbi hannelt sik dat üm en düchtig stark negativ laadte Keed vun Zuckers, de sik an dat Protein Antithrombin anbackt. Disse ... III. (Geweevs-)Thromboplastin, Tissue factor (TF). In't subendothelial Geweev, Kofakter vun VIIa. ...

https://nds.wikipedia.org/wiki/Hämostaas

Heavy chains γ, α and δ have a constant region composed of three tandem (in a line) Ig domains, and a hinge region for added ... Basically, the antibody paratope is polygenic, made up of three genes, V, D, and J. Each paratope locus is also polymorphic, ... Differences, between the variable domains, are located on three loops known as hypervariable regions (HV-1, HV-2 and HV-3) or ... 31 (3-4): 263-278. doi:10.1081/IMM-120016245. PMID 12472184.. *^ a b Brehm-Stecher B, Johnson E (2004). "Single-cell ...

https://en.wikipedia.org/wiki/Antibody

In addition, for the first three days of "warfarinization", the levels of protein C and protein S (anticoagulation factors) ... an anticoagulant that acts upon antithrombin and helps reduce the risk of thrombosis, with warfarin therapy for four to five ... Retrieved 3 April 2011.. *^ a b c Hirsh J, Fuster V, Ansell J, Halperin JL (May 2003). "American Heart Association/American ... 11-3. ISBN 978-1-879284-36-4. .. *^ a b Bates SM, Greer IA, Middeldorp S, Veenstra DL, Prabulos AM, Vandvik PO (February 2012 ...

https://en.m.wikipedia.org/wiki/Warfarin

bind 抗凝血酶（英語：Antithrombin））. 低分子量肝素（貝米肝素（英語：Bemiparin sodium）、舍托肝素（英語：Certoparin sodium）、達肝素（英語：Dalteparin sodium）、依諾肝素、那屈肝素（英語 ... REG1（英語：REG1） · 去纖苷（英語：Defibrotide） · 雷馬曲班（英語：Ramatroban） · 抗凝血酶（英語：Antithrombin） · 蛋白質C（英語：Protein C）（Drotrecogin alfa（英語： ... 1,3-茚滿二酮（英語：1,3-Indandione）: 氯茚二酮（英語：Clorindione

https://zh.wikipedia.org/zh-hant/阿斯匹林

Heparin works by binding to and activating the enzyme inhibitor antithrombin III, an enzyme that acts by inactivating thrombin ... Thrombi are classified in three major groups depending on the relative amount of platelets and red blood cells (RBCs).[3] The ...

https://en.m.wikipedia.org/wiki/Blood_clot

Antithrombin (inhibits II, IX, X, XI, XII). *Protein C (inhibits V, VIII)/Protein S (cofactor for protein C) ... Integrin beta-3 (β3) or CD61 is a protein that in humans is encoded by the ITGB3 gene.[5] CD61 is a cluster of differentiation ... "Entrez Gene: ITGB3 integrin, beta 3 (platelet glycoprotein IIIa, antigen CD61)".. *^ May, K. E.; Villar, J.; Kirtley, S.; ... ITGB3, BDPLT16, BDPLT2, CD61, GP3A, GPIIIa, GT, integrin subunit beta 3. External IDs. OMIM: 173470 MGI: 96612 HomoloGene: ...

https://en.wikipedia.org/wiki/Integrin_beta_3

9 (49): iii-iv, ix-x, 1-78. doi:10.3310/hta9490. PMID 16336844.. ... Antithrombin deficiency[6]. *Protein C deficiency[6]. *Protein ... The American College of Physicians (ACP) gave three strong recommendations with moderate quality evidence on VTE prevention in ... The three factors of stasis, hypercoaguability, and alterations in the blood vessel wall represent Virchow's triad, and changes ... Trimester 3 513 29.2 (26.8-31.9) 340 19.4 (17.4-21.6) 103 18.2 (15.0-22.1) 355 19.7 (17.7-21.9) ...

https://en.wikipedia.org/wiki/Venous_thrombosis

Heparin works by binding to and activating the enzyme inhibitor antithrombin III, an enzyme that acts by inactivating thrombin ... 3]*Common causes of stasis include anything that leads to prolonged immobility and reduced blood flow such as: trauma/broken ...

https://en.m.wikipedia.org/wiki/Blood_clots

All three studies showed that the risk of new thrombosis was decreased with the use of lepirudin, but the risk for major ... DTIs aren't dependent to cofactors like antithrombin to inhibit thrombin so they can both inhibit free/soluble thrombin as well ... Three prospective studies, called the Heparin-Associated-Thrombocytopenia (HAT) 1,2, and 3, were performed that compared ... In contrast, heparin drugs bind in exosite 2 and form a bridge between thrombin and antithrombin, a natural anticoagulant ...

https://en.wikipedia.org/wiki/Discovery_and_development_of_direct_thrombin_inhibitors

Like other serpins, PAI-2 has three beta sheets (A, B, C) and nine alpha helices (hA-hI).[6][7] The structure of PAI-2 mutants ... Antithrombin (inhibits II, IX, X, XI, XII). *Protein C (inhibits V, VIII)/Protein S (cofactor for protein C) ... PAI-2 exists in three polymeric states: monomeric, polymerigenic, and polymer (inactive state). Polymerization occurs by a so- ... 3 (3): 500-13. doi:10.1002/cam4.229. PMC 4101741. PMID 24644264.. *^ Valiente M, Obenauf AC, Jin X, Chen Q, Zhang XH, Lee DJ, ...

https://en.wikipedia.org/wiki/Plasminogen_activator_inhibitor-2

LSBio Antithrombin-III Elisa Kits [LifeSpan BioSciences, Inc.] LSBio Antithrombin-III Elisa Kits. LifeSpan BioSciences, Inc. ... LSBio Antithrombin-III Proteins [LifeSpan BioSciences, Inc.] LSBio Antithrombin-III Proteins. LifeSpan BioSciences, Inc. ... LSBio Antithrombin-III Antibodies [LifeSpan BioSciences, Inc.] LSBio Antithrombin-III Antibodies. LifeSpan BioSciences, Inc. ... antithrombin-III precursor [Bos taurus] antithrombin-III precursor [Bos taurus]. gi,77736341,ref,NP_001029870.1, ...

https://www.ncbi.nlm.nih.gov/protein/77736341

Buy our Antithrombin III 293T transfected lysate (positive control). ab94043 has been validated in western blot. Abcam now ... All lanes : Anti-Antithrombin III antibody (ab66234) at 1/500 dilution. Lane 1 : Antithrombin III overexpression 293T lysate ( ... Type III: alteration of the heparin-binding domain. Plasma AT-III antigen levels are normal in type II and III. Type IV: ... 293T cell transfected lysate in which Human Antithrombin III has been transiently over-expressed using a pCMV-Antithrombin III ...

http://www.abcam.com/antithrombin-iii-overexpression-293t-lysate-whole-cell-ab94043.html

... abnormal antithrombin with increased heparin affinity & reduced ability to inactivate thrombin; associated with familial ... antithrombin III Glasgow. Subscribe to New Research on antithrombin III Glasgow abnormal antithrombin with increased heparin ... 08/01/1987 - "Antithrombin III Glasgow: a variant with increased heparin affinity and reduced ability to inactivate thrombin, ... AT III Glasgow; Glasgow antithrombin III; antithrombin Glasgow III. Networked: 1 relevant articles (0 outcomes, 0 trials/ ...

http://www.curehunter.com/public/keywordSummaryC054089-antithrombin-III-Glasgow.do

Experimental: Anti-thrombin III Drug: Anti-thrombin III Intraoperatively- (correcting to 100%) according to the following ... Antithrombins. Antithrombin III. Hemostatics. Coagulants. Serine Proteinase Inhibitors. Protease Inhibitors. Enzyme Inhibitors ... Genetics Home Reference related topics: Hereditary antithrombin deficiency Drug Information available for: Antithrombin III ... Anti-thrombin III (ATIII) vs Placebo in Children (,7mo) Undergoing Open Congenital Cardiac Surgery. The safety and scientific ...

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Characterisation of a Novel Mutant form of Antithrombin III (Antithrcmbin Dublin) M. Daly ; M. Daly ... M. Daly, A. OMeara, F. Hallinan; Characterisation of a Novel Mutant form of Antithrombin III (Antithrcmbin Dublin). Clin Sci ... Ligand-dependent enhancement of human antithrombin gene expression by retinoid X receptor α and thyroid hormone receptor β ...

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16 for EF with antithrombin III and fibrinogen, respectively, and r=.06 for antithrombin III with fibrinogen). Additional ... The effect of antithrombin III on prognosis is shown in Fig 1⇓. Those patients in the upper two quartiles of the antithrombin ... Antithrombin III and Fibrinogen as Predictors of Cardiac Events in Patients With Angina Pectoris. S.G. Thompson, C. Fechtrup, E ... Antithrombin III: associations with age, race, sex and cardiovascular disease risk factors. Thromb Haemost. 1994;72:551-556. ...

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Keywords: Adult, Antigens, CD18, biosynthesis, metabolism, Antithrombin III, pharmacology, Humans, Leukocytes, drug effects, ... Attenuation of leukocyte beta 2-integrin expression by antithrombin-III.. Authors: D Gritti, A Malinverno, João C. Gasparetto, ... Keywords: Adult, Antigens, CD18, biosynthesis, metabolism, Antithrombin III, pharmacology, Humans, Leukocytes, drug effects, ... Antithrombin-III exerts antiinflammatory effects via ligation of heparan sulfate proteoglycans. Here we show in vitro that ...

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Olds, R. J. ; Lane, D. ; Caso, R. ; Tripodi, A. ; Mannucci, P. M. ; Thein, S. L. / Antithrombin III milano 2 : A single base ... Olds, R. J., Lane, D., Caso, R., Tripodi, A., Mannucci, P. M., & Thein, S. L. (1989). Antithrombin III milano 2: A single base ... Olds, RJ, Lane, D, Caso, R, Tripodi, A, Mannucci, PM & Thein, SL 1989, Antithrombin III milano 2: A single base substitution ... T1 - Antithrombin III milano 2. T2 - A single base substitution in the thrombin binding domain detected with PCR and direct ...

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Functional antithrombin III, functional AT, AT activity. What are these tests?. The antithrombin activity and antigen tests are ... Antithrombin works to thin the blood slightly so that it doesnt clot too much. A lack of antithrombin (AT) can make it more ... The antithrombin antigen test measures how much antithrombin protein your body has made, regardless of how well it functions. ... This problem is caused by a defect in the antithrombin protein. No evidence exists that higher-than-normal antithrombin levels ...

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Antithrombin III for critically ill patients Edited (no change to conclusions) answers are found in the Cochrane Abstracts ... Antithrombin III for critically ill patients Edited (no change to conclusions) is a topic covered in the Cochrane Abstracts. To ... "Antithrombin III for Critically Ill Patients Edited (no Change to Conclusions)." Cochrane Abstracts, Evidence Central, evidence ... Antithrombin III for critically ill patients Edited (no change to conclusions). In Cochrane Abstracts Retrieved March 31, 2020 ...

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U. Hedner, I.M. Nilsson, Antithrombin III in clinical material. Thrombos. Res. 3:631-641 (1973).CrossRefGoogle Scholar ... J.R. OBrien, Antithrombin III and heparin clotting times in thrombosis and atherosclerosis. Thromb. Piathes. Haemorrh. 32:116- ... O.R. Odegard, M.K. Fagerhol, M. Lie, Heparin cofactor activity and antithrombin III concentration in plasma related to age and ... R.H. Yue, M.M. Gertler, T. Staar, R. Koutrouby, Alteration of plasma antithrombin III levels in ischemic heart disease. ...

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The results indicate that antithrombin III-heparin cofactor activity is significantly lower... ... The antithrombin III-heparin cofactor activity of 65 baboons and 130 healthy human subjects was measured. ... Antithrombin III deficiency in a Dutch family.J. Clin. Path., 26: 532-538.PubMedGoogle Scholar ... Antithrombin III, antifactor Xa and Heparin.Brit. J. Haemat., 19: 283-305.PubMedGoogle Scholar ...

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Congenital antithrombin III deficiency is a genetic disorder that causes the blood to clot more than normal. ... The abnormal gene leads to a low level of the antithrombin III protein. This low level of antithrombin III can cause abnormal ... Antithrombin III is a protein in the blood that blocks abnormal blood clots from forming. It helps the body keep a healthy ... Congenital antithrombin III deficiency is an inherited disease. It occurs when a person receives one abnormal copy of the ...

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AT III) is a protein that helps control blood clotting. A blood test can determine the amount of AT III present in your body. ... Functional antithrombin III; Clotting disorder - AT III; DVT - AT III; Deep vein thrombosis - AT III ... Antithrombin III (AT III) is a protein that helps control blood clotting. A blood test can determine the amount of AT III ... Antithrombin III (AT-III) test - diagnostic. In: Chernecky CC, Berger BJ, eds. Laboratory Tests and Diagnostic Procedures. 6th ...

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Species: Antithrombin-III (IPR015555). Key Species. Key species. Number of proteins. FASTA. Protein IDs. ...

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No sex-related difference is noted in terms of the prevalence of congenital antithrombin III deficiency. Women of childbearing ... Antithrombin III Deficiency Q&A What are the sexual predilections of antithrombin III (ATIII) deficiency?. Updated: Feb 10, ... Deficiency Of Antithrombin III (AT III) - Case Report and Review of the Literature. Curr Health Sci J. 2014 Apr-Jun. 40 (2):141 ... Women who are antithrombin III-deficient heterozygotes are at an increased risk of thrombosis when taking OCs, which have also ...

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Antithrombin III. Definition. Antithrombin III (AT III) is a protein that helps control blood clotting. A blood test can ... Functional antithrombin III; Clotting disorder - AT III; DVT - AT III; Deep vein thrombosis - AT III ... Antithrombin III (AT-III) test - diagnostic. In: Chernecky CC, Berger BJ, eds. Laboratory Tests and Diagnostic Procedures. 6th ... This can occur when there is not enough AT III in your blood, or when there is enough AT III in your blood, but the AT III does ...

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Erwachsene. m/w: 80 - 120 % Quelle: Packungsbeilage STA-Stachchrom ATIII. Kinder. 1 Tag: 58-90 %. 3 Tage: 60-89 %. 1-12 Monate: 72-134 %. 1-5 Jahre: 101-131 %. 6-10 Jahre: 95-134 %. 11-16 Jahre: 96-126 %. Quelle: Referenzbereiche bei Kindern, Fa. Stago Ref. 26184 ...

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Antithrombin deficiency in three Japanese families: one novel and two reported point mutations in the antithrombin gene.. ... AT; Ala; Alanine; Antithrombin; Antithrombin deficiency; Arg; Arginine; Asp; Aspartic acid; CL; CM; COS-1 cells; Cell lysates; ... We analyzed the SERPINC1 gene in three patients. Additionally, we expressed the three mutants in the COS-1 cells and compared ... We identified three distinct heterozygous mutations of c.2534C,T: p.56Arginine → Cysteine (R56C), c.13398C,A: p.459Alanine → ...

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Functional antithrombin III; Clotting disorder - AT III; DVT - AT III; Deep vein thrombosis - AT III. ... Antithrombin III (AT III) is a protein that helps control blood clotting. A blood test can determine the amount of AT III ... Antithrombin III blood test. Antithrombin; AT III; AT 3; ... Tests for Antithrombin III blood test. *Antithrombin III blood ... Antithrombin III (AT-III) test - diagnostic. In: Chernecky CC, Berger BJ, eds. Laboratory Tests and Diagnostic Procedures. 6th ...

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The complete amino acid sequence of bovine antithrombin (ATIII). (nih.gov)
Also known as Antithrombin-III (ATIII) (Serpin C1). (mybiosource.com)
Human antithrombin III (ATIII) is a plasma inhibitor of several serine proteases of the blood coagulation system. (ashpublications.org)
Recent studies from our laboratories have confirmed that ATIII inactivates factor XIIa and factor XIIf, but only contributes 2% to 3% to the inhibition of activated factor XII species in plasma. (ashpublications.org)

In type 1 AT deficiency, your body does not make enough antithrombin. (rochester.edu)
In type 2 AT deficiency, your body may make a normal amount of the antithrombin protein. (rochester.edu)
This is because clots in the arteries usually are not caused by antithrombin deficiency. (rochester.edu)
Antithrombin deficiency is one possible cause of a tendency to form unwanted blood clots. (rochester.edu)
In both type 1 and type 2 AT deficiency, the antithrombin activity test shows a low result because you don't have as much working antithrombin as you should have. (rochester.edu)
When the AT activity test shows that levels are low, the antithrombin antigen test can then be used to find out whether the deficiency is type 1 or type 2. (rochester.edu)
If the follow-up antithrombin antigen test shows a lower-than-normal result, then you probably have a type 1 deficiency. (rochester.edu)
More than 120 mutations have been identified for this gene, many of which are known to cause antithrombin-III deficiency. (utsouthwestern.edu)

Data reported as % Functional Activity, which is calculated as the ability of Antithrombin (AT) to suppress FIIa or FXa in the presence of heparin compared to normograms, and expressed as a percentage. (clinicaltrials.gov)
Furthermore, using purified factor XIIf and antithrombin III, heparin (3.6 to 57.2 U/mL) increased the inactivation rate constant of factor XIIf by 1.6 to 14.0 times. (ashpublications.org)

All these sites are occupied by covalently attached oligosaccharide side chains in the predominant form of human antithrombin, α-antithrombin. (chemeurope.com)

The protein that blocks thrombin is called antithrombin. (rochester.edu)
The antithrombin antigen test measures how much antithrombin protein your body has made, regardless of how well it functions. (rochester.edu)
The antithrombin activity test measures how well the protein inhibits thrombin. (rochester.edu)
Antithrombin (AT) is a small protein molecule that inactivates several enzymes of the coagulation system. (chemeurope.com)
[4] As deduced from protein and cDNA sequencing, cow, sheep, rabbit and mouse antithrombins are all 433 amino acids in length, which is one amino acid longer than human antithrombin III. (chemeurope.com)
[6] Shown below are the location of the four potential glycosylation sites within the tertiary structure of an antithrombin monomer , as taken from the protein data bank file 2ANT. (chemeurope.com)
Endothelial cells have two important anticoagulant systems, heparan sulfate-antithrombin system and thrombomodulin-protein C system. (blogspot.ca)
Thus, antithrombin and activated protein C might inhibit the endothelial perturbation induced by cytokines. (blogspot.ca)

Antithrombin is a serpin (serine protease inhibitor). (chemeurope.com)

Protease inactivation results as a consequence of the trapping the protease in an equimolar complex with antithrombin in which the active site of the protease enzyme is inaccessible to its usual substrate. (chemeurope.com)
[5] The formation of an antithrombin-protease complex involves an interaction between the protease and a specific reactive peptide bond within antithrombin. (chemeurope.com)
It is thought the trapping of protease enzymes in inactive antithrombin-protease complexes results as a consequence of their attack of the reactive bond. (chemeurope.com)

A competitive ELISA for quantitative measurement of Porcine Antithrombin III(AT III) in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (antibody-antibodies.com)

Patients randomized to receive Antithrombin concentrate will receive a dose of AT to achieve a target value of 1.2U/ml. (clinicaltrials.gov)

Cow, sheep, rabbit, mouse and human antithrombins share between 84 and 89% amino acid sequence identity. (chemeurope.com)

Here we show in vitro that recombinant human antithrombin-III attenuates CD11b/CD18 expression of activated neutrophils and monocytes in whole blood ex vivo. (scienceopen.com)

[2] The normal antithrombin concentration in human blood plasma is approximately 0.12 mg/ml, which is equivalent to a molar concentration of 2.3 μM. (chemeurope.com)
In human antithrombin this bond is between arginine (arg) 393 and serine (ser) 394. (chemeurope.com)

The antithrombin activity and antigen tests are used to help find out what may be causing abnormal blood clots in your body. (rochester.edu)

Patients randomized to the control group will receive a placebo consisting of normal saline in a volume equivalent to the volume of antithrombin the same patient in the treatment group would have received and administered by anesthesia and perfusion in the exact same manner as the AT is administered in the treatment group. (clinicaltrials.gov)
Antithrombin III for critically ill patients Edited (no change to conclusions) is a topic covered in the Cochrane Abstracts . (unboundmedicine.com)

It contains three disulfide bonds and a total of four possible glycosylation sites. (chemeurope.com)
α-antithrombin is the dominant form of antithrombin found in blood plasma and has an oligosaccharide occupying each of its four glycosylation sites. (chemeurope.com)
A single glycosylation site remains consistently un-occupied in the minor form of antithrombin, β-antithrombin. (chemeurope.com)
The potential glycosylation site at asparagine 135 is not occupied in a minor form of antithrombin, β-antithrombin. (chemeurope.com)

Antithrombin-III exerts antiinflammatory effects via ligation of heparan sulfate proteoglycans. (scienceopen.com)
Antithrombin stimulates prostacyclin generation from endothelial cells by interacting with heparan sulfate of endothelial cells and generated prostacyclin inhibits TNF-alpha production by monocytes. (blogspot.ca)

The physiological target proteases of antithrombin are those of the intrinsic coagulation system , namely the activated forms of Factor X (Xa), Factor IX (IXa), Factor VII (VIIa), Factor XI (XIa), Factor XII (XIIa) and Factor II (thrombin) (IIa). (chemeurope.com)

A method for the differential determination of plasma antithrombins. (scienceopen.com)
Antithrombin has a half life in blood plasma of around 3 days. (chemeurope.com)
[3] Antithrombin has been isolated from the plasma of a large number of species additional to humans. (chemeurope.com)

Antithrombin dimer drawn from PDB 1E03. (chemeurope.com)

Antithrombin works to thin the blood slightly so that it doesn't clot too much. (rochester.edu)
A lack of antithrombin (AT) can make it more likely for you to form blood clots. (rochester.edu)
Your provider usually will not order an antithrombin test for blood clots that form in arteries instead of veins. (rochester.edu)

Purification of a modified form of bovine antithrombin III as an HIV-1 CD8+ T-cell antiviral factor. (nih.gov)

Deficiency Of Antithrombin III (AT III) - Case Report and Review of the Literature. (medscape.com)
Acquired antithrombin III deficiency is a deficiency of antithrombin primarily due to consumption or decreased production. (medscape.com)
We describe the case of a 42-year-old man who presented with abdominal pain attributed to multiple hepatic infarctions who had a combination of homozygosity for the prothrombin gene variant and mild deficiency of antithrombin III (AT III). (biomedcentral.com)
These result in quantitative deficiency of antithrombin (type 1 deficiency). (labtestsonline.org.uk)

Role of antithrombin concentrate in treatment of hereditary antithrombin deficiency. (medscape.com)
Hereditary and acquired antithrombin deficiency: epidemiology, pathogenesis and treatment options. (medscape.com)
11 Thrombate III is approved by the FDA for the treatment of patients with hereditary AT deficiency in connection with surgical or obstetrical procedures or with thromboembolism. (ptcommunity.com)
Treatment of patients with hereditary antithrombin III deficiency (AT-III) in surgical or obstetrical procedures and thromboembolism. (psychiatryadvisor.com)
Concentrates of AT are used in the prophylaxis and treatment of thromboembolic disorders in patients with acquired or hereditary antithrombin deficiency. (google.com)
Natural anticoagulants, namely protein C and antithrombin III deficiencies, are among the common hereditary thrombophilias, known to predispose for the development of PVT. (cureus.com)
A hereditary or acquired prothrombotic state is found among patients with low concentrations of Antithrombin III. (apollodiagnostics.in)
Hereditary antithrombin deficiency is a disorder of blood clotting. (medlineplus.gov)
In hereditary antithrombin deficiency, abnormal blood clots usually form only in veins, although they may rarely occur in arteries. (medlineplus.gov)
About half of people with hereditary antithrombin deficiency will develop at least one abnormal blood clot during their lifetime. (medlineplus.gov)
Other factors can increase the risk of abnormal blood clots in people with hereditary antithrombin deficiency. (medlineplus.gov)
The combination of hereditary antithrombin deficiency and other inherited disorders of blood clotting can also influence risk. (medlineplus.gov)
Women with hereditary antithrombin deficiency are at increased risk of developing an abnormal blood clot during pregnancy or soon after delivery. (medlineplus.gov)
Hereditary antithrombin deficiency is estimated to occur in about 1 in 2,000 to 3,000 individuals. (medlineplus.gov)
Of people who have experienced an abnormal blood clot, about 1 in 20 to 200 have hereditary antithrombin deficiency. (medlineplus.gov)
Hereditary antithrombin deficiency is caused by mutations in the SERPINC1 gene. (medlineplus.gov)
Most of the mutations that cause hereditary antithrombin deficiency change single protein building blocks (amino acids) in antithrombin, which disrupts its ability to control blood clotting. (medlineplus.gov)
Brouwer JL, Lijfering WM, Ten Kate MK, Kluin-Nelemans HC, Veeger NJ, van der Meer J. High long-term absolute risk of recurrent venous thromboembolism in patients with hereditary deficiencies of protein S, protein C or antithrombin. (medlineplus.gov)
THROMBATE III ® (antithrombin III [human]) is indicated in patients with hereditary antithrombin deficiency for treatment and prevention of thromboembolism and for prevention of perioperative and peripartum thromboembolism. (thrombate.com)
Clinical applications include management of patients with hereditary antithrombin III (AT-III) deficiency. (hemonc.org)

The increased activity of the coagulation system of baboon is coupled with decreased antithrombin III-heparin cofactor activity. (springer.com)
Common conditions that result in acquired antithrombin III deficiency include disseminated intravascular coagulation (DIC) , microangiopathic hemolytic anemias due to endothelial damage (ie, hemolytic-uremic syndrome ), veno-occlusive disease (VOD) (in patients undergoing bone marrow transplantation ), sepsis, liver disease, and nephrotic syndrome. (medscape.com)
In addition, a number of recent studies have shown that antithrombin III has antiinflammatory properties, which are independent of its effects on coagulation. (biovendor.com)
Antithrombin (AT), a naturally occurring anticoagulant, is a vitamin K-independent glycoprotein that functions as an irreversible inhibitor of thrombin and factor Xa in the coagulation cascade. (ptcommunity.com)
All had coagulopathy, laboratory evidence of diffuse intravascular coagulation, and marked depletion of plasma antithrombin III. (annals.org)
The others had prompt control of intravascular coagulation coincident with elevation of the antithrombin III concentration by plasma transfusion. (annals.org)
3 Thus, binding of thrombin to TM induces a negative feedback loop that stops the coagulation. (ahajournals.org)
Drugs like heparin exponentially increase antithrombin levels in the blood to stop coagulation - thus thinning the blood. (babymed.com)
Antithrombin III is a small protein molecule that inactivates several enzymes of the coagulation system. (diff.org)
It is the principal plasma anticoagulant serpin mediating inactivation of serine protease procoagulant enzymes, chiefly thrombin and coagulation factors Xa and IXa( 1) Heparin and certain other naturally occurring glycosaminoglycans markedly enhance antithrombin's anticoagulant activity (approximately 1,000-fold) by providing a template to catalyze formation of covalently bonded, inactive complexes of serine protease and antithrombin that are subsequently cleared from circulation. (diff.org)
Antithrombin III, an inhibitor which has several coagulation factors. (apollodiagnostics.in)
Antithrombin III is a serum protease inhibitor that inhibits the blood coagulation protease, thrombin, and is an important regulator of hemostasis. (scrippslabs.com)
The therapeutic effect is usually achieved when the coagulation time is lengthened in these tests by 2-3 times and is maintained at this level throughout the treatment. (treatment-diabetes-info.com)
Deep depression of the AT III level in plasma, creating or aggravating the thrombogenic hazard, is more often associated with the intensive consumption (consumption) of this anticoagulant to inactivate blood coagulation factors. (treatment-diabetes-info.com)
Defective inhibition of the coagulation cascade induced by excessive nonenzymatic glycosylation of antithrombin III in vivo could contribute to accumulation of fibrin in various diabetic tissues. (elsevier.com)
Antithrombin helps to regulate this process by inhibiting the action of several activated coagulation factors, chiefly thrombin and factor Xa to slow down the process and prevent excessive or inappropriate clotting. (labtestsonline.org.uk)

Two marketed formulations of AT concentrate are available in the U.S. Thrombate III (Grifols/Talecris), a lyophilized preparation of AT pooled from human serum, contains no preservatives. (ptcommunity.com)
Because Thrombate III is made from human plasma, the prescribing information includes a warning of potential infectious contamination, such as with the Creutzfeldt-Jakob agent, which can cause disease. (ptcommunity.com)
The elimination half-life of plasma-derived AT concentrate (Thrombate III) is nine times longer (range, 2.5-3.8 days) than that of recombinant human AT concentrate (ATryn) (range, 12-18 hours). (ptcommunity.com)
Report all infections suspected to be transmitted by Thrombate III to (800) 520-2807. (psychiatryadvisor.com)
Patients received 100 units/kg of ideal body weight of antithrombin III (Thrombate III ® ) at time zero, repeated 12 h later, and daily for three days. (biomedcentral.com)
Because THROMBATE III is made from human blood, it may carry a risk of transmitting infectious agents, eg, viruses, the variant Creutzfeldt-Jakob disease (vCJD) agent, and, theoretically, the Creutzfeldt-Jakob disease (CJD) agent. (thrombate.com)

Patients with inherited or acquired antithrombin deficiency are at increased risk of venous thrombosis . (labtestsonline.org.uk)

Once a person is diagnosed with antithrombin III deficiency, all close family members should be screened for this disorder. (medlineplus.gov)

Antithrombin III is a protein in the blood that blocks abnormal blood clots from forming. (medlineplus.gov)
The abnormal gene leads to a low level of the antithrombin III protein. (medlineplus.gov)
Antithrombin III (AT III) is a protein that helps control blood clotting. (medlineplus.gov)
ANTITHROMBIN III (AN te throm bin) is a natural protein. (ahealthyme.com)
Antithrombin III is a plasma protein synthesized in the liver and has molecular weight of 58kDa. (biovendor.com)
Lai KN, Yin JA, Yuen PM, Li PK (1990) Protein C, protein S, and antithrombin III levels in patients on continuous ambulatory peritoneal dialysis and hemodialysis. (springer.com)
Formation, characterization and detection of a ternary complex between S protein, thrombin and antithrombin III in serum. (biomedsearch.com)
S protein, a plasma glycoprotein with Mr 78,000, has been shown to interfere with the heparin-catalysed inhibition of thrombin by antithrombin III. (biomedsearch.com)
Native human blood was replaced by either radiolabelled antithrombin III or radiolabelled prothrombin in the reaction mixture, which was incubated at 37 degrees C. At various time intervals the serum formed from the incubated blood was withdrawn and analysed by crossed immunoelectrophoresis against anti-(S protein) serum in the second dimension. (biomedsearch.com)
Increasing quantities of radioactivity originating both from antithrombin III and from thrombin were precipitated in a cathodal shoulder to the S protein peak. (biomedsearch.com)
This observation indicated the formation of a ternary S protein-thrombin-antithrombin III (STAT) complex in serum. (biomedsearch.com)
This complex could also be observed by the same technique after incubation of purified thrombin in the presence of antithrombin III and S protein. (biomedsearch.com)
Owing to the association of S protein with the thrombin-antithrombin III (TAT) complex, the STAT complex assembled in vitro exhibited a higher Mr than the TAT complex as judged by polyacrylamide-gradient-gel electrophoresis in the absence of SDS. (biomedsearch.com)
Low levels of the protein can be associated with clotting disorders, liver cirrhosis and possibly an inherited disorder known as Antithrombin Deficiency. (babymed.com)
Among the causes, predisposing an individual to CTPV is natural anticoagulant protein C and antithrombin III deficiencies. (cureus.com)
We discuss a case of a nine-year-old male child diagnosed as CTPV secondary to protein C and antithrombin III deficiency who was treated symptomatically for anemia and varices and was referred for transjugular intrahepatic portosystemic shunt (TIPS). (cureus.com)
We report a case of a nine-year-old male child diagnosed as CPTV secondary to protein C and antithrombin III deficiency who presented with generalized weakness, pancytopenia, portal vein thrombosis, splenomegaly, and perisplenic and splenorenal varices. (cureus.com)
The location of the four potential glycosylation sites within the tertiary structure of an antithrombin monomer are shown, as taken from the protein data bank file 2ANT. (diff.org)
As deduced from protein and cDNA sequencing, cow, sheep, rabbit and mouse antithrombins are all 433 amino acids in length, which is one amino acid longer than human antithrombin. (diff.org)
Inherited thrombophilia can be due to inactive variants of endogenous anticoagulants (protein C, S and anti-thrombin III). (biomedcentral.com)
This gene provides instructions for producing a protein called antithrombin (previously known as antithrombin III). (medlineplus.gov)
Antithrombin blocks the activity of proteins that promote blood clotting, especially a protein called thrombin. (medlineplus.gov)
Antithrombin III (Human Purified Protein) 10x10 IU (82072039) is a lyophilised powder prepared from human plasma after affinity chromatography on Heparin-Sepharose gel. (quadratech.co.uk)
Experimental conditions that increased the rate of nonenzymatic protein glycosylation were associated with decreases in the thrombin-inhibiting activity of antithrombin III. (elsevier.com)
The protein that blocks thrombin is called antithrombin. (rochester.edu)
In type 2 AT deficiency, your body may make a normal amount of the antithrombin protein. (rochester.edu)
The antithrombin activity test measures how well the protein inhibits thrombin. (rochester.edu)
3 In vitro studies in skin fibroblast cell lines derived from three patients showed improvement in protein glycosylation following D- galactose ( D- gal) treatment. (nature.com)
Antithrombin is a protein produced by the liver to help control blood clotting. (labtestsonline.org.uk)

Assay of progressive antithrombin in plasma. (springer.com)
LS-F15375 is a 96-well enzyme-linked immunosorbent assay (ELISA) for the Quantitative detection of Chicken Antithrombin-III. (lsbio.com)
The effect of nonenzymatic glycosylation on the biologic function of human antithrombin III was evaluated using a chromogenic thrombin substrate assay in the presence of catalytic amounts of heparin. (elsevier.com)
Antithrombin III activity was estimated by a chromogenic assay. (who.int)

J. Conard, Congenital AT III deficiency. (springer.com)
Congenital antithrombin III deficiency is a genetic disorder that causes the blood to clot more than normal. (medlineplus.gov)
Congenital antithrombin III deficiency is an inherited disease. (medlineplus.gov)
Congenital antithrombin deficiency in patients with splanchnic vein thrombosis. (medscape.com)
Severe congenital antithrombin III deficiency, in which the individual inherits two defective genes, is a rare autosomal recessive condition associated with increased thrombogenesis, typically noted in the neonatal period or early infancy. (medscape.com)
Once a patient with congenital antithrombin III deficiency has developed thrombosis, anticoagulation is more strongly indicated. (medscape.com)
No sex-related difference is noted in terms of the prevalence of congenital antithrombin III deficiency. (medscape.com)
Antithrombin III deficiency, like other congenital procoagulant defects, may contribute to an increased risk of spontaneous abortions. (medscape.com)
Based on clinical data presented by KabiVitrum, Baxter, Cutter Biologicals, and Hoescht-Roussel, the committee recommended approval of antithrombin III (AT-III) for treatment of patients with congenital deficiency of AT-III, for patients with low AT-III levels associated with acute fatty liver of pregnancy, and as a prophylactic treatment against deep-vein thrombosis associated with hip and knee replacement surgery. (informa.com)
All four companies have received orphan designations for their AT-III products as therapies for the congenital deficiency. (informa.com)
FDA noted that "with respect to congenital deficiency of AT-III, no controlled trials have been performed. (informa.com)
First, there are too few patients with congenital AT-III deficiency. (informa.com)
The committee voted unanimously to approve AT-III as a treatment for the congenital deficiency condition. (informa.com)

J.R. O'Brien, Antithrombin III and heparin clotting times in thrombosis and atherosclerosis. (springer.com)
Antithrombins Wibble and Wobble (T85M/K): archetypal conformational diseases with in vivo latent-transition, thrombosis, and heparin activation. (medscape.com)
Trend to efficacy and safety using antithrombin concentrate in prevention of thrombosis in children receiving l-asparaginase for acute lymphoblastic leukemia. (medscape.com)
Women who are antithrombin III-deficient heterozygotes are at an increased risk of thrombosis when taking OCs, which have also been implicated in causing some decrease in antithrombin III level. (medscape.com)
We analyzed the AT gene in three unrelated patients with an AT deficiency who developed thrombosis. (nih.gov)
The symptoms seen in antithrombin deficiency largely depends on the site of clot formation (thrombosis). (healthhype.com)
It is usually secondary to long-standing portal vein thrombosis (PVT) that causes portal hypertension and occlusion of the portal vein, consequently leading to the development of multiple small dilated blood vessels in and around the native portal vein [2-3] . (cureus.com)
In the hip replacement group, the AT-III patients had a post-op thrombosis incidence of 7%, compared to a 40% incidence among patients getting dextran. (informa.com)
In case of massive thrombosis of the great vessels and life-threatening embolic complications, 800-1200 ml of plasma is administered in 2-3 doses on the first day, and then 400 ml daily. (treatment-diabetes-info.com)
The level of AT III in the plasma decreases in the same manner in case of massive thrombosis and thromboembolism, which in the acute period makes it difficult to differentiate between primary (genetically determined) thrombophilia and secondary depression of AT III. (treatment-diabetes-info.com)
A significant decrease in the plasma AT III, accompanied by a predisposition to thrombosis, is observed in nephrotic syndrome, severe liver disease and some malignant neoplasms. (treatment-diabetes-info.com)
This has been demonstrated for anti-GP IIb/IIIa agents, which inhibit stasis-induced venous thrombosis in vivo 3 and thrombin formation in vitro. (ahajournals.org)
A deficiency of plasma antithrombin III has been identified as a potential risk factor for thrombosis. (who.int)

A thrombophilia screen confirmed a homozygous mutation for the prothrombin gene mutation, with mildly reduced levels of anti-thrombin III (AT III). (biomedcentral.com)
The prothrombinase complex can catalyze the activation of prothrombin at a rate 3 x 105-fold faster than can Factor Xa alone. (wikipedia.org)

Even just half the normal antithrombin levels are sufficient to lead to abnormal clotting. (healthhype.com)
The normal antithrombin concentration in human blood plasma is high at approximately 0.12 mg/ml, which is equivalent to a molar concentration of 2.3 μM. (diff.org)
With type 1, normal antithrombin is produced, but the quantity made is insufficient. (labtestsonline.org.uk)

Your search returned 79 antithrombin III ELISA ELISA Kit across 1 supplier. (biocompare.com)

O.R. Odegard, M.K. Fagerhol, M. Lie, Heparin cofactor activity and antithrombin III concentration in plasma related to age and sex. (springer.com)
H.W. Pratt, Alterations in plasma antithrombin III activity in patients with myocardial infarction. (springer.com)
R.H. Yue, M.M. Gertler, T. Staar, R. Koutrouby, Alteration of plasma antithrombin III levels in ischemic heart disease. (springer.com)
Purification of two progressive antithrombins of human plasma. (springer.com)
Thrombin inhibitory activity of fractions obtained by gel filtration of Antithrombin III deficient plasma. (springer.com)
Comparison of progressive antithrombin activity and the concentrations of three thrombin inhibitors in human plasma. (springer.com)
In these patients, replacement of antithrombin III using antithrombin III concentrates or fresh frozen plasma is recommended. (medscape.com)
Human Antithrombin III purified from plasma. (abcam.com)
After reconstitution, administration must occur within 3 hours for plasma-derived AT concentrate and within 8 to 12 hours for the recombinant product. (ptcommunity.com)
Plasma and dialysate levels of tissue-plasminogen activator were similar in heparin and AT-III groups on both day 3 and day 14. (springer.com)
Mori R, Triolo L, De Stefano V, Giusti BP, De Sole P, Leone G (1988) Plasma levels and loss of antithrombin III in chronic ambulatory peritoneal dialysis and nephrotic patients. (springer.com)
Severe antithrombin III depression may be a major cause of the persistent intravascular clotting and can be corrected by plasma transfusion. (annals.org)
Usual infusion rate is 50 to a maximum of 100 international units/minute I.V. Dosage calculation is based on anticipated 1.4% increase in plasma AT-III activity produced by 1 international unit/kg of body weight. (thefreedictionary.com)
Antithrombin III (AT) is a plasma glycoprotein having a total molecular weight of 58.1 kDa (Lebing et al, Vox Sang. (google.com)
A method for the differential determination of plasma antithrombins. (scienceopen.com)
The antithrombin gene on chromosome 1 encodes a glycoprotein of approximately 58,000 molecular weight that is syn= thesized in the liver and is present in a relatively high plasma concentration (approximately 2.3 umol/L). (diff.org)
Antithrombin II (AT II) refers to a cofactor in plasma, which together with heparin interferes with the interaction of thrombin and fibrinogen. (diff.org)
Antithrombin III (AT III ) refers to a substance in plasma that inactivates thrombin. (diff.org)
Antithrombin has a half-life in blood plasma of around 3 days. (diff.org)
Antithrombin has been isolated from the plasma of a large number of species additional to humans. (diff.org)
AT-III (Human) is an antithrombin concentrate prepared from pooled human plasma. (clinicaltrials.gov)
Patients with surgery- or pregnancy-related VTE were tested for AT, PC, and PS at least 3 months after operation or delivery, in order to avoid changes in plasma levels of the naturally occurring anticoagulants related to these conditions. (thrombate.com)
A competitive ELISA for quantitative measurement of Porcine Antithrombin III(AT III) in samples from blood, plasma, serum, cell culture supernatant and other biological fluids. (antibody-antibodies.com)
If the patient has already received intensive heparin therapy, which is ineffective due to a deficiency of AT III, then its administration with plasma can immediately cause deep hypocoagulation and even hemorrhagic complications. (treatment-diabetes-info.com)
Plasma doses depend on the clinical situation and the AT III deficiency. (treatment-diabetes-info.com)
In case of milder thrombophilia, a pronounced therapeutic effect is achieved even with small doses of lyophilized plasma (200 ml every 1-2 days) in combination with the subcutaneous injection of small doses of heparin into the anterior abdominal wall (5000 IU 3-4 times a day). (treatment-diabetes-info.com)
They are dosed in units of activity or concentration units (K / U is the amount of AT III, which is contained in 1 liter of standard donor plasma). (treatment-diabetes-info.com)
The use of heparin without plasma is ineffective and can aggravate AT III deficiency. (treatment-diabetes-info.com)
An eluate from Al(OH)(3), which has been incubated with normal plasma, supplies factors X and IX in their ;plasma' (unactivated) form with II. (tripdatabase.com)
Methods and Results -Human thromboplastin was injected intravenously into wild-type or P2Y 1 -deficient mice, and the effects on platelet count and mortality were determined and plasma thrombin-antithrombin III (TAT) complexes were quantified. (ahajournals.org)
IMSEAR at SEARO: Plasma antithrombin III deficiency in ischaemic stroke in the young. (who.int)
Nagaraja D, Christopher R, Tripathi M. Plasma antithrombin III deficiency in ischaemic stroke in the young. (who.int)
In a pilot study of 56 patients aged less than 40 years who presented with ischaemic stroke of unknown etiology, we detected only one case of plasma antithrombin III deficiency. (who.int)

Antithrombin III is found in normal serum at 15 mg per 100 ml. (creative-enzymes.com)

ANTITHROMBIN III POLYCLONAL ANTIBODIES (HOST RABBIT) Rabbit anti human antithrombin III antiserum rabbit polyclonal These antibodies are very stable and can be stored up to 2 months at fridge temperature under 10C. (antibody-antibodies.com)
Do not freeze taw, rather use ANTITHROMBIN III POLYCLONAL ANTIBODIES (HOST RABBIT) Rabbit anti human antithrombin III antiserum from the fridge if your use is less than 1 or 2 weeks. (antibody-antibodies.com)
ANTITHROMBIN III POLYCLONAL ANTIBODIES (HOST RABBIT) Rabbit anti human antithrombin III antiserum Human samples 80 % of the research is conducted on human samples. (antibody-antibodies.com)
12% T, pH 7.9), or isoelectric focusing (pH 4.2-4.9) followed by immunoblotting with rabbit antiserum to human antithrombin III. (ndsl.kr)

The antithrombin III-heparin cofactor activity of 65 baboons and 130 healthy human subjects was measured. (springer.com)
The results indicate that antithrombin III-heparin cofactor activity is significantly lower in baboons than in humans. (springer.com)

Antithrombin deficiency is a condition where a natural anti-clotting agent in the blood, known as antithrombin III, is either deficient or dysfunctional. (healthhype.com)

ab94043 is a 293T cell transfected lysate in which Human Antithrombin III has been transiently over-expressed using a pCMV-Antithrombin III plasmid. (abcam.com)
Antithrombin III, Goat anti_Human Human samples 80 % of the research is conducted on human samples. (antibody-antibodies.com)
Here we show in vitro that recombinant human antithrombin-III attenuates CD11b/CD18 expression of activated neutrophils and monocytes in whole blood ex vivo. (scienceopen.com)
All these sites are occupied by cova= lently attached oligosaccharide side-chains in the predominant form of human antithrombin, α-antithrombin, resulting in a molecular weight for this form of antithrombin of 58,200. (diff.org)
Scripps Laboratories is a world-leading producer and supplier of purified human Antithrombin III. (scrippslabs.com)
The purpose of this study is to determine the safety and effectiveness of human-derived antithrombin III (AT-III [Human]) supplementation prior to high-risk, non-emergency, cardiac surgery with cardiopulmonary bypass (CPB). (clinicaltrials.gov)
A total of 404 adult subjects undergoing CPB who meet the study eligibility criteria were planned to be randomized to receive either AT-III (Human) or placebo. (clinicaltrials.gov)
The primary objective of this clinical study was to compare the percentage of subjects with any component of a 7 item major morbidity composite (postoperative mortality, stroke, acute kidney injury ([AKI]), surgical re-exploration, arterial or venous thromboembolic event, prolonged mechanical ventilation, or infection) between 2 groups of subjects randomly allocated to receive preoperative supplementation of AT-III (Human) (Antithrombin-III ([Human ]) or Placebo. (clinicaltrials.gov)
Additionally, safety objectives included the evaluation of AT III (Human) for clinical safety including adverse events (AEs), risks for bleeding, clinical laboratory testing, physical exam, and vital signs. (clinicaltrials.gov)
AT-III (Human) is provided as a freeze-dried preparation for intravenous use. (clinicaltrials.gov)
The AT-III (Human) preparation is reconstituted in 10 or 20 mL of sterile water for injection prior to intravenous administration. (clinicaltrials.gov)
Inhibition of heparin-catalyzed human antithrombin III activity by nonenzymatic glycosylation. (elsevier.com)
Fingerprint Dive into the research topics of 'Inhibition of heparin-catalyzed human antithrombin III activity by nonenzymatic glycosylation. (elsevier.com)

A particular form of antithrombin III, which was first characterized by Wardell et al (Biochemistry 36, 13133-13142, 1997), is known as the latent form (L-AT). (google.com)

Measurement and properties of antithrombin. (springer.com)
Okajima K, Uchiba M (1998) The anti-inflammatory properties of antithrombin III: new therapeutic implications. (springer.com)

With type II antithrombin deficiency, the quantity of antithrombin is normal but it does not function as it should. (healthhype.com)
Antithrombin 3 Deficiency, type II (medical condition): Type II Antithrombin deficiency refers the malfunction of a substance that. (rightdiagnosis.com)

Antithrombin testing measures the function and quantity of antithrombin. (labtestsonline.org.uk)
With type 2, there is a sufficient quantity of antithrombin produced, but it is dysfunctional. (labtestsonline.org.uk)

It is due to absent or deficient levels of antithrombin III in the blood. (thefreedictionary.com)
Antithrombin may not be completely deficient for the manifestations of antithrombin deficiency to arise. (healthhype.com)

Rheaume M, Weber F, Durand M, Mahone M. Pregnancy-Related Venous Thromboembolism Risk in Asymptomatic Women With Antithrombin Deficiency: A Systematic Review. (medscape.com)

The third condition for which AT-III use was approved, fatty liver of pregnancy, was described by Baxter as an extremely rare, life-threatening disease of the liver occurring in pregnant women in the third trimester. (informa.com)

This low level of antithrombin III can cause abnormal blood clots (thrombi) that can block blood flow and damage organs. (medlineplus.gov)

Acquired antithrombin deficiencies may occur at any age. (labtestsonline.org.uk)

Natural oestrogens and antithrombin-III levels. (springer.com)
Subsequent dose should be based on AT-III levels obtained 20 minutes post-infusion, every 12hrs, and before the next dose. (psychiatryadvisor.com)
Maintain AT-III levels at 80-120% of normal for 2-8 days. (psychiatryadvisor.com)
Monitor AT-III levels during treatment. (psychiatryadvisor.com)
Clinical conditions associated with low levels of Antithrombin III are venous thromboembolism and liver disease. (scrippslabs.com)
2,3 Download your copy of the AT and VTE risk fact sheet and see why it's important to achieve balance between VTE risk and AT levels. (thrombate.com)
This study was undertaken to verify if "supra-normal" levels of antithrombin III (AT-III) are similarly able to quench intravascular thrombin generation triggered by APL cells. (elsevier.com)
Antithrombin-III levels and transferrin-glycosylation showed significant improvement, and increase in galactosylation and whole glycan content. (nature.com)

AT-III inhibits thrombin as well as factors IXa, Xa and XIa. (abcam.com)

However, the presence of anticoagulants like antithrombin ensures that the activated clotting enzymes do not create clots at various sites in the circulation. (healthhype.com)

12 At the intracellular level, ADP has been shown to act synergistically with thrombin to activate PI 3-kinase 13 and phospholipase D. 14 Two ADP receptors involved in ADP-induced platelet responses have been described to date. (ahajournals.org)

Di Minno MN, Dentali F, Lupoli R, Ageno W. Mild antithrombin deficiency and risk of recurrent venous thromboembolism: a prospective cohort study. (medscape.com)
Mild Antithrombin Deficiency and Risk of Recurrent Venous Thromboembolism: Results from the MEGA follow-up Study. (medscape.com)

Tabata T, Shimada H, Emoto M, Morita A, Furumitsu Y, Fujita J, Inoue T, Miki T, Nishizawa Y, Morii H (1990) Inhibitory effect of heparin and/or antithrombin III on intraperitoneal fibrin formation in continuous ambulatory peritoneal dialysis. (springer.com)

Organisms2

Diseases11

Chemicals and Drugs55

Analytical, Diagnostic and Therapeutic Techniques and Equipment7

Phenomena and Processes13

Information Science2

Sperm chemotaxis. (1/874)

Age-related changes in blood coagulation and fibrinolysis in mice fed on a high-cholesterol diet. (2/874)

Single and combined prothrombotic factors in patients with idiopathic venous thromboembolism: prevalence and risk assessment. (3/874)

Oxidation of methionine residues in antithrombin. Effects on biological activity and heparin binding. (4/874)

Dose response of intravenous heparin on markers of thrombosis during primary total hip replacement. (5/874)

Effect of thrombin inhibition in vascular dementia and silent cerebrovascular disease. An MR spectroscopy study. (6/874)

Comparison of the antithrombotic effect of PEG-hirudin and heparin in a human ex vivo model of arterial thrombosis. (7/874)

Prognostic significance of elevated hemostatic markers in patients with acute myocardial infarction. (8/874)

Antithrombin III

Antithrombin III Deficiency

Antithrombins

Heparin

Antithrombin Proteins

Thrombin

Factor Xa

Factor X

Blood Coagulation

Heparin Cofactor II

Prothrombin

Serine Proteinase Inhibitors

Protein C

Blood Coagulation Tests

Disseminated Intravascular Coagulation

Anticoagulants

Blood Coagulation Factors

Thrombophlebitis

Hemostasis

Fibrinogen

Protein C Deficiency

Blood Coagulation Disorders

Thrombophilia

Protein S Deficiency

Thiohydantoins

Hirudins

p-Dimethylaminoazobenzene

Protein S

Factor IXa

Thrombosis

Thrombin Time

Kinetics

Heparin Lyase

alpha 1-Antitrypsin

Immunoelectrophoresis, Two-Dimensional

Chromogenic Compounds

Pentosan Sulfuric Polyester

Partial Thromboplastin Time

Dermatan Sulfate

Factor V

Heparin Antagonists

Fibrinopeptide A

Chromatography, Affinity

Oligosaccharides

alpha-2-Antiplasmin

Factor XIa

Binding Sites

Complement C1 Inactivator Proteins

alpha-Macroglobulins

Heparitin Sulfate

Protein Binding

Fibrinolysis

Protease Inhibitors

Cetacea

Amino Acid Sequence

Fibrinopeptide B

Protease Nexins

Serpins

Glycosaminoglycans

Factor XI

Factor IX

Factor VIIa

Heparinoids

Phlebitis

Benzamidines

Umbelliferones

Molecular Sequence Data

Electrophoresis, Polyacrylamide Gel

Fibrin Fibrinogen Degradation Products

Swine

Fibrin

Pipecolic Acids

Activated Protein C Resistance

Protein Conformation

Molecular Weight

Thromboembolism

Dansyl Compounds

Receptors, Thrombin

Prothrombin Time

Polysaccharides

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