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At least 19 recordsLinked to original sources
PubMed1983

Isolation and characterization of a hereditary abnormal antithrombin III 'Antithrombin III Toyama'.

A hereditary abnormal antithrombin III (AT-III) 'Antithrombin III Toyama' was purified from the plasma of a patient with recurrent thrombophlebitis by a procedure involving barium chloride and ammonium sulfate fractionations, affinity chromatography on anti-AT-III-Sepharose gel, and DEAE-Sephadex chromatography. Purified abnormal AT-III was shown to be the same as normal one in the molecular size, having the same molecular weight, amino-terminal sequence and carboxy-terminal amino acid. Abnormal AT-III gave the same UV spectrum as normal AT-III and both proteins were immunologically identical. Abnormal AT-III, however, showed the different electrophoretic mobility on agarose gel electrophoresis and immunoelectrophoresis. Abnormal AT-III was more electronegative than normal one, before and after a neuraminidase digestion of both proteins. These results suggest that in antithrombin III Toyama an amino acid residue at the heparin-binding site has been replaced by less basic or more acidic one which has no ability to interact with heparin, resulting in a loss of heparin cofactor activity of this protein.

Adult↗
PubMed1974

Abnormal antithrombin III (antithrombin III "Budapest") as a cause of a familial thrombophilia.

A family with a high incidence of spontaneous thromboembolism has been investigated and those members affected were found to have significantly depressed levels of plasma and serum heparin cofactor activity; i.e., antithrombin III and anti-Xa activity. Further studies revealed that despite a marked diminution of antithrombin III activity in these patients measurement of antithrombin III by immunological techniques showed the levels to be normal. It is concluded that this anomaly represents a defect in the synthesis of the antithrombin III molecule. The abnormality appeared to be inherited but the mode of inheritance could not be determined with the available data.

Adsorption↗
PubMed1982

A new familial variant of antithrombin III: 'antithrombin III Paris'.

A 59-year-old woman presented a recurrent history of thromboembolism. A qualitative defect of antithrombin III (AT III) was suggested by the discrepancy between a normal amount of AT III antigen and a decreased heparin cofactor activity. Six members of the same family showed a similar defect although clinically asymptomatic. The qualitative abnormality of AT III was confirmed by two-dimensional immunoelectrophoresis. In the absence of heparin, a single peak was obtained with both control and patients' plasmas. In the presence of heparin, two peaks of AT III were observed in the patients' plasmas: the mobility of one peak was similar to that of the control, whereas the other showed a decreased mobility, suggesting a lack of binding to heparin. The two populations of AT III were separated by affinity chromatography on heparin-agarose. 50% of the patients' AT III bound to the agarose beads. The remainder, recovered in the supernatant, migrated in two-dimensional immunoelectrophoresis as a single peak with the same mobility in the presence or absence of heparin, and was devoid of heparin cofactor activity. This familial AT III variant characterized a reduced affinity for heparin is tentatively named 'Antithrombin III Paris'.

Antigens↗
PubMed1982

Distinction of two pathologic antithrombin III molecules: antithrombin III "Aalborg' and antithrombin III "Budapest'.

Plasma from two different thrombophilic families with functional inherited antithrombin III deficiency, i.e., with low antithrombin III activity but normal immunoreactive antithrombin III concentration, were investigated simultaneously in the same laboratory. The experiments (thrombin and Factor Xa inactivation, heparin affinity chromatography, modified two dimensional immunoelectrophoresis and gel filtration) showed a distinct difference between the two antithrombin III anomalies. The antithrombin III "Aalborg' had decreased thrombininactivating activity but normal Factor Xa-inactivating activity. The heparin affinity and the molecule weight are normal. The antithrombin III "Budapest' displays a more profound abnormality with pathologic thrombin and Factor Xa inactivation, decreased heparin affinity and abnormal molecular weight.

Antithrombin III↗
PubMed1987

Antithrombin III microheterogeneity in antithrombin III deficiency and in the antithrombin III abnormality, "antithrombin III Toyama".

Antithrombin III (AT III) microheterogeneity was investigated in 12 cases of congenital AT III deficiency and 2 cases of congenital AT III abnormality by isoelectric focusing (IEF) and immunofixation. In congenital AT III deficiency, IEF and immunofixation revealed AT III as 8 bands which was indistinguishable from normal control in terms of the number of bands and the isoelectric point (pI) of each band. In the proband of the congenital AT III abnormality, however, IEF and immunofixation showed AT III as 8 bands which shifted slightly but definitely to the acidic side compared to those of normal subjects. This change in pI of the abnormal AT III was considered to reflect the amino acid replacement in the polypeptide chain of the abnormal AT III molecule.

Adult↗
PubMed1992

Safety of virus inactivated antithrombin III concentrate antithrombin III immuno (AT III).

In a prospective clinical trial the risk of infection after application of virus inactivated antithrombin III concentrate ANTITHROMBIN III IMMUNO (AT III) was investigated in patients undergoing cardiovascular surgery. The study was conducted according to the recommendations of the International Committee on Thrombosis and Hemostasis (ICTH), with the exception that most patients required additional blood products as well as AT III. Twenty-seven patients were eligible to test for the risk of acquiring hepatitis B. Twenty-six patients could be evaluated in terms of hepatitis NANB transmission considering ALT-levels whereas 20 patients could be tested for anti-HCV one year after surgery. Samples from 78 patients could be monitored for anti-HIV-1. None of these patients showed any signs of infection. AT III IMMUNO seems to be an antithrombin III concentrate with low or absent infectivity.

Acquired Immunodeficiency Syndrome↗
PubMed1982

Differences between normal antithrombin III and antithrombin III Padua as determined by laser nephelometry.

Laser nephelometry was used to characterize an abnormal antithrombin III (AT III Padua) in comparison with normal antithrombin. Heparinized (0.2 IU/ml) or non-heparinized AT III Padua plasma reacts with Laser nephelometry antithrombin III antiserum in a different way compared with pooled normal plasma. There is in fact a slower antigen-antibody reaction during the first 40-45 min both in AT III Padua heparinized and non-heparinized plasmas, compared with pooled normal plasma; then the kinetics overlap. On the contrary the concentrations of antithrombin III Padua in percent correlate well with those obtained by Mancini's and Laurell's methods. These data indicate that Laser nephelometry is suitable for AT III antigen determinations and may also supply useful information for the characterization of abnormal clotting factors.

Antithrombin III↗
PubMed1983

Anticoagulating and non-enzymatic fibrinolytic activities of heparin-antithrombin III and antithrombin III-heparin-thrombin complexes in vitro and in vivo.

The heparin-antithrombin III and antithrombin III-heparin-thrombin complexes were prepared in vitro. The formation of complexes was controlled by crossed electrophoretic and spectrophotometric methods. All the binary and ternary complexes prepared at the weight ratio of components 1: 1: 1 and at some other weight correlations were active as non-crosslinked fibrin solvents and kept this activity in the presence of inhibitors of plasmin fibrinolysis. A considerable prolongation of thrombin time and an increasing of total and in particular non-enzymatic lytic actions of plasma were achieved in 7 and 30 min after intravenous injection of 1 ml 0.1-0.2% solution of heparin-antithrombin III complex in rats. The obtained results of experiments allow to conclude that the heparin-antithrombin III and antithrombin III-heparin-thrombin complexes possess the non-enzymatic fibrinolytic action on non-crosslinked fibrin. The degree of this activity is dependent on the quantitative correlation of heparin-antithrombin III or antithrombin III-heparin-thrombin concentrations during the reaction of complex formation.

Animals↗
PubMed1990

[Oral contraceptive agents and antithrombin III].

Antithrombin III is one of the most important inhibitors of serine proteases of coagulation and fibrinolysis. It inhibits the activity of thrombin and factor X. Its congenital or acquired reduction leads to an increased risk of thrombosis. In their study the authors aimed to investigate the influence of oral contraceptive preparations--Gravistat and Nonovolan on the activity of antithrombin III. Thirty five women, receiving these drugs for a period of one month to ten years (on the average two and a half years were examined. All women received the drugs in accordance with the physician prescription, taking into consideration the lack of history data on increased frequency of thrombosis. Part of the examined group (the first ten on the table of the results) were smokers with mean usage of 15 cigarettes per day. The study was carried out on 25 women at the three stages of the hormonal cycle, but singly on the remaining 10 women in its beginning. Blood sample for examination was taken with anticoagulant (citrate) in the morning before breakfast and the activity of the inhibitor was determined by kinetic colorimetric method and chromatogenic Chromasin TN (a modification of Kamenov). The results were presented in percentages. The mean activity of antithrombin III was: means = 107.5%, which did not differ from the reference values. The activities at the three phases of the menstrual cycle did not differ significantly (p greater than 0.05). The results, obtained from the study, proved that hormonal contraceptive drugs did not reduce the activity of antithrombin III.

Adult↗
PubMed1994

[Renal pathology in the Ivory Coast: exploration and functional activity of antithrombin iii].

Antithrombin III activity was determined in 96 ivorian adults clinically divided into 3 groups: I) nephrotic syndrome, II) chronic renal failure, and III) terminal uremia requiring maintenance dialysis. In the nephrotic syndrome, a significative decrease of antithrombin III is found, which can explain the existence of thrombotic complications. In chronic renal failure and terminal uremia, antithrombin III activity is normal, and thromboembolic events may be related to a deficiency of other inhibitors of the coagulation.

Adolescent↗
PubMed1980

Purification and characterization of rat plasma antithrombin III.

Antithrombin III was purified from rat plasma in 70% yield by salting out with (NH4)2SO4, affinity chromatography on heparin-Sepharose 4B, and ion-exchange chromatography on DE-52. The preparation was homogeneous as judged by polyacrylamide gel electrophoresis in the presence and absence of sodium dodecyl sulfate, by analytical ultracentrifugation, and by immuno-chemical analysis. It was composed of a single polypeptide chain whose molecular weight was estimated to be about 64 000 both by sodium dodecyl sulfate polyacrylamide gel electrophoresis and by sedimentation equilibrium analysis. Antithrombin III was a glycoprotein containing 3.6% glucosamine, 0.2% fucose, 2.5% mannose, 1.6% galactose and 3.9% sialic acid. Isoelectric focusing in polyacrylamide gel revealed four bands in the range of pH 4.7--4.9, indicating the microheterogeneity. Rat antithrombin III inhibited bovine alpha-thrombin by forming an equimolar complex. Kinetics of this reaction were studied by gel electrophoresis in sodium dodecyl sulfate. When the inhibitor was allowed to react with an excess amount of thrombin, the initial equimolar complex with a molecular weight of 110 000 was cleaved gradually to a product with a molecular weight of 97 000, which was further cleaved to a second product with a molecular weight of 85 000.

Animals↗
PubMed1981

[Anticoagulating activity and lytic action of the heparin-antithrombin III and antithrombin III-heparin-thrombin complexes on non-stabilized fibrin].

The heparin-antithrombin III and antithrombin III-heparin-thrombin complexes were prepared by rapid mixing of the components at different weight ratios (1:1, 1:3, 1:4, 1:6, 1:7, 3:1 - heparin/antithrombin III), pH 7.0-7.2. The reaction mixture was incubated for 15 min at 37 degrees. The complexes were precipitated at pH 4.5-4.8. All the heparin-antithrombin III complexes possess high anticoagulating and lytic activities. The antithrombin III-heparin-thrombin complex prepared at the weight ratio of 1:1:6 has a high lytic activity. The antithrombin III-heparin-thrombin complex prepared at the weight ratio of 1:1:1 reveals a high anticoagulating activity and a strong lytic action with respect to the non-stabilized fibrin.

Antithrombin III↗
PubMed1991

Site-directed mutagenesis of alanine-382 of human antithrombin III.

Antithrombin III Hamilton is a structural variant of antithrombin III (AT-III) with normal heparin affinity but impaired serine protease inhibitory activity. The molecular defect of AT-III-Hamilton is a substitution of threonine for alanine at amino acid residue 382. Recently it has been shown that both plasma-derived and cell-free-derived AT-III-Hamilton polypeptides act as substrates rather than inhibitors of thrombin and factor Xa. In the present study, the cell-free expression phagemid vector pGEM-3Zf(+)-AT-III1-432 was mutated at amino acid residue 382 of AT-III to generate 7 cell-free-derived variants. All these cell-free-derived AT-III variants were able to bind heparin as effectively as cell-free-derived normal AT-III. In terms of alpha-thrombin inhibitory activity each variant reacted differently. Variants could be grouped into 3 categories with respect to thrombin-AT-III complex formation: (1) near normal activity (glycine, isoleucine, leucine, valine); (2) low activity (threonine, glutamine); (3) no detectable activity (lysine). These data suggest that mutations at position 382 of AT-III may have a variable effect on protease inhibitory activity, depending on either the stability of the P12-P9 region of the exposed loop of AT-III, or the inability of the amino acid residue at position 382 to interact with a conserved hydrophobic pocket consisting of phenylalanine (at positions 77, 221 and 422) and isoleucine (position 412) residues.

Alanine↗
PubMed1980

Effects of the reduction and S-carbamidomethylation on the conformation, activity and heparin-binding capacity of human antithrombin III.

Antithrombin III has been shown to contain three disulphide bridges. They can be broken by reduction under non-denaturing conditions. The completely reduced and S-carbamidomethylated protein is devoid of thrombin-inhibiting activity and does not bind heparin. However, the immunological reactivity as determined by electroimmunoassay is almost unchanged, indicating that no large conformational changes occur upon cleavage of the disulphide bonds. This is also supported by the observation that the reduced and S-carbamidomethylated protein has the same fluorescence properties as the native protein dichroic spectrum of the native protein shows a pronounced pattern in the near-ultraviolet region, indicating restricted rotation of the aromatic amino acid side chains. This is drastically changed by the reduction and carbamidomethylation. The character of the far-ultraviolet circular dichroic spectrum is similar in the native and reduced S-carbamidomethylated protein. The reduction and S-carbamidomethylation of antithrombin III induces some local changes in the tertiary structure affecting the inhibitor activity, heparin binding and near-ultraviolet circular dichroic spectrum, but do not seem to induce any substantial general conformation change.

2,2'-Dipyridyl↗
PubMed1977

Crossed immunoelectrophoresis as applied to studies on complex formation. The binding of heparin to antithrombin III and the antithrombin III--thrombin complex.

A two-dimensional immunoelectrophoretic method has been used to obtain information on the binding of heparin to purified antithrombin III and the antithrombin III--thrombin complex. The difference in mobility of the components in a gel containing heparin enables distinction between free and complexed forms of antithrombin III. The results obtained with purified preparations show that heparin is bound more strongly to antithrombin III than to the antithrombin III--thrombin complex. In plasma heparin is bound to several components, only a fraction being bound to antithrombin III. Several components containing antithrombin III are detectable in serum.

Animals↗