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Journal articles on the topic 'Antithrombin III'

Author: Grafiati

Published: 4 June 2021

Last updated: 26 July 2025

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1

Sakuragawa, Nobuo, Shin-ichi Kondo, Masahiko Katoh, Kaoru Takahashi, and Takehiko Koide. "Antithrombin III microheterogeneity in antithrombin III deficiency and in the antithrombin III abnormality, “antithrombin III toyama”." Thrombosis Research 47, no. 2 (1987): 147–53. http://dx.doi.org/10.1016/0049-3848(87)90371-9.

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2

George, PM, P. Pemberton, IC Bathurst, et al. "Characterization of antithrombins produced by active site mutagenesis of human alpha 1-antitrypsin expressed in yeast." Blood 73, no. 2 (1989): 490–96. http://dx.doi.org/10.1182/blood.v73.2.490.490.

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Abstract Both congenital and acquired antithrombin-III (AT-III) deficiencies are amenable to replacement therapy. We describe two antithrombins produced by recombinant DNA techniques from human alpha 1-antitrypsin (alpha 1AT) cDNA in yeast. Alteration of the alpha 1AT active site, replacing methionine 358 with arginine, results in a thrombin inhibition rate similar to that of heparin-activated AT-III. Alteration of two further residues, to give a five-residue sequence identical to AT-III, does not increase this rate further. Neither antithrombin is activated by heparin; both are unglycosylated

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3

George, PM, P. Pemberton, IC Bathurst, et al. "Characterization of antithrombins produced by active site mutagenesis of human alpha 1-antitrypsin expressed in yeast." Blood 73, no. 2 (1989): 490–96. http://dx.doi.org/10.1182/blood.v73.2.490.bloodjournal732490.

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Both congenital and acquired antithrombin-III (AT-III) deficiencies are amenable to replacement therapy. We describe two antithrombins produced by recombinant DNA techniques from human alpha 1-antitrypsin (alpha 1AT) cDNA in yeast. Alteration of the alpha 1AT active site, replacing methionine 358 with arginine, results in a thrombin inhibition rate similar to that of heparin-activated AT-III. Alteration of two further residues, to give a five-residue sequence identical to AT-III, does not increase this rate further. Neither antithrombin is activated by heparin; both are unglycosylated and have

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4

Beresford, Charles H., and Maurice C. Owen. "Antithrombin III." International Journal of Biochemistry 22, no. 2 (1990): 121–28. http://dx.doi.org/10.1016/0020-711x(90)90172-y.

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5

Owen, MC, JY Borg, C. Soria, J. Soria, J. Caen, and RW Carrell. "Heparin binding defect in a new antithrombin III variant: Rouen, 47 Arg to His." Blood 69, no. 5 (1987): 1275–79. http://dx.doi.org/10.1182/blood.v69.5.1275.1275.

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Abstract Antithrombin III (AT-III) Rouen is a hereditary abnormal antithrombin with normal progressive inhibitory activity and reduced heparin cofactor activity. It was isolated from the plasma of a woman who suffered a sudden idiopathic sensorineural hearing loss and balance impairment. There was no familial history of thrombosis. By heparin- Sepharose chromatography, AT-III Rouen was separated from the normal antithrombin on elution with increasing concentrations of NaCl. AT-III Rouen eluted earlier than is normal at both pH 7.4 and pH 6.0. At the lower pH, the antithrombins bound more avidl

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6

Owen, MC, JY Borg, C. Soria, J. Soria, J. Caen, and RW Carrell. "Heparin binding defect in a new antithrombin III variant: Rouen, 47 Arg to His." Blood 69, no. 5 (1987): 1275–79. http://dx.doi.org/10.1182/blood.v69.5.1275.bloodjournal6951275.

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Antithrombin III (AT-III) Rouen is a hereditary abnormal antithrombin with normal progressive inhibitory activity and reduced heparin cofactor activity. It was isolated from the plasma of a woman who suffered a sudden idiopathic sensorineural hearing loss and balance impairment. There was no familial history of thrombosis. By heparin- Sepharose chromatography, AT-III Rouen was separated from the normal antithrombin on elution with increasing concentrations of NaCl. AT-III Rouen eluted earlier than is normal at both pH 7.4 and pH 6.0. At the lower pH, the antithrombins bound more avidly to the

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7

Bararu-Bojan, Iris, Maria Cristina Vladeanu (Apavaloaie), Andrei Bojan, Paul-Dan Sirbu, Manuela Ciocoiu, and Oana Badulescu. "The Role of Antithrombin III in the Pathogenesis of the Thrombotic Status in Type 2 Diabetes Mellitus." Revista de Chimie 70, no. 3 (2019): 1047–52. http://dx.doi.org/10.37358/rc.19.3.7061.

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Diabetes mellitus is one of the costliest chronic pathology worldwide with a continuous rising incidence. Diabetes mellitus is linked to frequent cardiovascular events. It is associated with vascular events, especially when the glycated hemoglobin has elevated values. Diabetic patients seem to develop abnormalities of the haemostatic process, such as alterations of the thrombocytic function, modifications of the coagulation and of the fibrinolysis that lead to a thrombophillic status. The acquired thrombophilia present in diabetic patients may be due to the non-enzymatic glycosilation of clott

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8

Logston, Brittany B., Emily A. Rodman, Kimberly L. Dinh, Jennifer L. Placencia, Brady S. Moffett, and Danielle R. Rios. "Effect of Exogenous Antithrombin Administration on Anti-Xa Levels in Infants Treated With Enoxaparin." Journal of Pediatric Pharmacology and Therapeutics 23, no. 4 (2018): 315–19. http://dx.doi.org/10.5863/1551-6776-23.4.315.

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OBJECTIVES Determine the effect of exogenous antithrombin III administration on low molecular weight heparin anti-Xa levels in the context of enoxaparin dosing in infants. METHODS A retrospective chart review of infants receiving concomitant antithrombin III and enoxaparin. The primary objective of this study was to determine the median change in anti-Xa level with antithrombin III supplementation. Secondary objectives were to analyze the median change in antithrombin III levels after administration of exogenous antithrombin III, the dosing of antithrombin III, and the dose of enoxaparin throu

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9

Hatton, MW, SL Moar, and M. Richardson. "On the interaction of rabbit antithrombin III with the luminal surface of the normal and deendothelialized rabbit thoracic aorta in vitro." Blood 67, no. 4 (1986): 878–86. http://dx.doi.org/10.1182/blood.v67.4.878.878.

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Abstract Pure rabbit antithrombin III was isotope labeled (with 125I or 3H) by two different methods; neither procedure caused a loss of antithrombin activity although both methods affected the affinity of the protein for Sepharose-heparin. From segments from freshly excised rabbit aorta, the uptake of isotope-labeled antithrombin III by the endothelium was rapid and saturable, although relatively small compared to the uptake of thrombin; binding of 3H-antithrombin III to the endothelium resembled that of 125I-antithrombin III. Transendothelial passage of antithrombin III into the subendotheli

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10

Hatton, MW, SL Moar, and M. Richardson. "On the interaction of rabbit antithrombin III with the luminal surface of the normal and deendothelialized rabbit thoracic aorta in vitro." Blood 67, no. 4 (1986): 878–86. http://dx.doi.org/10.1182/blood.v67.4.878.bloodjournal674878.

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Pure rabbit antithrombin III was isotope labeled (with 125I or 3H) by two different methods; neither procedure caused a loss of antithrombin activity although both methods affected the affinity of the protein for Sepharose-heparin. From segments from freshly excised rabbit aorta, the uptake of isotope-labeled antithrombin III by the endothelium was rapid and saturable, although relatively small compared to the uptake of thrombin; binding of 3H-antithrombin III to the endothelium resembled that of 125I-antithrombin III. Transendothelial passage of antithrombin III into the subendothelial layers

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11

Preiss, Dieter Ulrich, Delawer Abdullah, Bruno Eberspächer, and Karlheinz Wilhelm. "Safety of virus inactivated antithrombin III concentrate ANTITHROMBIN III IMMUNO (AT III)." Thrombosis Research 65, no. 6 (1992): 677–86. http://dx.doi.org/10.1016/0049-3848(92)90107-l.

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12

Menache, Doris. "Antithrombin III Concentrates." Hematology/Oncology Clinics of North America 6, no. 5 (1992): 1115–20. http://dx.doi.org/10.1016/s0889-8588(18)30298-3.

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13

Beresford, C. H. "Antithrombin III deficiency." Blood Reviews 2, no. 4 (1988): 239–50. http://dx.doi.org/10.1016/0268-960x(88)90013-6.

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14

Tomar, AS, M. Daga, N. Kaushik, and PremKumar Singh. "Antithrombin III Deficiency." Annals of Cardiac Anaesthesia 6, no. 1 (2003): 80. http://dx.doi.org/10.4103/0971-9784.38737.

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15

Uszynski, Mieczyslaw, Andrzej Kielkowski, Waldemar Uszynski, and Ewa Zekanowska. "Thrombin-Antithrombin III Complexes and Antithrombin III in Amniotic Fluid." Gynecologic and Obstetric Investigation 43, no. 1 (1997): 29–33. http://dx.doi.org/10.1159/000291813.

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16

Shiozaki, Arihiro, Takashi Arai, Rikuichi Izumi, Kenji Niiya, and Nobuo Sakuragawa. "Congenital antithrombin III deficient neonate treated with antithrombin III concentrates." Thrombosis Research 70, no. 3 (1993): 211–16. http://dx.doi.org/10.1016/0049-3848(93)90127-a.

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17

Weiler, J. M., and R. J. Linhardt. "Antithrombin III regulates complement activity in vitro." Journal of Immunology 146, no. 11 (1991): 3889–94. http://dx.doi.org/10.4049/jimmunol.146.11.3889.

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Abstract Heparin, a polyion, exerts its main activity to inhibit coagulation through a serine protease inhibitor, antithrombin III. Previous studies have clearly shown that heparin in the absence of antithrombin III also has the capacity to regulate C activity. The present studies examined the ability of purified human antithrombin III to regulate classical and alternative pathways of C, alone and in the presence of heparin. Antithrombin III alone inhibited generation of both pathways in a dose-related manner; antithrombin III at 8 micrograms/10(7) cellular intermediates inhibited generation o

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18

Sorial, Mark N., Rebecca A. Greene, Andrew R. Zullo, Christine Berard-Collins, and Steve Willis. "Exogenous supplementation of antithrombin III in adult and pediatric patients receiving extracorporeal membrane oxygenation." International Journal of Artificial Organs 43, no. 5 (2019): 315–22. http://dx.doi.org/10.1177/0391398819888932.

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Background: Antithrombin III deficiency can occur with heparin anticoagulation during extracorporeal membrane oxygenation leading to heparin resistance. Antithrombin III supplementation has been shown to improve anticoagulation; however, there is no consensus on appropriate administration. We described the effect of antithrombin III supplementation on coagulation parameters in adult and pediatric extracorporeal membrane oxygenation patients. Methods: We conducted a retrospective cohort study using electronic medical records of patients who received ⩾1 dose of antithrombin III during extracorpo

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19

Devraj-Kizuk, R., DH Chui, EV Prochownik, CJ Carter, FA Ofosu, and MA Blajchman. "Antithrombin-III-Hamilton: a gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity." Blood 72, no. 5 (1988): 1518–23. http://dx.doi.org/10.1182/blood.v72.5.1518.1518.

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Abstract Antithrombin-III-Hamilton is a structural mutant of antithrombin III with defective serine protease reactivity, demonstrable in three members of a French Canadian family. The propositus, a 54-year-old man with a history of recurrent thromboembolic events, and his two asymptomatic grown children are heterozygous for the mutant antithrombin III gene. In all three individuals, the immunoreactive antithrombin III level is normal, while the antithrombin and antifactor Xa activity is approximately 50% of the control value. Two dimensional immunoelectrophoresis of antithrombin-III-Hamilton i

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20

Devraj-Kizuk, R., DH Chui, EV Prochownik, CJ Carter, FA Ofosu, and MA Blajchman. "Antithrombin-III-Hamilton: a gene with a point mutation (guanine to adenine) in codon 382 causing impaired serine protease reactivity." Blood 72, no. 5 (1988): 1518–23. http://dx.doi.org/10.1182/blood.v72.5.1518.bloodjournal7251518.

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Antithrombin-III-Hamilton is a structural mutant of antithrombin III with defective serine protease reactivity, demonstrable in three members of a French Canadian family. The propositus, a 54-year-old man with a history of recurrent thromboembolic events, and his two asymptomatic grown children are heterozygous for the mutant antithrombin III gene. In all three individuals, the immunoreactive antithrombin III level is normal, while the antithrombin and antifactor Xa activity is approximately 50% of the control value. Two dimensional immunoelectrophoresis of antithrombin-III-Hamilton in the pre

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21

Pahl, M. V., N. D. Vaziri, F. Oveisi, J. Wang, and Y. Ding. "Antithrombin III inhibits mesangial cell proliferation." Journal of the American Society of Nephrology 7, no. 10 (1996): 2249–53. http://dx.doi.org/10.1681/asn.v7102249.

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Thrombin stimulates and heparin and heparan sulfate inhibit mesangial cell proliferation. In addition, heparin has been shown to inhibit thrombin-stimulated smooth muscle cell proliferation. The anticoagulant action of heparin is mediated by antithrombin III. This study investigated whether heparin's antiproliferative action is also mediated by antithrombin III. To this end, the effect of antithrombin III on thrombin-stimulated mesangial cell growth was examined. As expected, thrombin stimulated DNA synthesis and cell growth in cultured human mesangial cells. The effect of thrombin on DNA synt

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22

Johnstone, I. B., P. Physick-Sheard, and S. Crane. "Breed, age, and gender differences in plasma antithrombin-III activity in clinically normal young horses." American Journal of Veterinary Research 50, no. 10 (1989): 1751–53. https://doi.org/10.2460/ajvr.1989.50.10.1751.

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SUMMARY Plasma antithrombin-III activity was quantitated in plasma samples obtained from 165 clinically normal horses 3 years old or younger. In the horses as a group, antithrombin-III activity ranged from 63 to 131% of a species-specific reference plasma. Thoroughbred horses had significantly higher antithrombin-III activity (103.3 ± 18.3; mean ± sd) than did Standardbred horses (92.3 ± 14.2). The plasma antithrombin-III activities were significantly lower in horses younger than 16 months old when compared with those in more mature horses (3 years old). There was no statistically significant

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23

Emerson, T. E. "Antithrombin III replacement in animal models of acquired antithrombin III deficiency." Blood Coagulation & Fibrinolysis 5, no. 1 (1994): S37–46. http://dx.doi.org/10.1097/00001721-199401000-00006.

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24

Sambrano, J. E., L. J. Jacobson, E. B. Reeve, M. J. Manco-Johnson, and W. E. Hathaway. "Abnormal antithrombin III with defective serine protease binding (antithrombin III "Denver")." Journal of Clinical Investigation 77, no. 3 (1986): 887–93. http://dx.doi.org/10.1172/jci112386.

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25

Blondel-Hill, Edith, and Michael J. Mant. "The pregnant antithrombin III deficient patient: Management without antithrombin III concentrate." Thrombosis Research 65, no. 2 (1992): 193–98. http://dx.doi.org/10.1016/0049-3848(92)90239-7.

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26

Lestari, Indah Nur, Chairul Yoel, and Munar Lubis. "The Association between the Level of Antithrombin III and Mortality in Children with Sepsis." Open Access Macedonian Journal of Medical Sciences 7, no. 6 (2019): 959–61. http://dx.doi.org/10.3889/oamjms.2019.211.

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BACKGROUND: Sepsis is a significant cause of morbidity and mortality in children. The diagnosis of sepsis remains continuing to develop which determines treatment and prognostic. Antithrombin III is one of the coagulation markers to evaluate the prognosis of sepsis. AIM: To determine the association between the level of antithrombin III and mortality in children with sepsis in the Pediatric Intensive Care Unit, Haji Adam Malik General Hospital, Medan. METHODS: A cross-sectional study was conducted in Haji Adam Malik General Hospital, Medan from April until June 2015. There were 41

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27

Vikydal, R., C. Korninger, P. A. Kyrle, et al. "The Prevalence of Hereditary Antithrombin-III Deficiency in Patients with a History of Venous Thromboembolism." Thrombosis and Haemostasis 54, no. 04 (1985): 744–45. http://dx.doi.org/10.1055/s-0038-1660123.

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SummaryAntithrombin-III activity was determined in 752 patients with a history of venous thrombosis and/or pulmonary embolism. 54 patients (7.18%) had an antithrombin-III activity below the normal range. Among these were 13 patients (1.73%) with proven hereditary deficiency. 14 patients were judged to have probable hereditary antithrombin-III deficiency, because they had a positive family history, but antithrombin-III deficiency could not be verified in other members of the family. In the 27 remaining patients (most of them with only slight deficiency) hereditary antithrombin-III deficiency wa

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28

Thompson, E. Anne, and Hatem H. Salem. "The Effects of Human Thrombomodulin on the Inactivation of Thrombin by Its Serum Inhibitors." Thrombosis and Haemostasis 58, no. 03 (1987): 806–10. http://dx.doi.org/10.1055/s-0038-1645994.

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SummaryThrombomodulin is an endothelial cell protein which accelerates thrombin-dependent protein C activation by over 1000 fold. In this study, the effect of thrombomodulin on the inactivation of thrombin by its serum inhibitors was evaluated. 125I-thrombin was incubated at 37° C with serum and the resulting complexes separated by SDS-PAGE. Antithrombin III was the major complex formed with some 125I-thrombin bound to heparin cofactor II and highermolecular weight fractions. Inclusion of thrombomodulin at increasing concentrations inhibited 125I-thrombin binding to antithrombin III and the hi

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29

Shimada, K., A. Kawamoto, K. Matsubayashi, and T. Ozawa. "Histidine-rich glycoprotein does not interfere with interactions between antithrombin III and heparin-like compounds on vascular endothelial cells." Blood 73, no. 1 (1989): 191–93. http://dx.doi.org/10.1182/blood.v73.1.191.191.

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Abstract The role of histidine-rich glycoprotein in controlling heparin-like compounds on the endothelial cell surface is still unclear. The effects of this heparin-neutralizing protein on the interaction between antithrombin III and cultured porcine aortic endothelial cells were examined. Displacement of 125I-labeled antithrombin III specifically bound to endothelial cells by unlabeled histidine-rich glycoprotein was much less potent than that by unlabeled antithrombin III. One hundred- fold molar excess of histidine-rich glycoprotein displaced specific 125I-antithrombin III binding only by 2

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30

Shimada, K., A. Kawamoto, K. Matsubayashi, and T. Ozawa. "Histidine-rich glycoprotein does not interfere with interactions between antithrombin III and heparin-like compounds on vascular endothelial cells." Blood 73, no. 1 (1989): 191–93. http://dx.doi.org/10.1182/blood.v73.1.191.bloodjournal731191.

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The role of histidine-rich glycoprotein in controlling heparin-like compounds on the endothelial cell surface is still unclear. The effects of this heparin-neutralizing protein on the interaction between antithrombin III and cultured porcine aortic endothelial cells were examined. Displacement of 125I-labeled antithrombin III specifically bound to endothelial cells by unlabeled histidine-rich glycoprotein was much less potent than that by unlabeled antithrombin III. One hundred- fold molar excess of histidine-rich glycoprotein displaced specific 125I-antithrombin III binding only by 20%. Furth

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31

Tomasini, BR, and DF Mosher. "Conformational states of vitronectin: preferential expression of an antigenic epitope when vitronectin is covalently and noncovalently complexed with thrombin-antithrombin III or treated with urea." Blood 72, no. 3 (1988): 903–12. http://dx.doi.org/10.1182/blood.v72.3.903.903.

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Abstract A difference in recognition of the adhesive glycoprotein vitronectin (also called S-protein, serum spreading factor, and epibolin) by monoclonal antibody 8E6 (Hayman EG, et al, Proc Natl Acad Sci USA 80:4003, 1983) was investigated using a competitive enzyme- immunosorbent assay and immunoaffinity chromatography. Recognition of vitronectin in serum was approximately 50-fold greater than recognition of vitronectin in plasma. Recognition of vitronectin incubated with heparin, thrombin-antithrombin III complex, or heparin and thrombin- antithrombin III complex together was 2.5-, 7-, or 3

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32

Tomasini, BR, and DF Mosher. "Conformational states of vitronectin: preferential expression of an antigenic epitope when vitronectin is covalently and noncovalently complexed with thrombin-antithrombin III or treated with urea." Blood 72, no. 3 (1988): 903–12. http://dx.doi.org/10.1182/blood.v72.3.903.bloodjournal723903.

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A difference in recognition of the adhesive glycoprotein vitronectin (also called S-protein, serum spreading factor, and epibolin) by monoclonal antibody 8E6 (Hayman EG, et al, Proc Natl Acad Sci USA 80:4003, 1983) was investigated using a competitive enzyme- immunosorbent assay and immunoaffinity chromatography. Recognition of vitronectin in serum was approximately 50-fold greater than recognition of vitronectin in plasma. Recognition of vitronectin incubated with heparin, thrombin-antithrombin III complex, or heparin and thrombin- antithrombin III complex together was 2.5-, 7-, or 32-fold gr

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33

&NA;. "Recombinant Human Antithrombin III." Drugs in R & D 5, no. 2 (2004): 110–12. http://dx.doi.org/10.2165/00126839-200405020-00009.

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34

Stefano, V. De, G. Leone, S. Mastrangelo, et al. "Microheterogeneity of antithrombin III." Blood Coagulation & Fibrinolysis 5, no. 1 (1994): 7–16. http://dx.doi.org/10.1097/00001721-199402000-00002.

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35

Hirsh, Jack, Franco Piovella, and Mario Pini. "Congenital antithrombin III deficiency." American Journal of Medicine 87, no. 3 (1989): S34—S38. http://dx.doi.org/10.1016/0002-9343(89)80529-7.

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36

Manco-Johnson, Marilyn J. "Neonatal antithrombin III deficiency." American Journal of Medicine 87, no. 3 (1989): S49—S52. http://dx.doi.org/10.1016/0002-9343(89)80532-7.

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37

Mammen, E. F. "Antithrombin III and sepsis." Intensive Care Medicine 24, no. 7 (1998): 649–50. http://dx.doi.org/10.1007/s001340050639.

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38

Knot, E. A. R., J. W. ten Cate, T. Bruin, A. H. C. Iburg, and G. N. J. Tytgat. "Antithrombin III metabolism in two colitis patients with acquired antithrombin III deficiency." Gastroenterology 89, no. 2 (1985): 421–25. http://dx.doi.org/10.1016/0016-5085(85)90346-4.

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39

Herion, P., M. Francotte, D. Siberdt, GG Soto, J. Urbain, and A. Bollen. "Monoclonal antibodies against plasma protease inhibitors: production and characterization of 15 monoclonal antibodies against human antithrombin III. Relation between antigenic determinants and functional sites of antithrombin III." Blood 65, no. 5 (1985): 1201–7. http://dx.doi.org/10.1182/blood.v65.5.1201.1201.

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Abstract Fifteen hybridomas secreting monoclonal antibodies against human antithrombin III, originating from two mouse strains, have been produced by the cell fusion technique. Eight monoclonal antibodies belong to the class IgG1, five to the class IgG2a, and two to the class IgG2b. All light chains belong to the kappa group. No cross-reaction of the monoclonal antibodies have been observed with a crude preparation of albumin nor with alpha 1-antitrypsin and alpha 2-antiplasmin. Five of these monoclonal antibodies exhibit a relatively high avidity for antithrombin III. Inhibition experiments s

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40

Herion, P., M. Francotte, D. Siberdt, GG Soto, J. Urbain, and A. Bollen. "Monoclonal antibodies against plasma protease inhibitors: production and characterization of 15 monoclonal antibodies against human antithrombin III. Relation between antigenic determinants and functional sites of antithrombin III." Blood 65, no. 5 (1985): 1201–7. http://dx.doi.org/10.1182/blood.v65.5.1201.bloodjournal6551201.

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Fifteen hybridomas secreting monoclonal antibodies against human antithrombin III, originating from two mouse strains, have been produced by the cell fusion technique. Eight monoclonal antibodies belong to the class IgG1, five to the class IgG2a, and two to the class IgG2b. All light chains belong to the kappa group. No cross-reaction of the monoclonal antibodies have been observed with a crude preparation of albumin nor with alpha 1-antitrypsin and alpha 2-antiplasmin. Five of these monoclonal antibodies exhibit a relatively high avidity for antithrombin III. Inhibition experiments showed tha

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41

Manoukian, Nora, and Durval Rosa Borges. "Hypoprothrombinemia in the compensated form of hepatosplenic schistosomiasis: further studies." Revista do Instituto de Medicina Tropical de São Paulo 30, no. 4 (1988): 274–80. http://dx.doi.org/10.1590/s0036-46651988000400005.

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Coagulation abnormality is frequently observed in schistosomiasis patients but its pathophysiology has not been established. We measured, by immunodiffusion. the prothrombin-antigen concentration in 56 individuals; of these 19 with demonstrated compensated form of hepatosplenic schistosomiasis, 17 with cirrhosis and 20 were control subjects. Transaminases, albumin, transthyretin, prothrombin time, antithrombin III, factor VII, and fibrinogen were also evaluated. All parameters were altered in the cirrhotic group but only albumin, prothrombin and antithrombin III levels were altered in the schi

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42

Pylaeva, N. Yu, E. M. Shifman, and A. V. Kulikov. "The effect of demographic and anthropometric indicators on the amount of antithrombin III in patients with severe pre-eclampsia." Voprosy ginekologii, akušerstva i perinatologii 20, no. 2 (2021): 13–19. http://dx.doi.org/10.20953/1726-1678-2021-2-13-19.

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A natural anticoagulant antithrombin III can serve as a possible marker of severe pre-eclampsia. The concentration variability of antithrombin III is known, depending on some demographic and anthropometric patient data. Objective. To study the connection between antithrombin III levels and the values of demographic and anthropometric indicators in patients with severe pre-eclampsia and normal pregnancy. Patients and methods. In order to achieve the objective of the study, two groups of 50 pregnant women in each were formed. Indicators were evaluated using the paired comparison method. Such ind

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Kuroda, Shintaro, Hirotaka Tashiro, Tsuyoshi Kobayashi, Masakazu Hashimoto, Yoshihiro Mikuriya, and Hideki Ohdan. "Administration of Antithrombin III Attenuates Posthepatectomy Liver Failure in Hepatocellular Carcinoma." Digestive Surgery 32, no. 3 (2015): 173–80. http://dx.doi.org/10.1159/000379759.

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Background/Aims: Coagulopathy can cause disseminated intravascular coagulation and posthepatectomy liver failure. Posthepatectomy liver failure predicts a poor prognosis after hepatectomy for hepatocellular carcinoma. Although antithrombin III reduces hypercoagulation, the impact of postoperative antithrombin III administration remains unknown. The aim of this study was to determine whether postoperative antithrombin III administration protects against the development of coagulation disorders. Methods: Data from 164 patients who received antithrombin III and 169 who did following curative hepa

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Demers, Christine, Jeffrey S. Ginsberg, Penny Henderson, Fred A. Ofosu, Jeffrey I. Weitz, and Morris A. Blajchman. "Measurement of Markers of Activated Coagulation in Antithrombin III Deficient Subjects." Thrombosis and Haemostasis 67, no. 05 (1992): 542–44. http://dx.doi.org/10.1055/s-0038-1648490.

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SummaryFunctional antithrombin III levels were measured by factor Xa inhibition in 63 members of a large family with type 2 antithrombin III deficiency and individuals were classified as antithrombin III deficient or non-deficient according to the results. FI+2 and TAT complexes were measured using an ELISA and FPA levels were measured by radioimmunoassay.Thirty subjects (48%) were classified as antithrombin III deficient and 33 (52%) as antithrombin III non-deficient. The mean level of FI+2 was significantly higher in the deficient adults (0.87 ± 0.26) compared to both the non-deficient adult

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Soons, H., G. Tans, and H. C. Hemker. "The heparin-catalysed inhibition of human factor XIa by antithrombin III is dependent on the heparin type." Biochemical Journal 256, no. 3 (1988): 815–20. http://dx.doi.org/10.1042/bj2560815.

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The effect of various well-characterized heparin preparations on the inactivation of human Factor XIa by human antithrombin III was studied. The heparin preparations used were unfractionated heparin and four heparin fractions obtained after anion-exchange chromatography. Inactivation of Factor XIa was monitored with S2366 as chromogenic substrate and followed pseudo-first-order reaction kinetics under all reaction conditions tested. Enhancement of the rate of inhibition of Factor XIa in the presence of unfractionated heparin correlated to the binding of antithrombin III to heparin. From the ki

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Wolf, M., C. Boyer, A. Tripodi, D. Meyer, MJ Larrieu, and PM Mannucci. "Antithrombin Milano: a new variant with monomeric and dimeric inactive antithrombin III." Blood 65, no. 2 (1985): 496–500. http://dx.doi.org/10.1182/blood.v65.2.496.496.

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Abstract A qualitative defect of antithrombin III (AT III) has been demonstrated over three generations in eight members of an Italian family by the discrepancy between a normal amount of antigen and decreased antithrombin and anti-Xa activity in the presence or in the absence of heparin. By two-dimensional immunoelectrophoresis in the absence of heparin, two peaks of AT III were present in all patients' plasma. AT III was purified from normal and propositus plasma by sulfate dextran precipitation followed by heparin affinity chromatography. The elution profile of the patient's AT III was abno

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47

Wolf, M., C. Boyer, A. Tripodi, D. Meyer, MJ Larrieu, and PM Mannucci. "Antithrombin Milano: a new variant with monomeric and dimeric inactive antithrombin III." Blood 65, no. 2 (1985): 496–500. http://dx.doi.org/10.1182/blood.v65.2.496.bloodjournal652496.

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Abstract:

A qualitative defect of antithrombin III (AT III) has been demonstrated over three generations in eight members of an Italian family by the discrepancy between a normal amount of antigen and decreased antithrombin and anti-Xa activity in the presence or in the absence of heparin. By two-dimensional immunoelectrophoresis in the absence of heparin, two peaks of AT III were present in all patients' plasma. AT III was purified from normal and propositus plasma by sulfate dextran precipitation followed by heparin affinity chromatography. The elution profile of the patient's AT III was abnormal and

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48

Farrell, David H., Keeley M. McConnell, Jevgenia Zilberman-Rudenko, et al. "Antithrombin III Levels and Outcomes Among Patients With Trauma." JAMA Network Open 7, no. 8 (2024): e2427786. http://dx.doi.org/10.1001/jamanetworkopen.2024.27786.

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ImportancePatients with trauma exhibit a complex balance of coagulopathy manifested by both bleeding and thrombosis. Antithrombin III is a plasma protein that functions as an important regulator of coagulation. Previous studies have found a high incidence of antithrombin III deficiency among patients with trauma.ObjectiveTo assess whether changes in antithrombin III activity are associated with thrombohemorrhagic complications among patients with trauma.Design, Setting, and ParticipantsThis cohort study was conducted from December 2, 2015, to March 24, 2017, at a level I trauma center. A total

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Pletcher, C. H., M. T. Cunningham, and G. L. Nelsestuen. "Molecular weight analysis of antithrombin III-heparin and antithrombin III-thrombin-heparin complexes." Journal of Biological Chemistry 261, no. 9 (1986): 4143–47. http://dx.doi.org/10.1016/s0021-9258(17)35637-5.

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Watanabe, Masaki, Yutaka Arahata, Yoshimasa Motegi, and Akira Deguchi. "Alterations in antithrombin III and thrombin-antithrombin III complex levels in brainstem infarction." Nosotchu 15, no. 4 (1993): 293–97. http://dx.doi.org/10.3995/jstroke.15.293.

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