Academic literature on the topic 'Antithrombin'
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Journal articles on the topic "Antithrombin"
Izaguirre, Gonzalo, Richard Swanson, Srikumar M. Raja, Alireza R. Rezaie, and Steven T. Olson. "Mechanism by Which Exosites Promote the Inhibition of Blood Coagulation Proteases by Heparin-activated Antithrombin." Journal of Biological Chemistry 282, no. 46 (September 17, 2007): 33609–22. http://dx.doi.org/10.1074/jbc.m702462200.
Full textZhou, Aiwu, James A. Huntington, and Robin W. Carrell. "Formation of the Antithrombin Heterodimer In Vivo and the Onset of Thrombosis." Blood 94, no. 10 (November 15, 1999): 3388–96. http://dx.doi.org/10.1182/blood.v94.10.3388.422k20_3388_3396.
Full textChang, Wun-Shaing W., and Paul L. Harper. "Commercial Antithrombin Concentrate Contains Inactive L-forms of Antithrombin." Thrombosis and Haemostasis 77, no. 02 (1997): 323–28. http://dx.doi.org/10.1055/s-0038-1655962.
Full textZhang, Weiqing, Yung-Jen Chuang, Richard Swanson, Juan Li, Kyunga Seo, Lawrence Leung, Lester F. Lau, and Steven T. Olson. "Antiangiogenic antithrombin down-regulates the expression of the proangiogenic heparan sulfate proteoglycan, perlecan, in endothelial cells." Blood 103, no. 4 (February 15, 2004): 1185–91. http://dx.doi.org/10.1182/blood-2003-08-2920.
Full textKaneider, Nicole C., Christina M. Reinisch, Stefan Dunzendorfer, Jürgen Römisch, and Christian J. Wiederman. "Syndecan-4 mediates antithrombin-induced chemotaxis of human peripheral blood lymphocytes and monocytes." Journal of Cell Science 115, no. 1 (January 1, 2002): 227–36. http://dx.doi.org/10.1242/jcs.115.1.227.
Full textGeorge, PM, P. Pemberton, IC Bathurst, RW Carrell, HL Gibson, S. Rosenberg, RA Hallewell, and PJ Barr. "Characterization of antithrombins produced by active site mutagenesis of human alpha 1-antitrypsin expressed in yeast." Blood 73, no. 2 (February 1, 1989): 490–96. http://dx.doi.org/10.1182/blood.v73.2.490.490.
Full textGeorge, PM, P. Pemberton, IC Bathurst, RW Carrell, HL Gibson, S. Rosenberg, RA Hallewell, and PJ Barr. "Characterization of antithrombins produced by active site mutagenesis of human alpha 1-antitrypsin expressed in yeast." Blood 73, no. 2 (February 1, 1989): 490–96. http://dx.doi.org/10.1182/blood.v73.2.490.bloodjournal732490.
Full textNavarro-Fernández, José, María Morena-Barrio, José Padilla, Antonia Miñano, Nataliya Bohdan, Sonia Águila, Irene Martínez-Martínez, et al. "Antithrombin Dublin (p.Val30Glu): a relatively common variant with moderate thrombosis risk of causing transient antithrombin deficiency." Thrombosis and Haemostasis 116, no. 07 (January 2016): 146–54. http://dx.doi.org/10.1160/th15-11-0871.
Full textKOIDE, Takehiko. "Antithrombin." Journal of Japan Atherosclerosis Society 23, no. 10 (1996): 573–79. http://dx.doi.org/10.5551/jat1973.23.10_573.
Full textRoemisch, J., E. Gray, J. N. Hoffmann, and C. J. Wiedermann. "Antithrombin." Blood Coagulation& Fibrinolysis 13, no. 8 (December 2002): 657–70. http://dx.doi.org/10.1097/00001721-200212000-00001.
Full textDissertations / Theses on the topic "Antithrombin"
Skinner, Richard. "Structural biology of antithrombin." Thesis, University of Cambridge, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.627475.
Full textBruce, David. "Antithrombin : structural variants and thrombosis." Thesis, Open University, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.386084.
Full textFitton, Hazel Louise. "Modulation of antithrombin by heparin." Thesis, University of Cambridge, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.624993.
Full textJin, L. "Antithrombin structures and the heparin pentasaccharide." Thesis, University of Cambridge, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.605606.
Full textChristey, Peter B. "Heparin binding and activation of antithrombin." Thesis, University of Cambridge, 1989. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.315820.
Full textCORNO, ANNA ROSA. "CARENZA CONGENITA DI ANTITROMBINA E DIAGNOSI DI LABORTORIO: QUALE TEST FUNZIONALE?" Doctoral thesis, Università degli Studi di Milano, 2014. http://hdl.handle.net/2434/233996.
Full textIntroduction – Antithrombin (AT) deficiency, associated with an increased risk for venous thrombosis, is classified into type I (quantitative defect) and type II (qualitative defect). Qualitative defects may affect the reactive site (RS), the heparin binding site (HBS) of AT, or they may have a pleiotropic effect (PE). Screening tests, which measure the ability of AT, in the presence of heparin, to inhibits either thrombin (anti-IIa activity) or FXa (anti-Xa activity), are able to detect most AT deficiencies; however, few cases of discrepancies have been described (i.e. normal vs. pathological value) with the two different methods. Aim of the study was the evaluation of agreement between an anti-Xa assay and an anti-IIa assay for AT, and the evaluation of their ability in detecting AT defects. Materials and Methods – The study population consisted of the “routine and thrombophilic” group (493 patients for which AT test was required) and the “historical deficiencies” group (23 subjects with known AT deficiency and 18 relatives). Anti-Xa HemosIL Antithrombin kit (from Instrumentation Laboratory) and a home-made anti-IIa method were used to measure AT activities. A control group (n= 100) was used to determine AT reference ranges. SERPINC1 gene analysis was carried out for 21 patients (Universitair Ziekenhuis in Bruxelles). Results – The results provided by the two methods showed a high correlation (Spearman rho>0.70); however, 8 discrepant results were observed (3 in the “routine and thrombophilia” group and 5 in the “historical deficiencies” group). Gene analysis confirmed the presence of a molecular defect in 18/21 subjects, 5 of which had also descrepant AT results. In fact, normal anti-Xa AT values were obtained for Cambridge II defect (RS), whereas anti-IIa test provided normal values for a HBS defect. Both methods provided pathological AT values for 5 type I deficiencies but normal AT values for other 2 HBS defects. In the study population AT anti-Xa and AT anti-IIa sensitivity was 61.1% and 55.6%, respectively; when both tests were used, sensitivity increased to 72.2%. When the ratio between AT anti-IIa and AT anti-Xa was added, sensitivity increased to 88.9%. Conclusions – Currently avaible screening tests are not able to detect all molecular defects. However, when anti-Xa assay is carried out together with anti-IIa method, and the ratio between the results provided by both is considered, the diagnostic power is increased. Anyway, laboratory test results should be considered together with personal and familiar clinical history of the single subject under evaluation.
Chen, Iris Ye Wu. "The interactions between human antithrombin and heparin." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1998. http://www.collectionscanada.ca/obj/s4/f2/dsk1/tape10/PQDD_0005/NQ42731.pdf.
Full textPerry, David James. "The genetic basis of human antithrombin deficiency." Thesis, University of Cambridge, 1993. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.283014.
Full textBelzar, Klara Jane. "The allosteric activation of antithrombin by heparin." Thesis, University of Cambridge, 2001. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.621213.
Full textBourti, Yasmine. "Evaluation d'un variant d'antithrombine dans différentes indications thérapeutiques." Thesis, Université Paris-Saclay (ComUE), 2016. http://www.theses.fr/2016SACLS404/document.
Full textOur team topic focuses on the structural-function relationship of a natural anticoagulant, antithrombin (AT), in order to develop potential therapeutic agents. AT inhibits several serine proteases of the coagulation cascade and its inhibitory activity is increased when AT binds to a pentasaccharidic motif contained within in the heparin derivatives. At high concentrations (500%), AT also exerts anti-inflammatory and cytoprotective properties through its binding to heparan sulfate proteoglycans, making it a good candidate for supportive therapy in clinical settings associating inflammation and coagulation activation. Indeed, AT has already been evaluated in vivo in various models of ischemia-reperfusion injury (IRI) and AT even reached a large-scale clinical trial in severe sepsis. However, the high concentrations of AT that are needed to exert anti-inflammatory properties are inconsistent with the safety profile of this anticoagulant protein.In this context we have further characterized an AT variant (AT-N135Q-Pro394) with increased affinity to heparin but devoid of anticoagulant activity. Indeed, this variant was described to be able to trap heparin derivatives and our work was to pursue the characterization of this variant as an antidote toward heparin derivatives in clinical situations of overdosing. In addition, this AT variant binds to heparan sulfate proteoglycans with higher affinity, as compared to native AT, and appears as a promising cytoprotective agent whose administration would not be associated with any bleeding risk.To test the latter hypothesis, we developed a murine model of renal IRI in which the renal function was severely impaired, as attested by increased kidney injury markers (urea, creatinine, kim-1) and local kidney inflammation (renal gene expression of il-6 and cxcl-1). Indeed, in 2003, Mizutani et al. reported a protective effect of AT in a similar murine model of renal IRI. Surprisingly, we observed none of the described protective effects, neither on inflammation nor renal function, with plasma AT, recombinant AT and an equimolar mixture of native and latent AT. Nevertheless, the same model enabled us to highlight the nephroprotective and anti-inflammatory properties of another anticoagulant protein, activated protein C (APC), as previously reported. These disappointing results coincided with the withdrawal in 2013 of the study of Mizutani et al., and our work allowed us to clarify the literature and to claim that neither recombinant nor plasma-derived native nor latent forms of AT exhibit a protective effect in renal IRI in mice. Under these conditions, AT-N135Q-Pro394 variant has not been tested in our model.AT-N135Q-Pro394 has also been previously shown to efficiently neutralise the anticoagulant activity of heparin derivatives, including unfractionated heparin (UFH), low molecular weight heparins (LMWH) and fondaparinux in vivo. Nevertheless, this reversal effect was only explored by anti-factor Xa assays whereas AT inhibits a number of coagulation proteases, including factors VIIa, IXa and IIa. Therefore, we explored AT-N135Q-Pro394 variant in a more global coagulation assay, the thrombin-generation assay (TGA), in order to compare its activity with non-specific reversal agents used toward heparin derivative overdose (recombinant-activated factor VII, activated prothrombin-complex concentrate or protamine). Interestingly, in plasma mimicking an overdose, our variant demonstrated greater reversal efficiency as compared to hemostatic agents and protamine sulfate toward fondaparinux and LMWH, respectively, and was as efficient as protamine sulfate toward UFH. Finally, when added to native plasma (in the absence of heparin derivative), AT-N135Q-Pro394 showed no effect on thrombin generation unlike hemostatics and protamine sulfate that all significantly affect the TGA profile
Books on the topic "Antithrombin"
Sas, Géza. The biology of antithrombins. Boca Raton, Fla: CRC Press, 1990.
Find full textWeilemann, L. S., and H. Schinzel, eds. Antithrombin — Diagnostik und Therapie. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-60305-1.
Full textSas, Géza. The biology of antithrombins. Boca Raton, Fla: CRC Press, 1990.
Find full textLantbruksuniversitet, Sveriges, ed. Why does Heparin bind antithrombin? Uppsala: Sveriges Lantbruksuniversitet, 1988.
Find full textRamirez, Pablo Antonio Rivera. Messung der Antithrombin III-aktivität bei der Katze: Referenzbereich und Veränderung bei verschiedenen Erkrankungen. Hannover: s.n., 1997.
Find full textSharma, Anupama. A comparison of the binding abilities of human kidney heparan sulphate and heparin glycosaminoglycans for antithrombin III. Manchester: University of Manchester, 1995.
Find full textGrebe, Susanne. Pharmakokinetik von intravenös und subkutan verabreichtem niedermolekularen Heparin beim Hund: Wirkung auf Thrombinzeit, aktivierte partielle Thromboplastinzeit, Resonanzthrombogramm und Antithrombin-III-Aktivität. Hannover: [s.n.], 1999.
Find full textJacobs, Christina. Pharmakokinetik von intravenös und subkutan verabreichtem unfraktionierten Heparin beim Hund: Wirkung auf aktivierte partielle Thromboplastinzeit, Thrombinzeit, Resonanzthrombogramm und Antithrombin-III-Aktivität. Hannover: [s.n.], 1999.
Find full textRoque, Pifarré, ed. New anticoagulants for the cardiovascular patient. Philadelphia: Hanley & Belfus, 1997.
Find full textWeilemann, L. S., and H. Schinzel. Antithrombin - Diagnostik und Therapie. Springer Berlin / Heidelberg, 1997.
Find full textBook chapters on the topic "Antithrombin"
Björk, Ingemar, and Steven T. Olson. "Antithrombin." In Advances in Experimental Medicine and Biology, 17–33. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-5391-5_3.
Full textHepner, Mirta, and Vasiliki Karlaftis. "Antithrombin." In Haemostasis, 355–64. Totowa, NJ: Humana Press, 2013. http://dx.doi.org/10.1007/978-1-62703-339-8_28.
Full textNess, SallyAnne L., and Marjory B. Brooks. "Antithrombin." In Interpretation of Equine Laboratory Diagnostics, 141–42. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2017. http://dx.doi.org/10.1002/9781118922798.ch21.
Full textSchuster, H. P., and S. Knaub. "Antithrombin III." In Intensivtherapie bei Sepsis und Multiorganversagen, 191–208. Berlin, Heidelberg: Springer Berlin Heidelberg, 2000. http://dx.doi.org/10.1007/978-3-662-07962-1_8.
Full textStief, T. "Antithrombin-3." In Lexikon der Medizinischen Laboratoriumsdiagnostik, 1–2. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-49054-9_253-1.
Full textStief, T. "Antithrombin-3." In Springer Reference Medizin, 177–79. Berlin, Heidelberg: Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_253.
Full textBrown, James P. R., and Joanne Douglas. "Antithrombin Deficiency." In Consults in Obstetric Anesthesiology, 39–40. Cham: Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-59680-8_10.
Full textScharnagl, Hubert, Winfried März, Markus Böhm, Thomas A. Luger, Federico Fracassi, Alessia Diana, Thomas Frieling, et al. "Antithrombin Deficiency." In Encyclopedia of Molecular Mechanisms of Disease, 109–10. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_122.
Full textRiess, H. "Hereditärer Antithrombin-Mangel." In Antithrombin — Diagnostik und Therapie, 21–29. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-60305-1_3.
Full textPindur, G. "Antithrombin und Sepsis." In Antithrombin — Diagnostik und Therapie, 31–38. Berlin, Heidelberg: Springer Berlin Heidelberg, 1998. http://dx.doi.org/10.1007/978-3-642-60305-1_4.
Full textConference papers on the topic "Antithrombin"
Knoller, S., and N. Savion. "MODULATION OF ANTITHROMBIN III ACTIVITY AND ANTITHROMBIN III-THROMBIN COMPLEXES BINDING TO CULTURED CELLS BY MONOCLONAL ANTIBODIES AGAINST ANTITHROMBIN III." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644361.
Full textSamama, J. P., M. Delarue, D. Moras, M. Petitou, J. C. Lormeau, and J. Choay. "CRYSTALLOGRAPHIC INVESTIGATION OF ANTITHROMBIN III." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643765.
Full textde Moerloose, Ph, G. Reber, Ph Minazio, and C. A. Bouvier. "ANTITHROMBIN III GENEVA : AN HEREDITARY ABNORMAL ANTITHROMBIN III (AT III) WITH DEFECTIVE HEPARIN COFACTOR ACTIVITY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644367.
Full textAsakura, S., N. Yoshida, and M. Matsuda. "MONOCLONAL ANTIBODIES AGAINST THROHBIN-ANTITHROMBIN III COMPLEX: EPITOPE SPECIFICITY AND EFFECT ON THROMBIN-ANTITHROMBIN III INTERACTION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643673.
Full textBaruch, D., J. Franssen, H. C. Hemker, and T. Lindhout. "THE ROLE OF HEPARIN CHARGE DENSITY IN THE ANTITHROMBIN III-DEPENDENT AND ANTITHROMBIN III-INDEPENDENT INACTIVATION OF THROMBIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644357.
Full textJordan, R. E., J. Kilpatrick, J. Nelson, J. O. New gren, and M. A. Fournel. "HEPARIN DIRECTS THE INACTIVATION OF ANTITHROMBIN BY ELASTASE." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643770.
Full textSchober, S., C. Deppisch, U. Holzer, R. Handgretinger, U. Ernemann, N. Kaiser, V. Icheva, and G. Wiegand. "Congenital Antithrombin Deficiency Type II: A Case Report." In 63rd Annual Meeting of the Society of Thrombosis and Haemostasis Research. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1680210.
Full textGoto, T., D. Kudo, R. Uchimido, K. Yamakawa, M. Hayakawa, S. Kushimoto, and H. Yasunaga. "Sepsis Phenotypes and the Effect of Antithrombin III." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a6006.
Full textKarges, H. E., G. Zettlemeiβl, H. Naumann, U. Eberhard, and M. Bröker. "PURIFICATION AND CHARACTERIZATION OF GENTECHNOLOGICALLY PREPARED ANTITHROMBIN III." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643684.
Full textsoons, H., T. Jansen-claessen, G. C. Tans, and H. C. Hemker. "HEPARIN CATALYZED FACTOR XIa INHIBITION BY ANTITHROMBIN III." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643768.
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