Biomolecules & Therapeutics

  • 제25권5호
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  • Pages.461-470
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  • 2017
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  • 1976-9148(pISSN)
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  • 2005-4483(eISSN)
한국응용약물학회 (The Korean Society of Applied Pharmacology)
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New Anticoagulants for the Prevention and Treatment of Venous Thromboembolism

  • Kim, Joo Hee (College of Pharmacy & Institute of Pharmaceutical Science and Technology, Ajou University) ;
  • Lim, Kyung-Min (College of Pharmacy, Ewha Womans University) ;
  • Gwak, Hye Sun (College of Pharmacy, Ewha Womans University)
  • 투고 : 2016.12.11
  • 심사 : 2017.01.26
  • 발행 : 2017.09.01
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초록

Anticoagulant drugs, like vitamin K antagonists and heparin, have been the mainstay for the treatment and prevention of venous thromboembolic disease for many years. Although effective if appropriately used, traditional anticoagulants have several limitations such as unpredictable pharmacologic and pharmacokinetic responses and various adverse effects including serious bleeding complications. New oral anticoagulants have recently emerged as an alternative because of their rapid onset/offset of action, predictable linear dose-response relationships and fewer drug interactions. However, they are still associated with problems such as bleeding, lack of reversal agents and standard laboratory monitoring. In an attempt to overcome these drawbacks, key steps of the hemostatic pathway are investigated as targets for anticoagulation. Here we reviewed the traditional and new anticoagulants with respect to their targets in the coagulation cascade, along with their therapeutic advantages and disadvantages. In addition, investigational anticoagulant drugs currently in the development stages were introduced.

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참고문헌

  1. Abraham, E., Reinhart, K., Opal, S., Demeyer, I., Doig, C., Rodriguez, A. L., Beale, R., Svoboda, P., Laterre, P. F., Simon, S., Light, B., Spapen, H., Stone, J., Seibert, A., Peckelsen, C., De Deyne, C., Postier, R., Pettila, V., Sprung, C. L., Artigas, A., Percell, S. R., Shu, V., Zwingelstein, C., Tobias, J., Poole, L., Stolzenbach, J. C. and Creasey, A. A. (2003) Efficacy and safety of tifacogin (recombinant tissue factor pathway inhibitor) in severe sepsis: A randomized controlled trial. JAMA 290, 238-247. https://doi.org/10.1001/jama.290.2.238
  2. Ageno, W., Gallus, A. S., Wittkowsky, A., Crowther, M., Hylek, E. M. and Palareti, G. (2012) Oral anticoagulant therapy: antithrombotic therapy and prevention of thrombosis, 9th ed: American college of chest physicians evidence-based clinical practice guidelines. Chest 141, e44S-e88S. https://doi.org/10.1378/chest.11-2292
  3. Ahmed, Z., Hassan, S. and Salzman, G. A. (2016) Novel oral anticoagulants for venous thromboembolism with special emphasis on risk of hemorrhagic complications and reversal agents. Curr. Drug Ther. 11, 3-20. https://doi.org/10.2174/1574885511666160421145036
  4. Amiral, J., Bridey, F., Wolf, M., Boyer-Neumann, C., Fressinaud, E., Vissac, A. M., Peynaud-Debayle, E., Dreyfus, M. and Meyer, D. (1995) Antibodies to macromolecular platelet factor 4-heparin complexes in heparin-induced thrombocytopenia: a study of 44 cases. Thromb. Haemost. 73, 21-28. https://doi.org/10.1055/s-0038-1651670
  5. Bates, S. M. and Weitz, J. I. (2000) The mechanism of action of thrombin inhibitors. J. Invasive Cardiol. 12 Suppl F, 27F-32.
  6. Baumann Kreuziger, L. M., Keenan, J. C., Morton, C. T. and Dries, D. J. (2014) Management of the bleeding patient receiving new oral anticoagulants: A role for prothrombin complex concentrates. BioMed Res. Int. 2014, 583794.
  7. Bea, F., Kreuzer, J., Preusch, M., Schaab, S., Isermann, B., Rosenfeld, M. E., Katus, H. and Blessing, E. (2006) Melagatran reduces advanced atherosclerotic lesion size and may promote plaque stability in apolipoprotein E-deficient mice. Arterioscler. Thromb. Vasc. Biol. 26, 2787-2792. https://doi.org/10.1161/01.ATV.0000246797.05781.ad
  8. Bounameaux, H. and Camm, A. J. (2014) Edoxaban: an update on the new oral direct factor Xa inhibitor. Drugs 74, 1209-1231. https://doi.org/10.1007/s40265-014-0261-1
  9. Bruni-Fitzgerald, K. R. (2015) Venous thromboembolism: an overview. J. Vasc. Nurs. 33, 95-99. https://doi.org/10.1016/j.jvn.2015.02.001
  10. Butenas, S., Brummel, K. E., Branda, R. F., Paradis, S. G. and Mann, K. G. (2002) Mechanism of factor VIIa-dependent coagulation in hemophilia blood. Blood 99, 923-930. https://doi.org/10.1182/blood.V99.3.923
  11. Buller, H. R., Bethune, C., Bhanot, S., Gailani, D., Monia, B. P., Raskob, G. E., Segers, A., Verhamme, P. and Weitz, J. I. (2015) Factor XI antisense oligonucleotide for prevention of venous thrombosis. N. Engl. J. Med. 372, 232-240. https://doi.org/10.1056/NEJMoa1405760
  12. Cabral, K. P. and Ansell, J. E. (2015) The role of factor Xa inhibitors in venous thromboembolism treatment. Vasc. Health Risk Manage. 11, 117-123.
  13. Chapin, J. C. and Hajjar, K. A. (2015) Fibrinolysis and the control of blood coagulation. Blood Rev. 29, 17-24. https://doi.org/10.1016/j.blre.2014.09.003
  14. Chow, F. S., Benincosa, L. J., Sheth, S. B., Wilson, D., Davis, C. B., Minthorn, E. A. and Jusko, W. J. (2002) Pharmacokinetic and pharmacodynamic modeling of humanized anti-factor IX antibody (SB 249417) in humans. Clin. Pharmacol. Ther. 71, 235-245. https://doi.org/10.1067/mcp.2002.122276
  15. Connolly, G. and Spyropoulos, A. C. (2013) Practical issues, limitations, and periprocedural management of the NOAC's. J. Thromb. Thrombolysis 36, 212-222. https://doi.org/10.1007/s11239-013-0911-2
  16. Connors, J. M. (2015) Antidote for factor Xa anticoagulants. N. Engl. J. Med. 373, 2471-2472. https://doi.org/10.1056/NEJMe1513258
  17. Coughlin, S. R. (1994) Thrombin receptor function and cardiovascular disease. Trends Cardiovasc. Med. 4, 77-83. https://doi.org/10.1016/1050-1738(94)90013-2
  18. Das, A. and Liu, D. (2015) Novel antidotes for target specific oral anticoagulants. Exp. Hematol. Oncol. 4, 25. https://doi.org/10.1186/s40164-015-0020-3
  19. Dellinger, R. P. (2003) Inflammation and coagulation: Implications for the septic patient. Clin. Infect. Dis. 36, 1259-1265. https://doi.org/10.1086/374835
  20. Dickinson, C. D. and Ruf, W. (1997) Active site modification of factor VIIa affects interactions of the protease domain with tissue factor. J. Biol. Chem. 272, 19875-19879. https://doi.org/10.1074/jbc.272.32.19875
  21. Di Nisio, M., Middeldorp, S. and Buller, H. R. (2005) Direct thrombin inhibitors. N. Engl. J. Med. 353, 1028-1040. https://doi.org/10.1056/NEJMra044440
  22. Eriksson, B. I., Quinlan, D. J. and Weitz, J. I. (2009) Comparative pharmacodynamics and pharmacokinetics of oral direct thrombin and factor Xa inhibitors in development. Clin. Pharmacokinet. 48, 1-22. https://doi.org/10.2165/0003088-200948010-00001
  23. Esmon, C. T. (2005) The interactions between inflammation and coagulation. Br. J. Haematol. 131, 417-430. https://doi.org/10.1111/j.1365-2141.2005.05753.x
  24. Evans, H. C., Perry, C. M. and Faulas, D. (2004) Ximelagatran/melagatran. Drugs 64, 649-678. https://doi.org/10.2165/00003495-200464060-00010
  25. Fareed, J., Hoppensteadt, D. A., Fareed, D., Demir, M., Wahi, R., Clarke, M., Adiguzel, C. and Bick, R. (2008) Survival of heparins, oral anticoagulants, and aspirin after the year 2010. Semin. Thromb. Hemost. 34, 58-73.
  26. Fitzmaurice, D. A., Blann, A. D. and Lip, G. Y. H. (2002) Bleeding risks of antithrombotic therapy. BMJ 325, 828-831. https://doi.org/10.1136/bmj.325.7368.828
  27. Franchini, M., Liumbruno, G. M., Bonfanti, C. and Lippi, G. (2016) The evolution of anticoagulant therapy. Blood Transfus. 14, 175-184.
  28. Fung, E., Patsopoulos, N. A., Belknap, S. M., O'Rourke, D. J., Robb, J. F., Anderson, J. L., Shworak, N. W. and Moore, J. H. (2012) Effect of genetic variants, especially CYP2C9 and VKORC1, on the pharmacology of warfarin. Semin. Thromb. Hemost. 38, 893-904.
  29. Gandhi, N. S. and Mancera, R. L. (2010) Heparin/heparan sulphatebased drugs. Drug Discov. Today 15, 1058-1069. https://doi.org/10.1016/j.drudis.2010.10.009
  30. Garcia, D. A., Baglin, T. P., Weitz, J. I. and Samama, M. M. (2012) Parenteral anticoagulants: antithrombotic therapy and prevention of thrombosis, 9th ed: American college of chest physicians evidence-based clinical practice guidelines. Chest 141, e24S-e43S. https://doi.org/10.1378/chest.11-2291
  31. Greinacher, A., Thiele, T. and Selleng, K. (2015) Reversal of anticoagulants: an overview of current developments. Thromb. Haemost. 113, 931-942. https://doi.org/10.1160/TH14-11-0982
  32. Hagedorn, I., Schmidbauer, S., Pleines, I., Kleinschnitz, C., Kronthaler, U., Stoll, G., Dickneite, G. and Nieswandt, B. (2010) Factor XIIa inhibitor recombinant human albumin Infestin-4 abolishes occlusive arterial thrombus formation without affecting bleeding. Circulation 121, 1510-1517. https://doi.org/10.1161/CIRCULATIONAHA.109.924761
  33. Hardy, S., Schirm, S., Liu, X. and Dai, Y. (2006) Tifacogin increases bacterial clearance from blood. Crit. Care 10, P155. https://doi.org/10.1186/cc4993
  34. Heit, J. A., Spencer, F. A. and White, R. H. (2016) The epidemiology of venous thromboembolism. J. Thromb. Thrombolysis 41, 3-14. https://doi.org/10.1007/s11239-015-1311-6
  35. Hirsh, J. (1991) Heparin. N. Engl. J. Med. 324, 1565-1574. https://doi.org/10.1056/NEJM199105303242206
  36. Hirsh, J. (1998) Low-molecular-weight heparin. Circulation 98, 1575-1582. https://doi.org/10.1161/01.CIR.98.15.1575
  37. Hirsh, J., Fuster, V., Ansell, J. and Halperin, J. L. (2003) American heart association/American college of cardiology foundation guide to warfarin therapy. J. Am. Coll. Cardiol. 41, 1633-1652. https://doi.org/10.1016/S0735-1097(03)00416-9
  38. Hirsh, J., O'Donnell, M. and Eikelboom, J. W. (2007) Beyond unfractionated heparin and warfarin: current and future advances. Circulation 116, 552-560. https://doi.org/10.1161/CIRCULATIONAHA.106.685974
  39. Hirsh, J. and Fuster, V. (1994) Guide to anticoagulant therapy. Part I: heparin. Circulation. 89, 1449-1468. https://doi.org/10.1161/01.CIR.89.3.1449
  40. Hirsh, J. and Raschke, R. (2004) Heparin and low-molecular-weight heparin: The seventh ACCP conference on antithrombotic and thrombolytic therapy. Chest 126, 188S-203S. https://doi.org/10.1378/chest.126.3_suppl.188S
  41. Holmer, E., Soderberg, K., Bergqvist, D. and Lindahl, U. (1986) Heparin and its low molecular weight derivatives: Anticoagulant and antithrombotic properties. Haemostasis 16 Suppl 2, 1-7.
  42. Hoppensteadt, D., Walenga, J. M., Fareed, J. and Bick, R. L. (2003) Heparin, low-molecular-weight heparins, and heparin pentasaccharide: Basic and clinical differentiation. Hematol. Oncol. Clin. North Am. 17, 313-341. https://doi.org/10.1016/S0889-8588(02)00091-6
  43. Howard, E. L., Becker, K. C. D., Rusconi, C. P. and Becker, R. C. (2007) Factor IXa inhibitors as novel anticoagulants. Arterioscler. Thromb. Vasc. Biol. 27, 722-727. https://doi.org/10.1161/01.ATV.0000259363.91070.f1
  44. Hu, T. Y., Vaidya, V. R. and Asirvatham, S. J. (2016) Reversing anticoagulant effects of novel oral anticoagulants: Role of ciraparantag, andexanet alfa, and idarucizumab. Vasc. Health Risk Manag. 12, 35-44.
  45. Hyers, T. M. (1999) Venous thromboembolism. Am. J. Respir. Crit. Care Med. 159, 1-14. https://doi.org/10.1164/ajrccm.159.1.9803109
  46. Kearon, C., Comp, P., Douketis, J., Royds, R., Yamada, K. and Gent, M. (2005) Dose-response study of recombinant human soluble thrombomodulin (ART-123) in the prevention of venous thromboembolism after total hip replacement. J. Thrombo Haemost. 3, 962-968. https://doi.org/10.1111/j.1538-7836.2005.01251.x
  47. Kim, J. H., Lee, J., Kang, S., Moon, H., Chung, K. H. and Kim, K. R. (2016) Antiplatelet and antithrombotic effects of the extract of lindera obtusiloba leaves. Biomol. Ther. (Seoul) 24, 659-664. https://doi.org/10.4062/biomolther.2016.021
  48. Koster, A., Fischer, K. G., Harder, S. and Mertzlufft, F. (2007) The direct thrombin inhibitor argatroban: a review of its use in patients with and without HIT. Biologics 1, 105-112.
  49. Kreimann, M., Brandt, S., Krauel, K., Block, S., Helm, C. A., Weitschies, W., Greinacher, A. and Delcea, M. (2014) Binding of anti-platelet factor 4/heparin antibodies depends on the thermodynamics of conformational changes in platelet factor 4. Blood 124, 2442-2449. https://doi.org/10.1182/blood-2014-03-559518
  50. Krishnaswamy, A., Lincoff, A. M. and Cannon, C. P. (2010) The use and limitations of unfractionated heparin. Crit. Pathw. Cardiol. 9, 35-40. https://doi.org/10.1097/HPC.0b013e3181d29713
  51. Kwon, I. S., Yim, J. H., Lee, H. K. and Pyo, S. (2016) Lobaric acid inhibits VCAM-1 expression in TNF-alpha-stimulated vascular smooth muscle cells via modulation of NF-kappaB and MAPK signaling pathways. Biomol. Ther. (Seoul) 24, 25-32. https://doi.org/10.4062/biomolther.2015.084
  52. Laterre, P. F., Opal, S. M., Abraham, E., LaRosa, S. P., Creasey, A. A., Xie, F., Poole, L. and Wunderink, R. G. (2009) A clinical evaluation committee assessment of recombinant human tissue factor pathway inhibitor (tifacogin) in patients with severe community-acquired pneumonia. Critic. Care 13, R36. https://doi.org/10.1186/cc7747
  53. Lee, C. J. and Ansell, J. E. (2011) Direct thrombin inhibitors. Br. J. Clin. Pharmacol. 72, 581-592. https://doi.org/10.1111/j.1365-2125.2011.03916.x
  54. Lee, D. H., Kim, H. H., Lim, D. H., Kim, J. L. and Park, H. J. (2015) Effect of cordycepin-enriched WIB801C from cordyceps militaris suppressing fibrinogen binding to glycoprotein IIb/IIIa. Biomol. Ther. (Seoul) 23, 60-70. https://doi.org/10.4062/biomolther.2014.086
  55. Lenting, P. J., van Mourik, J. A. and Mertens, K. (1998) The life cycle of coagulation factor VIII in view of its structure and function. Blood 92, 3983-3996.
  56. Liaw, P. C., Becker, D. L., Stafford, A. R., Fredenburgh, J. C. and Weitz, J. I. (2001) Molecular basis for the susceptibility of fibrinbound thrombin to inactivation by heparin cofactor II in the presence of dermatan sulfate but not heparin. J. Biol. Chem. 276, 20959-20965. https://doi.org/10.1074/jbc.M010584200
  57. Linkins, L. A., Choi, P. T. and Douketis, J. D. (2003) Clinical impact of bleeding in patients taking oral anticoagulant therapy for venous thromboembolism: A meta-analysis. Ann. Intern. Med. 139, 893-900. https://doi.org/10.7326/0003-4819-139-11-200312020-00007
  58. Loke, C., Ali, S. S. and Johari, V. (2012) Pharmacology of anticoagulants. Dis. Mon. 58, 424-430. https://doi.org/10.1016/j.disamonth.2012.04.005
  59. Lurie, Y., Loebstein, R., Kurnik, D., Almog, S. and Halkin, H. (2010) Warfarin and vitamin K intake in the era of pharmacogenetics. Br. J. Clin. Pharmacol. 70, 164-170. https://doi.org/10.1111/j.1365-2125.2010.03672.x
  60. Majeed, A. and Schulman, S. (2013) Bleeding and antidotes in new oral anticoagulants. Best Pract. Res. Clin. Haematol. 26, 191-202. https://doi.org/10.1016/j.beha.2013.07.001
  61. Mann, K. G., Brummel, K. and Butenas, S. (2003) What is all that thrombin for? J. Thromb. Haemost. 1, 1504-1514. https://doi.org/10.1046/j.1538-7836.2003.00298.x
  62. Marmur, J. D. (2002) Direct versus indirect thrombin inhibition in percutaneous coronary intervention. J. Invasive Cardiol. 14 Suppl B, 8B-18B.
  63. Masuko, S. and Linhardt, R. J. (2012) Chemoenzymatic synthesis of the next generation of ultralow MW heparin therapeutics. Future Med. Chem. 4, 289-296. https://doi.org/10.4155/fmc.11.185
  64. Matyal, R., Mahmood, F. and Park, K. W. (2005) Tifacogin, recombinant tissue factor pathway inhibitor. Int. Anesthesiol. Clin. 43, 135-144. https://doi.org/10.1097/01.aia.0000157499.41843.a3
  65. Mega, J. L. and Simon, T. (2015) Pharmacology of antithrombotic drugs: an assessment of oral antiplatelet and anticoagulant treatments. Lancet 386, 281-291. https://doi.org/10.1016/S0140-6736(15)60243-4
  66. Mekaj, Y. H., Mekaj, A. Y., Duci, S. B. and Miftari, E. I. (2015) New oral anticoagulants: their advantages and disadvantages compared with vitamin K antagonists in the prevention and treatment of patients with thromboembolic events. Ther. Clin. Risk Manag. 11, 967-977.
  67. Merli, G. J. and Groce, J. B. (2010) Pharmacological and clinical differences between low-molecular-weight heparins: Implications for prescribing practice and therapeutic interchange. P. T. 35, 95-105.
  68. Miller, C. S., Grandi, S. M., Shimony, A., Filion, K. B. and Eisenberg, M. J. (2012) Meta-analysis of efficacy and safety of new oral anticoagulants (dabigatran, rivaroxaban, apixaban) versus warfarin in patients with atrial fibrillation. Am. J. Cardio. 110, 453-460. https://doi.org/10.1016/j.amjcard.2012.03.049
  69. Nawarskas, J. J. and Anderson, J. R. (2001) Bivalirudin: A new approach to anticoagulation. Heart Dis. 3, 131-137.
  70. Park, J. M., Chang, K. H., Park, K. H., Choi, S. J., Lee, K., Lee, J. Y., Satoh M., Song S. Y. and Lee, M. Y. (2016) Differential effects between cigarette total particulate matter and cigarette smoke extract on blood and blood vessel. Toxicol. Res. 32, 353-358. https://doi.org/10.5487/TR.2016.32.4.353
  71. Pempe, E. H., Xu, Y., Gopalakrishnan, S., Liu, J. and Harris, E. N. (2012) Probing structural selectivity of synthetic heparin binding to stabilin protein receptors. J. Biol. Chem. 287, 20774-20783. https://doi.org/10.1074/jbc.M111.320069
  72. Perzborn, E., Roehrig, S., Straub, A., Kubitza, D. and Misselwitz, F. (2011) The discovery and development of rivaroxaban, an oral, direct factor Xa inhibitor. Nat. Rev. Drug Discov. 10, 61-75. https://doi.org/10.1038/nrd3185
  73. Piazza, G. and Goldhaber, S. Z. (2010) Venous thromboembolism and atherothrombosis: an integrated approach. Circulation 121, 2146-2150. https://doi.org/10.1161/CIRCULATIONAHA.110.951236
  74. Previtali, E., Bucciarelli, P., Passamonti, S. M. and Martinelli, I. (2011) Risk factors for venous and arterial thrombosis. Blood Transfus. 9, 120-138.
  75. Puurunen, M. K., Gona, P. N., Larson, M. G., Murabito, J. M., Magnani, J. W. and O'Donnell, C. J. (2016) Epidemiology of venous thromboembolism in the framingham heart study. Thromb. Res. 145, 27-33. https://doi.org/10.1016/j.thromres.2016.06.033
  76. Rauova, L., Poncz, M., McKenzie, S. E., Reilly, M. P., Arepally, G., Weisel, J. W., Nagaswami, C., Cines, D. B. and Sachais, B. S. (2005) Ultralarge complexes of PF4 and heparin are central to the pathogenesis of heparin-induced thrombocytopenia. Blood 105, 131-138. https://doi.org/10.1182/blood-2004-04-1544
  77. Rauova, L., Zhai, L., Kowalska, M. A., Arepally, G. M., Cines, D. B. and Poncz, M. (2006) Role of platelet surface PF4 antigenic complexes in heparin-induced thrombocytopenia pathogenesis: diagnostic and therapeutic implications. Blood 107, 2346-2353. https://doi.org/10.1182/blood-2005-08-3122
  78. Roser-Jones, C., Chan, M., Howard, E. L., Becker, K. C., Rusconi, C. P. and Becker, R. C. (2011) Factor IXa as a target for pharmacologic inhibition in acute coronary syndrome. Cardiovasc. Ther. 29, e22-e35. https://doi.org/10.1111/j.1755-5922.2010.00134.x
  79. Ruiz, F. A., Lea, C. R., Oldfield, E. and Docampo, R. (2004) Human platelet dense granules contain polyphosphate and are similar to acidocalcisomes of bacteria and unicellular eukaryotes. J. Biol. Chem. 279, 44250-44257. https://doi.org/10.1074/jbc.M406261200
  80. Ruppert, A., Lees, M. and Steinle, T. (2010) Clinical burden of venous thromboembolism. Curr. Med. Res. Opin. 26, 2465-2473. https://doi.org/10.1185/03007995.2010.516090
  81. Rupprecht, H. J. and Blank, R. (2010) Clinical pharmacology of direct and indirect factor Xa inhibitors. Drugs 70, 2153-2170.
  82. Schmid, P., Fischer, A. G. and Wuillemin, W. A. (2009) Low-molecularweight heparin in patients with renal insufficiency. Swiss Med. Wkly 139, 438-452.
  83. Schroeder, M., Hogwood, J., Gray, E., Mulloy, B., Hackett, A. M. and Johansen, K. B. (2011) Protamine neutralisation of low molecular weight heparins and their oligosaccharide components. Anal. Bioanal. Chem. 399, 763-771. https://doi.org/10.1007/s00216-010-4220-8
  84. Short, N. J. and Connors, J. M. (2014) New oral anticoagulants and the cancer patient. Oncologist 19, 82-93. https://doi.org/10.1634/theoncologist.2013-0239
  85. Sie, P. (2016) Spotlight on idarucizumab and its potential for the reversal of anticoagulant effects of dabigatran. Drug Des. Devel. Ther. 10, 1683-1689.
  86. Smith, S. A., Choi, S. H., Collins, J. N., Travers, R. J., Cooley, B. C. and Morrissey, J. H. (2012) Inhibition of polyphosphate as a novel strategy for preventing thrombosis and inflammation. Blood 120, 5103-5110. https://doi.org/10.1182/blood-2012-07-444935
  87. Smith, S. A. and Morrissey, J. H. (2008) Polyphosphate enhances fibrin clot structure. Blood 112, 2810-2816. https://doi.org/10.1182/blood-2008-03-145755
  88. Stangier, J. and Clemens, A. (2009) Pharmacology, pharmacokinetics, and pharmacodynamics of dabigatran etexilate, an oral direct thrombin inhibitor. Clin. Appl. Thromb. Hemost. 15 Suppl 1, 9S-16S. https://doi.org/10.1177/1076029609343004
  89. Teitel, J. M. and Rosenberg, R. D. (1983) Protection of factor Xa from neutralization by the heparin-antithrombin complex. J. Clin. Invest. 71, 1383-1391. https://doi.org/10.1172/JCI110891
  90. Tollefsen, D. M., Majerus, D. W. and Blank, M. K. (1982) Heparin cofactor II. Purification and properties of a heparin-dependent inhibitor of thrombin in human plasma. J. Biol. Chem. 257, 2162-2169.
  91. Tran, H. A., Chunilal, S. D., Harper, P. L., Tran, H., Wood, E. M. and Gallus, A. S. (2013) An update of consensus guidelines for warfarin reversal. Med. J. Aust. 198, 198-199. https://doi.org/10.5694/mja12.10614
  92. Travers, R. J., Shenoi, R. A., Kalathottukaren, M. T., Kizhakkedathu, J. N. and Morrissey, J. H. (2014) Nontoxic polyphosphate inhibitors reduce thrombosis while sparing hemostasis. Blood 124, 3183-3190. https://doi.org/10.1182/blood-2014-05-577932
  93. Vavalle, J. P. and Cohen, M. G. (2012) The REG1 anticoagulation system: A novel actively controlled factor IX inhibitor using RNA aptamer technology for treatment of acute coronary syndrome. Future Cardiol. 8, 371-382. https://doi.org/10.2217/fca.12.5
  94. Verhamme, P., Pakola, S., Jensen, T. J., Berggren, K., Sonesson, E., Saint-Remy, J. M., Balchen, T., Belmans, A., Cahillane, G., Stassen, J. M., Peerlinck, K., Glazer, S. and Jacquemin, M. (2010) Tolerability and pharmacokinetics of TB-402 in healthy male volunteers. Clin. Ther. 32, 1205-1220. https://doi.org/10.1016/j.clinthera.2010.06.012
  95. Verhoef, T. I., Redekop, W. K., Daly, A. K., van Schie, R. M., de Boer, A. and Maitland-van der Zee, A. H. (2014) Pharmacogenetic-guided dosing of coumarin anticoagulants: algorithms for warfarin, acenocoumarol and phenprocoumon. Br. J. Clin. Pharmacol. 77, 626-641. https://doi.org/10.1111/bcp.12220
  96. Vincent, J. L., Ramesh, M. K., Ernest, D., LaRosa, S. P., Pachl, J., Aikawa, N., Hoste, E., Levy, H., Hirman, J., Levi, M., Daga, M., Kutsogiannis, D. J., Crowther, M., Bernard, G. R., Devriendt, J., Puigserver, J. V., Blanzaco, D. U, Esmon, C. T, Parrillo, J. E., Guzzi, L., Henderson, S. J., Pothirat, C., Mehta, P., Fareed, J., Talwar, D., Tsuruta, K., Gorelick, K. J., Osawa, Y. and Kaul, I. (2013) A randomized, double-blind, placebo-controlled, Phase 2b study to evaluate the safety and efficacy of recombinant human soluble thrombomodulin, ART-123, in patients with sepsis and suspected disseminated intravascular coagulation. Crit. Care Med. 41, 2069-2079. https://doi.org/10.1097/CCM.0b013e31828e9b03
  97. Vlasuk, G. P. and Rote, W. E. (2002) Inhibition of factor VIIa/tissue factor with nematode anticoagulant protein c2: from unique mechanism to a promising new clinical anticoagulant. Trends Cardiovasc. Med. 12, 325-331. https://doi.org/10.1016/S1050-1738(02)00185-8
  98. Walenga, J. M. and Lyman, G. H. (2013) Evolution of heparin anticoagulants to ultra-low-molecular-weight heparins: a review of pharmacologic and clinical differences and applications in patients with cancer. Crit. Rev. Oncol. Hematol. 88, 1-18. https://doi.org/10.1016/j.critrevonc.2013.06.007
  99. Weitz, J. I. (1997) Low-molecular-weight heparins. N. Engl. J. Med. 337, 688-698. https://doi.org/10.1056/NEJM199709043371007
  100. Weitz, J. I., Hudoba, M., Massel, D., Maraganore, J. and Hirsh, J. (1990) Clot-bound thrombin is protected from inhibition by heparinantithrombin III but is susceptible to inactivation by antithrombin III-independent inhibitors. J. Clin. Invest. 86, 385-391. https://doi.org/10.1172/JCI114723
  101. Wessler, S. and Gitel, S. N. (1986) Pharmacology of heparin and warfarin. J. Am. Coll. Cardiol. 8, 10B-20B. https://doi.org/10.1016/S0735-1097(86)80003-1
  102. Wolzt, M., Weltermann, A., Nieszpaur-Los, M., Schneider, B., Fassolt, A., Lechner, K., Eichler, H. G. and Kyrle, P. A. (1995) Studies on the neutralizing effects of protamine on unfractionated and low molecular weight heparin (Fragmin) at the site of activation of the coagulation system in man. Thromb. Haemost. 73, 439-443.
  103. Wood, J. P., Ellery, P. E., Maroney, S. A. and Mast, A. E. (2014) Biology of tissue factor pathway inhibitor. Blood 123, 2934-2943. https://doi.org/10.1182/blood-2013-11-512764
  104. Yeh, C. H., Fredenburgh, J. C. and Weitz, J. I. (2012) Oral direct factor Xa inhibitors. Circ. Res. 111, 1069-1078. https://doi.org/10.1161/CIRCRESAHA.112.276741

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