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Volumn 21, Issue 1, 2007, Pages 33-50

Regulation of Thrombin Activity-Pharmacologic and Structural Aspects

Author keywords

[No Author keywords available]

Indexed keywords

ANTICOAGULANT AGENT; ANTITHROMBIN; ARGATROBAN; CHONDROITIN SULFATE; DERMATAN SULFATE; DROTRECOGIN; FONDAPARINUX; HEPARIN; HEPARIN COFACTOR II; HIRUDIN; HIRULOG; INTIMATAN; LEPIRUDIN; LOW MOLECULAR WEIGHT HEPARIN; MELAGATRAN; MUTANT PROTEIN; PROTAMINE; RECOMBINANT ANTITHROMBIN III; RECOMBINANT THROMBOMODULIN; THROMBIN; THROMBIN INHIBITOR; THROMBOMODULIN; UNCLASSIFIED DRUG; XIMELAGATRAN;

EID: 33846466747     PISSN: 08898588     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.hoc.2006.11.008     Document Type: Review
Times cited : (22)

References (94)
  • 1
    • 17844385569 scopus 로고    scopus 로고
    • New anticoagulants: beyond heparin, low-molecular-weight heparin and warfarin
    • Bates S.M., and Weitz J.I. New anticoagulants: beyond heparin, low-molecular-weight heparin and warfarin. Br J Pharmacol 144 8 (2005) 1017-1028
    • (2005) Br J Pharmacol , vol.144 , Issue.8 , pp. 1017-1028
    • Bates, S.M.1    Weitz, J.I.2
  • 2
    • 0033214353 scopus 로고    scopus 로고
    • "Normal" thrombin generation
    • Butenas S., van't Veer C., and Mann K.G. "Normal" thrombin generation. Blood 94 7 (1999) 2169-2178
    • (1999) Blood , vol.94 , Issue.7 , pp. 2169-2178
    • Butenas, S.1    van't Veer, C.2    Mann, K.G.3
  • 3
    • 0141484541 scopus 로고    scopus 로고
    • Thrombin interactions
    • Di Cera E. Thrombin interactions. Chest 124 3 Suppl (2003) 11S-17S
    • (2003) Chest , vol.124 , Issue.3 SUPPL
    • Di Cera, E.1
  • 4
    • 17644371341 scopus 로고    scopus 로고
    • Exosite-driven substrate specificity and function in coagulation
    • Krishnaswamy S. Exosite-driven substrate specificity and function in coagulation. J Thromb Haemost 3 1 (2005) 54-67
    • (2005) J Thromb Haemost , vol.3 , Issue.1 , pp. 54-67
    • Krishnaswamy, S.1
  • 6
    • 0018869509 scopus 로고
    • Some properties of antithrombin-III and its concentration in human plasma
    • Murano G., Williams L., Miller-Andersson M., et al. Some properties of antithrombin-III and its concentration in human plasma. Thromb Res 18 1-2 (1980) 259-262
    • (1980) Thromb Res , vol.18 , Issue.1-2 , pp. 259-262
    • Murano, G.1    Williams, L.2    Miller-Andersson, M.3
  • 7
    • 0025017717 scopus 로고
    • Evaluation of the safety, recovery, half-life, and clinical efficacy of antithrombin III (human) in patients with hereditary antithrombin III deficiency
    • Menache D., O'Malley J.P., Schorr J.B., et al. Evaluation of the safety, recovery, half-life, and clinical efficacy of antithrombin III (human) in patients with hereditary antithrombin III deficiency. Blood 75 1 (1990) 33-39
    • (1990) Blood , vol.75 , Issue.1 , pp. 33-39
    • Menache, D.1    O'Malley, J.P.2    Schorr, J.B.3
  • 8
    • 0029858330 scopus 로고    scopus 로고
    • Blood clotting in minimally altered whole blood
    • Rand M.D., Lock J.B., van't Veer C., et al. Blood clotting in minimally altered whole blood. Blood 88 9 (1996) 3432-3445
    • (1996) Blood , vol.88 , Issue.9 , pp. 3432-3445
    • Rand, M.D.1    Lock, J.B.2    van't Veer, C.3
  • 9
    • 0036660207 scopus 로고    scopus 로고
    • Thrombin functions during tissue factor-induced blood coagulation
    • Brummel K.E., Paradis S.G., Butenas S., et al. Thrombin functions during tissue factor-induced blood coagulation. Blood 100 1 (2002) 148-152
    • (2002) Blood , vol.100 , Issue.1 , pp. 148-152
    • Brummel, K.E.1    Paradis, S.G.2    Butenas, S.3
  • 10
    • 0034687422 scopus 로고    scopus 로고
    • Structure of a serpin-protease complex shows inhibition by deformation
    • Huntington J.A., Read R.J., and Carrell R.W. Structure of a serpin-protease complex shows inhibition by deformation. Nature 407 6806 (2000) 923-926
    • (2000) Nature , vol.407 , Issue.6806 , pp. 923-926
    • Huntington, J.A.1    Read, R.J.2    Carrell, R.W.3
  • 11
    • 8744274071 scopus 로고    scopus 로고
    • Allosteric activation of antithrombin critically depends upon hinge region extension
    • Langdown J., Johnson D.J.D., Baglin T.P., et al. Allosteric activation of antithrombin critically depends upon hinge region extension. J Biol Chem 279 45 (2004) 47288-47297
    • (2004) J Biol Chem , vol.279 , Issue.45 , pp. 47288-47297
    • Langdown, J.1    Johnson, D.J.D.2    Baglin, T.P.3
  • 12
    • 0033807066 scopus 로고    scopus 로고
    • Complete antithrombin deficiency in mice results in embryonic lethality
    • Ishiguro K., Kojima T., Kadomatsu K., et al. Complete antithrombin deficiency in mice results in embryonic lethality. J Clin Invest 106 7 (2000) 873-878
    • (2000) J Clin Invest , vol.106 , Issue.7 , pp. 873-878
    • Ishiguro, K.1    Kojima, T.2    Kadomatsu, K.3
  • 13
    • 0024447029 scopus 로고
    • Congenital antithrombin III deficiency. Incidence and clinical features
    • Hirsh J., Piovella F., and Pini M. Congenital antithrombin III deficiency. Incidence and clinical features. Am J Med 87 3B (1989) 34S-38S
    • (1989) Am J Med , vol.87 , Issue.3 B
    • Hirsh, J.1    Piovella, F.2    Pini, M.3
  • 14
    • 0026077290 scopus 로고
    • The influence of preoperative anticoagulation on heparin response during cardiopulmonary bypass
    • Dietrich W., Spannagl M., Schramm W., et al. The influence of preoperative anticoagulation on heparin response during cardiopulmonary bypass. J Thorac Cardiovasc Surg 102 4 (1991) 505-514
    • (1991) J Thorac Cardiovasc Surg , vol.102 , Issue.4 , pp. 505-514
    • Dietrich, W.1    Spannagl, M.2    Schramm, W.3
  • 15
    • 0028238483 scopus 로고
    • Heparin resistance after preoperative heparin therapy or intraaortic balloon pumping
    • Staples M.H., Dunton R.F., Karlson K.J., et al. Heparin resistance after preoperative heparin therapy or intraaortic balloon pumping. Ann Thorac Surg 57 5 (1994) 1211-1216
    • (1994) Ann Thorac Surg , vol.57 , Issue.5 , pp. 1211-1216
    • Staples, M.H.1    Dunton, R.F.2    Karlson, K.J.3
  • 16
    • 6444239394 scopus 로고    scopus 로고
    • The effects of argatroban on thrombin generation and hemostatic activation in vitro
    • Tanaka K.A., Szlam F., Katori N., et al. The effects of argatroban on thrombin generation and hemostatic activation in vitro. Anesth Analg 99 5 (2004) 1283-1289
    • (2004) Anesth Analg , vol.99 , Issue.5 , pp. 1283-1289
    • Tanaka, K.A.1    Szlam, F.2    Katori, N.3
  • 17
    • 0025146426 scopus 로고
    • Clot-bound thrombin is protected from inhibition by heparin-antithrombin III but is susceptible to inactivation by antithrombin III-independent inhibitors
    • Weitz J.I., Hudoba M., Massel D., et al. Clot-bound thrombin is protected from inhibition by heparin-antithrombin III but is susceptible to inactivation by antithrombin III-independent inhibitors. J Clin Invest 86 2 (1990) 385-391
    • (1990) J Clin Invest , vol.86 , Issue.2 , pp. 385-391
    • Weitz, J.I.1    Hudoba, M.2    Massel, D.3
  • 18
    • 0027959329 scopus 로고
    • Effects of the synthetic thrombin inhibitor argatroban on fibrin- or clot-incorporated thrombin: comparison with heparin and recombinant hirudin
    • Berry C.N., Girardot C., Lecoffre C., et al. Effects of the synthetic thrombin inhibitor argatroban on fibrin- or clot-incorporated thrombin: comparison with heparin and recombinant hirudin. Thromb Haemost 72 3 (1994) 381-386
    • (1994) Thromb Haemost , vol.72 , Issue.3 , pp. 381-386
    • Berry, C.N.1    Girardot, C.2    Lecoffre, C.3
  • 19
    • 0018924505 scopus 로고
    • Effect of heparin and heparin fractions on platelet aggregation
    • Salzman E.W., Rosenberg R.D., Smith M.H., et al. Effect of heparin and heparin fractions on platelet aggregation. J Clin Invest 65 1 (1980) 64-73
    • (1980) J Clin Invest , vol.65 , Issue.1 , pp. 64-73
    • Salzman, E.W.1    Rosenberg, R.D.2    Smith, M.H.3
  • 20
    • 0022652413 scopus 로고
    • Effect of a new anticoagulant (MD 805) on platelet activation in the hemodialysis circuit
    • Matsuo T., Nakao K., Yamada T., et al. Effect of a new anticoagulant (MD 805) on platelet activation in the hemodialysis circuit. Thromb Res 41 1 (1986) 33-41
    • (1986) Thromb Res , vol.41 , Issue.1 , pp. 33-41
    • Matsuo, T.1    Nakao, K.2    Yamada, T.3
  • 21
    • 0345487533 scopus 로고    scopus 로고
    • Platelet activation with unfractionated heparin at therapeutic concentrations and comparisons with a low-molecular-weight heparin and with a direct thrombin inhibitor
    • Xiao Z., and Theroux P. Platelet activation with unfractionated heparin at therapeutic concentrations and comparisons with a low-molecular-weight heparin and with a direct thrombin inhibitor. Circulation 97 3 (1998) 251-256
    • (1998) Circulation , vol.97 , Issue.3 , pp. 251-256
    • Xiao, Z.1    Theroux, P.2
  • 22
    • 23044475017 scopus 로고    scopus 로고
    • Efficacy and safety of heparinase I versus protamine in patients undergoing coronary artery bypass grafting with and without cardiopulmonary bypass
    • Stafford-Smith M., Lefrak E.A., Qazi A.G., et al. Efficacy and safety of heparinase I versus protamine in patients undergoing coronary artery bypass grafting with and without cardiopulmonary bypass. Anesthesiology 103 2 (2005) 229-240
    • (2005) Anesthesiology , vol.103 , Issue.2 , pp. 229-240
    • Stafford-Smith, M.1    Lefrak, E.A.2    Qazi, A.G.3
  • 23
    • 0031596139 scopus 로고    scopus 로고
    • Transgenically produced human antithrombin: structural and functional comparison to human plasma-derived antithrombin
    • Edmunds T., Van Patten S.M., Pollock J., et al. Transgenically produced human antithrombin: structural and functional comparison to human plasma-derived antithrombin. Blood 91 12 (1998) 4561-4571
    • (1998) Blood , vol.91 , Issue.12 , pp. 4561-4571
    • Edmunds, T.1    Van Patten, S.M.2    Pollock, J.3
  • 24
    • 0036241285 scopus 로고    scopus 로고
    • Recombinant human transgenic antithrombin in cardiac surgery: a dose-finding study
    • Levy J.H., Despotis G.J., Szlam F., et al. Recombinant human transgenic antithrombin in cardiac surgery: a dose-finding study. Anesthesiology 96 5 (2002) 1095-1102
    • (2002) Anesthesiology , vol.96 , Issue.5 , pp. 1095-1102
    • Levy, J.H.1    Despotis, G.J.2    Szlam, F.3
  • 25
    • 21744444282 scopus 로고    scopus 로고
    • Recombinant human antithrombin III restores heparin responsiveness and decreases activation of coagulation in heparin-resistant patients during cardiopulmonary bypass
    • Avidan M.S., Levy J.H., van Aken H., et al. Recombinant human antithrombin III restores heparin responsiveness and decreases activation of coagulation in heparin-resistant patients during cardiopulmonary bypass. J Thorac Cardiovasc Surg 130 1 (2005) 107-113
    • (2005) J Thorac Cardiovasc Surg , vol.130 , Issue.1 , pp. 107-113
    • Avidan, M.S.1    Levy, J.H.2    van Aken, H.3
  • 26
    • 9644278069 scopus 로고    scopus 로고
    • The heparin binding properties of heparin cofactor II suggest an antithrombin-like activation mechanism
    • O'Keeffe D., Olson S.T., Gasiunas N., et al. The heparin binding properties of heparin cofactor II suggest an antithrombin-like activation mechanism. J Biol Chem 279 48 (2004) 50267-50273
    • (2004) J Biol Chem , vol.279 , Issue.48 , pp. 50267-50273
    • O'Keeffe, D.1    Olson, S.T.2    Gasiunas, N.3
  • 27
    • 0029009699 scopus 로고
    • Deletion mutagenesis of heparin cofactor II: defining the minimum size of a thrombin inhibiting serpin
    • Sheffield W.P., and Blajchman M.A. Deletion mutagenesis of heparin cofactor II: defining the minimum size of a thrombin inhibiting serpin. FEBS Lett 365 2-3 (1995) 189-192
    • (1995) FEBS Lett , vol.365 , Issue.2-3 , pp. 189-192
    • Sheffield, W.P.1    Blajchman, M.A.2
  • 28
    • 0141718479 scopus 로고    scopus 로고
    • Localization of heparin cofactor II in injured human skin: a potential role in wound healing
    • Hoffman M., Loh K.L., Bond V.K., et al. Localization of heparin cofactor II in injured human skin: a potential role in wound healing. Exp Mol Pathol 75 2 (2003) 109-118
    • (2003) Exp Mol Pathol , vol.75 , Issue.2 , pp. 109-118
    • Hoffman, M.1    Loh, K.L.2    Bond, V.K.3
  • 29
    • 0032080132 scopus 로고    scopus 로고
    • Proteoglycans in macrophages: characterization and possible role in the cellular uptake of lipoproteins
    • Halvorsen B., Aas U.K., Kulseth M.A., et al. Proteoglycans in macrophages: characterization and possible role in the cellular uptake of lipoproteins. Biochem J 331 3 (1998) 743-752
    • (1998) Biochem J , vol.331 , Issue.3 , pp. 743-752
    • Halvorsen, B.1    Aas, U.K.2    Kulseth, M.A.3
  • 30
    • 0034630104 scopus 로고    scopus 로고
    • Endogenously produced glycosaminoglycans affecting the release of lipoprotein lipase from macrophages and the interaction with lipoproteins
    • Zimmermann R., Sartipy P., Winkler R., et al. Endogenously produced glycosaminoglycans affecting the release of lipoprotein lipase from macrophages and the interaction with lipoproteins. Biochim Biophys Acta Mol Cell Biol Lipids 1484 2-3 (2000) 316-324
    • (2000) Biochim Biophys Acta Mol Cell Biol Lipids , vol.1484 , Issue.2-3 , pp. 316-324
    • Zimmermann, R.1    Sartipy, P.2    Winkler, R.3
  • 31
    • 0014555003 scopus 로고
    • Binding of thrombin to antithrombin III
    • Abildgaard U. Binding of thrombin to antithrombin III. Scand J Clin Lab Invest 24 1 (1969) 23-27
    • (1969) Scand J Clin Lab Invest , vol.24 , Issue.1 , pp. 23-27
    • Abildgaard, U.1
  • 32
    • 0017240008 scopus 로고
    • Inhibition of bovine factor IXa and factor Xabeta by antithrombin III
    • Kurachi K., Fujikawa K., Schmer G., et al. Inhibition of bovine factor IXa and factor Xabeta by antithrombin III. Biochemistry 15 2 (1976) 373-377
    • (1976) Biochemistry , vol.15 , Issue.2 , pp. 373-377
    • Kurachi, K.1    Fujikawa, K.2    Schmer, G.3
  • 33
    • 0017167631 scopus 로고
    • Inhibition of activated factor XII by antithrombin-heparin cofactor
    • Stead N., Kaplan A.P., and Rosenberg R.D. Inhibition of activated factor XII by antithrombin-heparin cofactor. J Biol Chem 251 21 (1976) 6481-6488
    • (1976) J Biol Chem , vol.251 , Issue.21 , pp. 6481-6488
    • Stead, N.1    Kaplan, A.P.2    Rosenberg, R.D.3
  • 34
    • 0023218920 scopus 로고
    • Regulation of factor VIIa activity in plasma: evidence that antithrombin III is the sole plasma protease inhibitor of human factor VIIa
    • Kondo S., and Kisiel W. Regulation of factor VIIa activity in plasma: evidence that antithrombin III is the sole plasma protease inhibitor of human factor VIIa. Thromb Res 46 2 (1987) 325-335
    • (1987) Thromb Res , vol.46 , Issue.2 , pp. 325-335
    • Kondo, S.1    Kisiel, W.2
  • 35
    • 0021989130 scopus 로고
    • The protease specificity of heparin cofactor II. Inhibition of thrombin generated during coagulation
    • Parker K.A., and Tollefsen D.M. The protease specificity of heparin cofactor II. Inhibition of thrombin generated during coagulation. J Biol Chem 260 6 (1985) 3501-3505
    • (1985) J Biol Chem , vol.260 , Issue.6 , pp. 3501-3505
    • Parker, K.A.1    Tollefsen, D.M.2
  • 36
    • 0012302073 scopus 로고
    • Inhibition of chymotrypsin by heparin cofactor II
    • Church F.C., Noyes C.M., and Griffith M.J. Inhibition of chymotrypsin by heparin cofactor II. Proc Natl Acad Sci U S A 82 19 (1985) 6431-6434
    • (1985) Proc Natl Acad Sci U S A , vol.82 , Issue.19 , pp. 6431-6434
    • Church, F.C.1    Noyes, C.M.2    Griffith, M.J.3
  • 37
    • 0035896608 scopus 로고    scopus 로고
    • Identification of the protein C/activated protein C binding sites on the endothelial cell protein C receptor. Implications for a novel mode of ligand recognition by a major histocompatibility complex class 1-type receptor
    • Liaw P.C., Mather T., Oganesyan N., et al. Identification of the protein C/activated protein C binding sites on the endothelial cell protein C receptor. Implications for a novel mode of ligand recognition by a major histocompatibility complex class 1-type receptor. J Biol Chem 276 11 (2001) 8364-8370
    • (2001) J Biol Chem , vol.276 , Issue.11 , pp. 8364-8370
    • Liaw, P.C.1    Mather, T.2    Oganesyan, N.3
  • 38
    • 10244232835 scopus 로고    scopus 로고
    • Antithrombotic activity of dermatan sulfate in heparin cofactor II-deficient mice
    • Vicente C.P., He L., Pavao M.S., et al. Antithrombotic activity of dermatan sulfate in heparin cofactor II-deficient mice. Blood 104 13 (2004) 3965-3970
    • (2004) Blood , vol.104 , Issue.13 , pp. 3965-3970
    • Vicente, C.P.1    He, L.2    Pavao, M.S.3
  • 39
    • 0023543224 scopus 로고
    • Hereditary heparin cofactor II deficiency and the risk of development of thrombosis
    • Bertina R.M., van der Linden I.K., Engesser L., et al. Hereditary heparin cofactor II deficiency and the risk of development of thrombosis. Thromb Haemost 57 2 (1987) 196-200
    • (1987) Thromb Haemost , vol.57 , Issue.2 , pp. 196-200
    • Bertina, R.M.1    van der Linden, I.K.2    Engesser, L.3
  • 40
    • 0030062348 scopus 로고    scopus 로고
    • Molecular and cellular basis for type I heparin cofactor II deficiency (heparin cofactor II Awaji)
    • Kondo S., Tokunaga F., Kario K., et al. Molecular and cellular basis for type I heparin cofactor II deficiency (heparin cofactor II Awaji). Blood 87 3 (1996) 1006-1012
    • (1996) Blood , vol.87 , Issue.3 , pp. 1006-1012
    • Kondo, S.1    Tokunaga, F.2    Kario, K.3
  • 41
    • 0036155992 scopus 로고    scopus 로고
    • Heparin cofactor II inhibits arterial thrombosis after endothelial injury
    • He L., Vicente C.P., Westrick R.J., et al. Heparin cofactor II inhibits arterial thrombosis after endothelial injury. J Clin Invest 109 2 (2002) 213-219
    • (2002) J Clin Invest , vol.109 , Issue.2 , pp. 213-219
    • He, L.1    Vicente, C.P.2    Westrick, R.J.3
  • 42
    • 0842264178 scopus 로고    scopus 로고
    • High plasma heparin cofactor II activity is associated with reduced incidence of in-stent restenosis after percutaneous coronary intervention
    • Takamori N., Azuma H., Kato M., et al. High plasma heparin cofactor II activity is associated with reduced incidence of in-stent restenosis after percutaneous coronary intervention. Circulation 109 4 (2004) 481-486
    • (2004) Circulation , vol.109 , Issue.4 , pp. 481-486
    • Takamori, N.1    Azuma, H.2    Kato, M.3
  • 43
    • 27144514073 scopus 로고    scopus 로고
    • Effects of antithrombin and heparin cofactor II levels on anticoagulation with Intimatan
    • Tanaka K.A., Szlam F., Vinten-Johansen J., et al. Effects of antithrombin and heparin cofactor II levels on anticoagulation with Intimatan. Thromb Haemost 94 4 (2005) 808-813
    • (2005) Thromb Haemost , vol.94 , Issue.4 , pp. 808-813
    • Tanaka, K.A.1    Szlam, F.2    Vinten-Johansen, J.3
  • 44
    • 0034666733 scopus 로고    scopus 로고
    • Anticoagulant and antithrombin effects of Intimatan, a heparin cofactor II agonist
    • Buchanan M.R., and Brister S.J. Anticoagulant and antithrombin effects of Intimatan, a heparin cofactor II agonist. Thromb Res 99 6 (2000) 603-612
    • (2000) Thromb Res , vol.99 , Issue.6 , pp. 603-612
    • Buchanan, M.R.1    Brister, S.J.2
  • 45
    • 0026682821 scopus 로고
    • Elevated levels of thrombin-heparin cofactor II complex in plasma from patients with disseminated intravascular coagulation
    • Andersson T.R., Sie P., Pelzer H., et al. Elevated levels of thrombin-heparin cofactor II complex in plasma from patients with disseminated intravascular coagulation. Thromb Res 66 5 (1992) 591-598
    • (1992) Thromb Res , vol.66 , Issue.5 , pp. 591-598
    • Andersson, T.R.1    Sie, P.2    Pelzer, H.3
  • 46
    • 0032904662 scopus 로고    scopus 로고
    • Dermatan sulphate in patients with heparin-induced thrombocytopenia
    • Taliani M.R., Agnelli G., Nenci G.G., et al. Dermatan sulphate in patients with heparin-induced thrombocytopenia. Br J Haematol 104 1 (1999) 87-89
    • (1999) Br J Haematol , vol.104 , Issue.1 , pp. 87-89
    • Taliani, M.R.1    Agnelli, G.2    Nenci, G.G.3
  • 47
    • 0036719075 scopus 로고    scopus 로고
    • The lectin-like domain of thrombomodulin confers protection from neutrophil-mediated tissue damage by suppressing adhesion molecule expression via nuclear factor kappaB and mitogen-activated protein kinase pathways
    • Conway E.M., Van de Wouwer M., Pollefeyt S., et al. The lectin-like domain of thrombomodulin confers protection from neutrophil-mediated tissue damage by suppressing adhesion molecule expression via nuclear factor kappaB and mitogen-activated protein kinase pathways. J Exp Med 196 5 (2002) 565-577
    • (2002) J Exp Med , vol.196 , Issue.5 , pp. 565-577
    • Conway, E.M.1    Van de Wouwer, M.2    Pollefeyt, S.3
  • 49
    • 0028876697 scopus 로고
    • Absence of the blood-clotting regulator thrombomodulin causes embryonic lethality in mice before development of a functional cardiovascular system
    • Healy A.M., Rayburn H.B., Rosenberg R.D., et al. Absence of the blood-clotting regulator thrombomodulin causes embryonic lethality in mice before development of a functional cardiovascular system. Proc Natl Acad Sci U S A 92 3 (1995) 850-854
    • (1995) Proc Natl Acad Sci U S A , vol.92 , Issue.3 , pp. 850-854
    • Healy, A.M.1    Rayburn, H.B.2    Rosenberg, R.D.3
  • 50
    • 0034892611 scopus 로고    scopus 로고
    • Endothelium-specific loss of murine thrombomodulin disrupts the protein C anticoagulant pathway and causes juvenile-onset thrombosis
    • Isermann B., Hendrickson S.B., Zogg M., et al. Endothelium-specific loss of murine thrombomodulin disrupts the protein C anticoagulant pathway and causes juvenile-onset thrombosis. J Clin Invest 108 4 (2001) 537-546
    • (2001) J Clin Invest , vol.108 , Issue.4 , pp. 537-546
    • Isermann, B.1    Hendrickson, S.B.2    Zogg, M.3
  • 51
    • 0141609935 scopus 로고    scopus 로고
    • Inflammation and thrombosis
    • Esmon C.T. Inflammation and thrombosis. J Thromb Haemost 1 7 (2003) 1343-1348
    • (2003) J Thromb Haemost , vol.1 , Issue.7 , pp. 1343-1348
    • Esmon, C.T.1
  • 52
    • 0034996440 scopus 로고    scopus 로고
    • Carboxypeptidase R is an inactivator of complement-derived inflammatory peptides and an inhibitor of fibrinolysis
    • Campbell W., Okada N., and Okada H. Carboxypeptidase R is an inactivator of complement-derived inflammatory peptides and an inhibitor of fibrinolysis. Immunol Rev 180 (2001) 162-167
    • (2001) Immunol Rev , vol.180 , pp. 162-167
    • Campbell, W.1    Okada, N.2    Okada, H.3
  • 53
    • 0037036069 scopus 로고    scopus 로고
    • Activation of endothelial cell protease activated receptor 1 by the protein C pathway
    • Riewald M., Petrovan R.J., Donner A., et al. Activation of endothelial cell protease activated receptor 1 by the protein C pathway. Science 296 5574 (2002) 1880-1882
    • (2002) Science , vol.296 , Issue.5574 , pp. 1880-1882
    • Riewald, M.1    Petrovan, R.J.2    Donner, A.3
  • 54
    • 4444331574 scopus 로고    scopus 로고
    • Activated protein C variants with normal cytoprotective but reduced anticoagulant activity
    • Mosnier L.O., Gale A.J., Yegneswaran S., et al. Activated protein C variants with normal cytoprotective but reduced anticoagulant activity. Blood 104 6 (2004) 1740-1744
    • (2004) Blood , vol.104 , Issue.6 , pp. 1740-1744
    • Mosnier, L.O.1    Gale, A.J.2    Yegneswaran, S.3
  • 55
    • 1342269932 scopus 로고    scopus 로고
    • Activated protein C prevents neuronal apoptosis via protease activated receptors 1 and 3
    • Guo H., Liu D., Gelbard H., et al. Activated protein C prevents neuronal apoptosis via protease activated receptors 1 and 3. Neuron 41 4 (2004) 563-572
    • (2004) Neuron , vol.41 , Issue.4 , pp. 563-572
    • Guo, H.1    Liu, D.2    Gelbard, H.3
  • 56
    • 16844383361 scopus 로고    scopus 로고
    • PAR1 cleavage and signaling in response to activated protein C and thrombin
    • Ludeman M.J., Kataoka H., Srinivasan Y., et al. PAR1 cleavage and signaling in response to activated protein C and thrombin. J Biol Chem 280 13 (2005) 13122-13128
    • (2005) J Biol Chem , vol.280 , Issue.13 , pp. 13122-13128
    • Ludeman, M.J.1    Kataoka, H.2    Srinivasan, Y.3
  • 57
    • 21244502159 scopus 로고    scopus 로고
    • Protease-activated receptor-1 signaling by activated protein C in cytokine-perturbed endothelial cells is distinct from thrombin signaling
    • Riewald M., and Ruf W. Protease-activated receptor-1 signaling by activated protein C in cytokine-perturbed endothelial cells is distinct from thrombin signaling. J Biol Chem 280 20 (2005) 19808-19814
    • (2005) J Biol Chem , vol.280 , Issue.20 , pp. 19808-19814
    • Riewald, M.1    Ruf, W.2
  • 58
    • 0141819138 scopus 로고    scopus 로고
    • The protein C pathway
    • Esmon C.T. The protein C pathway. Chest 124 3 Suppl (2003) 26S-32S
    • (2003) Chest , vol.124 , Issue.3 SUPPL
    • Esmon, C.T.1
  • 59
    • 0033594760 scopus 로고    scopus 로고
    • Soluble thrombomodulin as a predictor of incident coronary heart disease and symptomless carotid artery atherosclerosis in the Atherosclerosis Risk in Communities (ARIC) Study: a case-cohort study
    • Salomaa V., Matei C., Aleksic N., et al. Soluble thrombomodulin as a predictor of incident coronary heart disease and symptomless carotid artery atherosclerosis in the Atherosclerosis Risk in Communities (ARIC) Study: a case-cohort study. Lancet 353 9166 (1999) 1729-1734
    • (1999) Lancet , vol.353 , Issue.9166 , pp. 1729-1734
    • Salomaa, V.1    Matei, C.2    Aleksic, N.3
  • 60
    • 0028300383 scopus 로고
    • Influence of aprotinin on the thrombomodulin/protein C system in pediatric cardiac operations
    • Boldt J., Zickmann B., Schindler E., et al. Influence of aprotinin on the thrombomodulin/protein C system in pediatric cardiac operations. J Thorac Cardiovasc Surg 107 5 (1994) 1215-1221
    • (1994) J Thorac Cardiovasc Surg , vol.107 , Issue.5 , pp. 1215-1221
    • Boldt, J.1    Zickmann, B.2    Schindler, E.3
  • 61
    • 10244250329 scopus 로고    scopus 로고
    • Patients with severe sepsis vary markedly in their ability to generate activated protein C
    • Liaw P.C.Y., Esmon C.T., Kahnamoui K., et al. Patients with severe sepsis vary markedly in their ability to generate activated protein C. Blood 104 13 (2004) 3958-3964
    • (2004) Blood , vol.104 , Issue.13 , pp. 3958-3964
    • Liaw, P.C.Y.1    Esmon, C.T.2    Kahnamoui, K.3
  • 62
    • 0035826096 scopus 로고    scopus 로고
    • Efficacy and safety of recombinant human activated protein C for severe sepsis
    • Bernard G.R., Vincent J.L., Laterre P.F., et al. Efficacy and safety of recombinant human activated protein C for severe sepsis. N Engl J Med 344 10 (2001) 699-709
    • (2001) N Engl J Med , vol.344 , Issue.10 , pp. 699-709
    • Bernard, G.R.1    Vincent, J.L.2    Laterre, P.F.3
  • 63
    • 12444249948 scopus 로고    scopus 로고
    • Drotrecogin alfa (activated) (recombinant human activated protein C) reduces host coagulopathy response in patients with severe sepsis
    • Dhainaut J.F., Yan S.B., Margolis B.D., et al. Drotrecogin alfa (activated) (recombinant human activated protein C) reduces host coagulopathy response in patients with severe sepsis. Thromb Haemost 90 4 (2003) 642-653
    • (2003) Thromb Haemost , vol.90 , Issue.4 , pp. 642-653
    • Dhainaut, J.F.1    Yan, S.B.2    Margolis, B.D.3
  • 64
    • 17944378441 scopus 로고    scopus 로고
    • Decreased plasma activity of antithrombin or protein C is not due to consumption coagulopathy in septic patients with disseminated intravascular coagulation
    • Asakura H., Ontachi Y., Mizutani T., et al. Decreased plasma activity of antithrombin or protein C is not due to consumption coagulopathy in septic patients with disseminated intravascular coagulation. Eur J Haematol 67 3 (2001) 170-175
    • (2001) Eur J Haematol , vol.67 , Issue.3 , pp. 170-175
    • Asakura, H.1    Ontachi, Y.2    Mizutani, T.3
  • 65
    • 12544255807 scopus 로고    scopus 로고
    • Thrombomodulin accelerates activated protein C production and inhibits thrombin generation in the plasma of disseminated intravascular coagulation patients
    • Wada H., Sakakura M., Kushiya F., et al. Thrombomodulin accelerates activated protein C production and inhibits thrombin generation in the plasma of disseminated intravascular coagulation patients. Blood Coagul Fibrinolysis 16 1 (2005) 17-24
    • (2005) Blood Coagul Fibrinolysis , vol.16 , Issue.1 , pp. 17-24
    • Wada, H.1    Sakakura, M.2    Kushiya, F.3
  • 66
    • 0032696866 scopus 로고    scopus 로고
    • Recombinant thrombomodulin and activated protein C in the treatment of disseminated intravascular coagulation
    • Maruyama I. Recombinant thrombomodulin and activated protein C in the treatment of disseminated intravascular coagulation. Thromb Haemost 82 2 (1999) 718-721
    • (1999) Thromb Haemost , vol.82 , Issue.2 , pp. 718-721
    • Maruyama, I.1
  • 67
    • 19944432294 scopus 로고    scopus 로고
    • Phase I study of a novel recombinant human soluble thrombomodulin, ART-123
    • Moll S., Lindley C., Pescatore S., et al. Phase I study of a novel recombinant human soluble thrombomodulin, ART-123. J Thromb Haemost 2 10 (2004) 1745-1751
    • (2004) J Thromb Haemost , vol.2 , Issue.10 , pp. 1745-1751
    • Moll, S.1    Lindley, C.2    Pescatore, S.3
  • 68
    • 23844438376 scopus 로고    scopus 로고
    • Dose-response study of recombinant human soluble thrombomodulin (ART-123) in the prevention of venous thromboembolism after total hip replacement
    • Kearon C., Comp P., Douketis J., et al. Dose-response study of recombinant human soluble thrombomodulin (ART-123) in the prevention of venous thromboembolism after total hip replacement. J Thromb Haemost 3 5 (2005) 962-968
    • (2005) J Thromb Haemost , vol.3 , Issue.5 , pp. 962-968
    • Kearon, C.1    Comp, P.2    Douketis, J.3
  • 69
    • 33644828014 scopus 로고    scopus 로고
    • Soluble thrombomodulin is antithrombotic in the presence of neutralising antibodies to protein C and reduces circulating activated protein C levels in primates
    • Tanaka K.A., Fernandez J.A., Marzec U.M., et al. Soluble thrombomodulin is antithrombotic in the presence of neutralising antibodies to protein C and reduces circulating activated protein C levels in primates. Br J Haematol 132 (2006) 197-203
    • (2006) Br J Haematol , vol.132 , pp. 197-203
    • Tanaka, K.A.1    Fernandez, J.A.2    Marzec, U.M.3
  • 70
    • 0027320820 scopus 로고
    • Recombinant human soluble thrombomodulin delivers bounded thrombin to antithrombin III: thrombomodulin associates with free thrombin and is recycled to activate protein C
    • Aritomi M., Watanabe N., Ohishi R., et al. Recombinant human soluble thrombomodulin delivers bounded thrombin to antithrombin III: thrombomodulin associates with free thrombin and is recycled to activate protein C. Thromb Haemost 70 3 (1993) 418-422
    • (1993) Thromb Haemost , vol.70 , Issue.3 , pp. 418-422
    • Aritomi, M.1    Watanabe, N.2    Ohishi, R.3
  • 71
    • 0035904368 scopus 로고    scopus 로고
    • Caring for the critically ill patient. High-dose antithrombin III in severe sepsis: a randomized controlled trial
    • Warren B.L., Eid A., Singer P., et al. Caring for the critically ill patient. High-dose antithrombin III in severe sepsis: a randomized controlled trial. JAMA 286 15 (2001) 1869-1878
    • (2001) JAMA , vol.286 , Issue.15 , pp. 1869-1878
    • Warren, B.L.1    Eid, A.2    Singer, P.3
  • 72
    • 0019891328 scopus 로고
    • Potent inhibition of thrombin by the newly synthesized arginine derivative No. 805. The importance of stereo-structure of its hydrophobic carboxamide portion
    • Okamoto S., Hijikata A., Kikumoto R., et al. Potent inhibition of thrombin by the newly synthesized arginine derivative No. 805. The importance of stereo-structure of its hydrophobic carboxamide portion. Biochem Biophys Res Commun 101 2 (1981) 440-446
    • (1981) Biochem Biophys Res Commun , vol.101 , Issue.2 , pp. 440-446
    • Okamoto, S.1    Hijikata, A.2    Kikumoto, R.3
  • 73
    • 33846530242 scopus 로고    scopus 로고
    • Okamoto S. Strategies for creating new medicines. Kobe Research Project on Thrombosis and Hemostasis; 2003.
  • 74
    • 0021327417 scopus 로고
    • 2-[(3-methyl-1,2,3,4-tetrahydro-8-quinolinyl )sulfonyl]-L-arginyl)]-2-piperidinecarboxylic acid
    • 2-[(3-methyl-1,2,3,4-tetrahydro-8-quinolinyl )sulfonyl]-L-arginyl)]-2-piperidinecarboxylic acid. Biochemistry 23 1 (1984) 85-90
    • (1984) Biochemistry , vol.23 , Issue.1 , pp. 85-90
    • Kikumoto, R.1    Tamao, Y.2    Tezuka, T.3
  • 75
    • 0025161898 scopus 로고
    • The effect of substituting phosphotyrosine for sulphotyrosine on the activity of hirudin
    • Hofsteenge J., Stone S.R., Donella-Deana A., et al. The effect of substituting phosphotyrosine for sulphotyrosine on the activity of hirudin. Eur J Biochem 188 1 (1990) 55-59
    • (1990) Eur J Biochem , vol.188 , Issue.1 , pp. 55-59
    • Hofsteenge, J.1    Stone, S.R.2    Donella-Deana, A.3
  • 76
    • 12644267274 scopus 로고    scopus 로고
    • Effect of renal impairment on the pharmacokinetics and pharmacodynamics of desirudin
    • Lefevre G., Duval M., Gauron S., et al. Effect of renal impairment on the pharmacokinetics and pharmacodynamics of desirudin. Clin Pharmacol Ther 62 1 (1997) 50-59
    • (1997) Clin Pharmacol Ther , vol.62 , Issue.1 , pp. 50-59
    • Lefevre, G.1    Duval, M.2    Gauron, S.3
  • 77
    • 0028587155 scopus 로고
    • Kinetic mechanism for the interaction of hirulog with thrombin
    • Parry M.A., Maraganore J.M., and Stone S.R. Kinetic mechanism for the interaction of hirulog with thrombin. Biochemistry 33 49 (1994) 14807-14814
    • (1994) Biochemistry , vol.33 , Issue.49 , pp. 14807-14814
    • Parry, M.A.1    Maraganore, J.M.2    Stone, S.R.3
  • 78
    • 0026780909 scopus 로고
    • Antithrombotic effects of synthetic peptides targeting various functional domains of thrombin
    • Kelly A.B., Maraganore J.M., Bourdon P., et al. Antithrombotic effects of synthetic peptides targeting various functional domains of thrombin. Proc Natl Acad Sci U S A 89 13 (1992) 6040-6044
    • (1992) Proc Natl Acad Sci U S A , vol.89 , Issue.13 , pp. 6040-6044
    • Kelly, A.B.1    Maraganore, J.M.2    Bourdon, P.3
  • 79
    • 0026598494 scopus 로고
    • Thrombin-specific inhibition by and slow cleavage of hirulog-1
    • Witting J.I., Bourdon P., Brezniak D.V., et al. Thrombin-specific inhibition by and slow cleavage of hirulog-1. Biochem J 283 Pt 3 (1992) 737-743
    • (1992) Biochem J , vol.283 , Issue.PART 3 , pp. 737-743
    • Witting, J.I.1    Bourdon, P.2    Brezniak, D.V.3
  • 80
    • 27844481103 scopus 로고    scopus 로고
    • Differences in the clinically effective molar concentrations of four direct thrombin inhibitors explain their variable prothrombin time prolongation
    • Warkentin T.E., Greinacher A., Craven S., et al. Differences in the clinically effective molar concentrations of four direct thrombin inhibitors explain their variable prothrombin time prolongation. Thromb Haemost 94 (2005) 958-964
    • (2005) Thromb Haemost , vol.94 , pp. 958-964
    • Warkentin, T.E.1    Greinacher, A.2    Craven, S.3
  • 81
    • 0028792216 scopus 로고
    • Triabin, a highly potent exosite inhibitor of thrombin
    • Noeske-Jungblut C., Haendler B., Donner P., et al. Triabin, a highly potent exosite inhibitor of thrombin. J Biol Chem 270 48 (1995) 28629-28634
    • (1995) J Biol Chem , vol.270 , Issue.48 , pp. 28629-28634
    • Noeske-Jungblut, C.1    Haendler, B.2    Donner, P.3
  • 82
    • 0027435111 scopus 로고
    • Antithrombotic effects of thrombin-induced activation of endogenous protein C in primates
    • Hanson S.R., Griffin J.H., Harker L.A., et al. Antithrombotic effects of thrombin-induced activation of endogenous protein C in primates. J Clin Invest 92 4 (1993) 2003-2012
    • (1993) J Clin Invest , vol.92 , Issue.4 , pp. 2003-2012
    • Hanson, S.R.1    Griffin, J.H.2    Harker, L.A.3
  • 83
    • 0034704118 scopus 로고    scopus 로고
    • Rational design of a potent anticoagulant thrombin
    • Cantwell A.M., and Di Cera E. Rational design of a potent anticoagulant thrombin. J Biol Chem 275 51 (2000) 39827-39830
    • (2000) J Biol Chem , vol.275 , Issue.51 , pp. 39827-39830
    • Cantwell, A.M.1    Di Cera, E.2
  • 84
    • 4544312894 scopus 로고    scopus 로고
    • The anticoagulant thrombin mutant W215A/E217A has a collapsed primary specificity pocket
    • Pineda A.O., Chen Z.W., Caccia S., et al. The anticoagulant thrombin mutant W215A/E217A has a collapsed primary specificity pocket. J Biol Chem 279 38 (2004) 39824-39828
    • (2004) J Biol Chem , vol.279 , Issue.38 , pp. 39824-39828
    • Pineda, A.O.1    Chen, Z.W.2    Caccia, S.3
  • 85
    • 0037008668 scopus 로고    scopus 로고
    • The thrombin mutant W215A/E217A shows safe and potent anticoagulant and antithrombotic effects in vivo
    • Gruber A., Cantwell A.M., Di Cera E., et al. The thrombin mutant W215A/E217A shows safe and potent anticoagulant and antithrombotic effects in vivo. J Biol Chem 277 31 (2002) 27581-27584
    • (2002) J Biol Chem , vol.277 , Issue.31 , pp. 27581-27584
    • Gruber, A.1    Cantwell, A.M.2    Di Cera, E.3
  • 86
    • 0036795261 scopus 로고    scopus 로고
    • Pharmacokinetic-pharmacodynamic analysis of drotrecogin alfa (activated) in patients with severe sepsis
    • Macias W.L., Dhainaut J.F., Yan S.C., et al. Pharmacokinetic-pharmacodynamic analysis of drotrecogin alfa (activated) in patients with severe sepsis. Clin Pharmacol Ther 72 4 (2002) 391-402
    • (2002) Clin Pharmacol Ther , vol.72 , Issue.4 , pp. 391-402
    • Macias, W.L.1    Dhainaut, J.F.2    Yan, S.C.3
  • 87
    • 3142628024 scopus 로고    scopus 로고
    • A recombinant murine meizothrombin precursor, prothrombin R157A/R268A, inhibits thrombosis in a model of acute carotid artery injury
    • Shim K., Zhu H., Westfield L.A., et al. A recombinant murine meizothrombin precursor, prothrombin R157A/R268A, inhibits thrombosis in a model of acute carotid artery injury. Blood 104 2 (2004) 415-419
    • (2004) Blood , vol.104 , Issue.2 , pp. 415-419
    • Shim, K.1    Zhu, H.2    Westfield, L.A.3
  • 88
    • 0035281601 scopus 로고    scopus 로고
    • Preparation of anhydrothrombin and characterization of its interaction with natural thrombin substrates
    • Hosokawa K., Ohnishi T., Shima M., et al. Preparation of anhydrothrombin and characterization of its interaction with natural thrombin substrates. Biochem J 354 Pt 2 (2001) 309-313
    • (2001) Biochem J , vol.354 , Issue.PART 2 , pp. 309-313
    • Hosokawa, K.1    Ohnishi, T.2    Shima, M.3
  • 89
    • 2942627502 scopus 로고    scopus 로고
    • A critical role for thrombin in platelet aggregation under high shear stress
    • Sakurai Y., Shima M., Giddings J., et al. A critical role for thrombin in platelet aggregation under high shear stress. Thromb Res 113 5 (2004) 311-318
    • (2004) Thromb Res , vol.113 , Issue.5 , pp. 311-318
    • Sakurai, Y.1    Shima, M.2    Giddings, J.3
  • 90
    • 0036470428 scopus 로고    scopus 로고
    • Evolution of enzyme cascades from embryonic development to blood coagulation
    • Krem M.M., and Cera E.D. Evolution of enzyme cascades from embryonic development to blood coagulation. Trends Biochem Sci 27 2 (2002) 67-74
    • (2002) Trends Biochem Sci , vol.27 , Issue.2 , pp. 67-74
    • Krem, M.M.1    Cera, E.D.2
  • 91
    • 0037253347 scopus 로고    scopus 로고
    • Participation in inflammation
    • Coughlin S.R., and Camerer E. Participation in inflammation. J Clin Invest 111 1 (2003) 25-27
    • (2003) J Clin Invest , vol.111 , Issue.1 , pp. 25-27
    • Coughlin, S.R.1    Camerer, E.2
  • 92
    • 0242401773 scopus 로고    scopus 로고
    • Calibrated automated thrombin generation measurement in clotting plasma
    • Hemker H.C., Giesen P., Al Dieri R., et al. Calibrated automated thrombin generation measurement in clotting plasma. Pathophysiol Haemost Thromb 33 1 (2003) 4-15
    • (2003) Pathophysiol Haemost Thromb , vol.33 , Issue.1 , pp. 4-15
    • Hemker, H.C.1    Giesen, P.2    Al Dieri, R.3
  • 93
    • 17944396396 scopus 로고    scopus 로고
    • Recombinant murine-activated protein C is neuroprotective in a murine ischemic stroke model
    • Fernandez J.A., Xu X., Liu D., et al. Recombinant murine-activated protein C is neuroprotective in a murine ischemic stroke model. Blood Cells Mol Dis 30 3 (2003) 271-276
    • (2003) Blood Cells Mol Dis , vol.30 , Issue.3 , pp. 271-276
    • Fernandez, J.A.1    Xu, X.2    Liu, D.3
  • 94
    • 0042563262 scopus 로고    scopus 로고
    • Prevention of thrombosis following deep arterial injury in rats by bovine activated protein C requiring co-administration of bovine protein S
    • Malm K., Dahlback B., and Arnljots B. Prevention of thrombosis following deep arterial injury in rats by bovine activated protein C requiring co-administration of bovine protein S. Thromb Haemost 90 2 (2003) 227-234
    • (2003) Thromb Haemost , vol.90 , Issue.2 , pp. 227-234
    • Malm, K.1    Dahlback, B.2    Arnljots, B.3


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