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Volumn 126, Issue 1, 2015, Pages 94-102

Hemostatic agents of broad applicability produced by selective tuning of factor Xa zymogenicity

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 10A; HEMOSTATIC AGENT; PROTHROMBIN; UNCLASSIFIED DRUG; ZYMOGEN LIKE FACTOR XA; ENZYME PRECURSOR; MUTANT PROTEIN; THROMBOPLASTIN;

EID: 84937780393     PISSN: 00064971     EISSN: 15280020     Source Type: Journal    
DOI: 10.1182/blood-2015-03-634329     Document Type: Article
Times cited : (19)

References (35)
  • 1
    • 84859596442 scopus 로고    scopus 로고
    • Modern haemophilia care
    • Berntorp E, Shapiro AD. Modern haemophilia care. Lancet. 2012;379(9824):1447-1456.
    • (2012) Lancet , vol.379 , Issue.9824 , pp. 1447-1456
    • Berntorp, E.1    Shapiro, A.D.2
  • 3
    • 84892526766 scopus 로고    scopus 로고
    • Molecular approaches for improved clotting factors for hemophilia
    • Kaufman RJ, Powell JS. Molecular approaches for improved clotting factors for hemophilia. Blood. 2013;122(22):3568-3574.
    • (2013) Blood , vol.122 , Issue.22 , pp. 3568-3574
    • Kaufman, R.J.1    Powell, J.S.2
  • 4
    • 79958144891 scopus 로고    scopus 로고
    • Recent advances in the development of coagulation factors and procoagulants for the treatment of hemophilia
    • Schaub RG. Recent advances in the development of coagulation factors and procoagulants for the treatment of hemophilia. Biochem Pharmacol. 2011;82(2):91-98.
    • (2011) Biochem Pharmacol , vol.82 , Issue.2 , pp. 91-98
    • Schaub, R.G.1
  • 5
    • 49649122047 scopus 로고    scopus 로고
    • The conformational switch from the factor X zymogen to protease state mediates exosite expression and prothrombinase assembly
    • Toso R, Zhu H, Camire RM. The conformational switch from the factor X zymogen to protease state mediates exosite expression and prothrombinase assembly. J Biol Chem. 2008; 283(27):18627-18635.
    • (2008) J Biol Chem , vol.283 , Issue.27 , pp. 18627-18635
    • Toso, R.1    Zhu, H.2    Camire, R.M.3
  • 6
    • 78650988916 scopus 로고    scopus 로고
    • Zymogen-like factor Xa variants restore thrombin generation and effectively bypass the intrinsic pathway in vitro
    • Bunce MW, Toso R, Camire RM. Zymogen-like factor Xa variants restore thrombin generation and effectively bypass the intrinsic pathway in vitro. Blood. 2011;117(1):290-298.
    • (2011) Blood , vol.117 , Issue.1 , pp. 290-298
    • Bunce, M.W.1    Toso, R.2    Camire, R.M.3
  • 7
    • 80755125572 scopus 로고    scopus 로고
    • A zymogenlike factor Xa variant corrects the coagulation defect in hemophilia
    • Ivanciu L, Toso R, Margaritis P, et al. A zymogenlike factor Xa variant corrects the coagulation defect in hemophilia. Nat Biotechnol. 2011;29(11): 1028-1033.
    • (2011) Nat Biotechnol , vol.29 , Issue.11 , pp. 1028-1033
    • Ivanciu, L.1    Toso, R.2    Margaritis, P.3
  • 8
    • 33947092515 scopus 로고
    • Structural basis of the activation and action of trypsin
    • Huber R, Bode W. Structural basis of the activation and action of trypsin. Acc Chem Res. 1978;11(3):114-122.
    • (1978) Acc Chem Res , vol.11 , Issue.3 , pp. 114-122
    • Huber, R.1    Bode, W.2
  • 9
    • 0031956497 scopus 로고    scopus 로고
    • Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes
    • Khan AR, James MN. Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes. Protein Sci. 1998;7(4):815-836.
    • (1998) Protein Sci , vol.7 , Issue.4 , pp. 815-836
    • Khan, A.R.1    James, M.N.2
  • 10
    • 0024431034 scopus 로고
    • The refined 1.9 A crystal structure of human a-thrombin: Interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment
    • Bode W, Mayr I, Baumann U, Huber R, Stone SR, Hofsteenge J. The refined 1.9 A crystal structure of human a-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment. EMBO J. 1989;8(11):3467-3475.
    • (1989) EMBO J , vol.8 , Issue.11 , pp. 3467-3475
    • Bode, W.1    Mayr, I.2    Baumann, U.3    Huber, R.4    Stone, S.R.5    Hofsteenge, J.6
  • 11
    • 0017893796 scopus 로고
    • The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 A resolution
    • Bode W, Schwager P, Huber R. The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. The refined crystal structures of the bovine trypsinogen-pancreatic trypsin inhibitor complex and of its ternary complex with Ile-Val at 1.9 A resolution. J Mol Biol. 1978;118(1):99-112.
    • (1978) J Mol Biol , vol.118 , Issue.1 , pp. 99-112
    • Bode, W.1    Schwager, P.2    Huber, R.3
  • 12
    • 0018781771 scopus 로고
    • The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. II. The binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and to p-guanidinobenzoate-trypsinogen
    • Bode W. The transition of bovine trypsinogen to a trypsin-like state upon strong ligand binding. II. The binding of the pancreatic trypsin inhibitor and of isoleucine-valine and of sequentially related peptides to trypsinogen and to p-guanidinobenzoate-trypsinogen. J Mol Biol. 1979;127(4):357-374.
    • (1979) J Mol Biol , vol.127 , Issue.4 , pp. 357-374
    • Bode, W.1
  • 13
    • 0021103421 scopus 로고
    • Solution composition dependent variation in extinction coefficients for p-nitroaniline
    • Lottenberg R, Jackson CM. Solution composition dependent variation in extinction coefficients for p-nitroaniline. Biochim Biophys Acta. 1983; 742(3):558-564.
    • (1983) Biochim Biophys Acta , vol.742 , Issue.3 , pp. 558-564
    • Lottenberg, R.1    Jackson, C.M.2
  • 14
    • 0020964886 scopus 로고
    • Steady state kinetic parameters for the thrombin-catalyzed conversion of human fibrinogen to fibrin
    • Higgins DL, Lewis SD, Shafer JA. Steady state kinetic parameters for the thrombin-catalyzed conversion of human fibrinogen to fibrin. J Biol Chem. 1983;258(15):9276-9282.
    • (1983) J Biol Chem , vol.258 , Issue.15 , pp. 9276-9282
    • Higgins, D.L.1    Lewis, S.D.2    Shafer, J.A.3
  • 15
    • 0037020083 scopus 로고    scopus 로고
    • Prothrombinase assembly and S1 site occupation restore the catalytic activity of FXa impaired by mutation at the sodium-binding site
    • Camire RM. Prothrombinase assembly and S1 site occupation restore the catalytic activity of FXa impaired by mutation at the sodium-binding site. J Biol Chem. 2002;277(40):37863-37870.
    • (2002) J Biol Chem , vol.277 , Issue.40 , pp. 37863-37870
    • Camire, R.M.1
  • 16
    • 2442655492 scopus 로고    scopus 로고
    • Removal of B-domain sequences from factor V rather than specific proteolysis underlies the mechanism by which cofactor function is realized
    • Toso R, Camire RM. Removal of B-domain sequences from factor V rather than specific proteolysis underlies the mechanism by which cofactor function is realized. J Biol Chem. 2004; 279(20):21643-21650.
    • (2004) J Biol Chem , vol.279 , Issue.20 , pp. 21643-21650
    • Toso, R.1    Camire, R.M.2
  • 17
    • 0037135531 scopus 로고    scopus 로고
    • Nematode anticoagulant protein c2 reveals a site on factor Xa that is important for macromolecular substrate binding to human prothrombinase
    • Buddai SK, Toulokhonova L, Bergum PW, Vlasuk GP, Krishnaswamy S. Nematode anticoagulant protein c2 reveals a site on factor Xa that is important for macromolecular substrate binding to human prothrombinase. J Biol Chem. 2002; 277(29):26689-26698.
    • (2002) J Biol Chem , vol.277 , Issue.29 , pp. 26689-26698
    • Buddai, S.K.1    Toulokhonova, L.2    Bergum, P.W.3    Vlasuk, G.P.4    Krishnaswamy, S.5
  • 18
    • 0017142556 scopus 로고
    • Factor X activating enzyme from Russell's viper venom: Isolation and characterization
    • Kisiel W, Hermodson MA, Davie EW. Factor X activating enzyme from Russell's viper venom: isolation and characterization. Biochemistry. 1976;15(22):4901-4906.
    • (1976) Biochemistry , vol.15 , Issue.22 , pp. 4901-4906
    • Kisiel, W.1    Hermodson, M.A.2    Davie, E.W.3
  • 19
    • 0242401773 scopus 로고    scopus 로고
    • Calibrated automated thrombin generation measurement in clotting plasma
    • Hemker HC, Giesen P, Al Dieri R, et al. Calibrated automated thrombin generation measurement in clotting plasma. Pathophysiol Haemost Thromb. 2003;33(1):4-15.
    • (2003) Pathophysiol Haemost Thromb , vol.33 , Issue.1 , pp. 4-15
    • Hemker, H.C.1    Giesen, P.2    Al Dieri, R.3
  • 20
    • 0030817391 scopus 로고    scopus 로고
    • A coagulation factor IX-deficient mouse model for human hemophilia B
    • Lin HF, Maeda N, Smithies O, Straight DL, Stafford DW. A coagulation factor IX-deficient mouse model for human hemophilia B. Blood. 1997;90(10):3962-3966.
    • (1997) Blood , vol.90 , Issue.10 , pp. 3962-3966
    • Lin, H.F.1    Maeda, N.2    Smithies, O.3    Straight, D.L.4    Stafford, D.W.5
  • 21
    • 0032005213 scopus 로고    scopus 로고
    • Human factor IX corrects the bleeding diathesis of mice with hemophilia B
    • Kung SH, Hagstrom JN, Cass D, et al. Human factor IX corrects the bleeding diathesis of mice with hemophilia B. Blood. 1998;91(3):784-790.
    • (1998) Blood , vol.91 , Issue.3 , pp. 784-790
    • Kung, S.H.1    Hagstrom, J.N.2    Cass, D.3
  • 22
    • 29244443415 scopus 로고    scopus 로고
    • Factor V Leiden improves in vivo hemostasis in murine hemophilia models
    • Schlachterman A, Schuettrumpf J, Liu JH, et al. Factor V Leiden improves in vivo hemostasis in murine hemophilia models. J Thromb Haemost. 2005;3(12):2730-2737.
    • (2005) J Thromb Haemost , vol.3 , Issue.12 , pp. 2730-2737
    • Schlachterman, A.1    Schuettrumpf, J.2    Liu, J.H.3
  • 23
    • 0026719689 scopus 로고
    • Analysis of residuals: Criteria for determining goodness-of-fit
    • Straume M, Johnson ML. Analysis of residuals: criteria for determining goodness-of-fit. Methods Enzymol. 1992;210:87-105.
    • (1992) Methods Enzymol , vol.210 , pp. 87-105
    • Straume, M.1    Johnson, M.L.2
  • 25
    • 0032479424 scopus 로고    scopus 로고
    • Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by a template mechanism. Evidence that calcium alleviates Gla domain antagonism of heparin binding to factor Xa
    • Rezaie AR. Calcium enhances heparin catalysis of the antithrombin-factor Xa reaction by a template mechanism. Evidence that calcium alleviates Gla domain antagonism of heparin binding to factor Xa. J Biol Chem. 1998;273(27): 16824-16827.
    • (1998) J Biol Chem , vol.273 , Issue.27 , pp. 16824-16827
    • Rezaie, A.R.1
  • 26
    • 0034602993 scopus 로고    scopus 로고
    • Identification of basic residues in the heparin-binding exosite of factor Xa critical for heparin and factor Va binding
    • Rezaie AR. Identification of basic residues in the heparin-binding exosite of factor Xa critical for heparin and factor Va binding. J Biol Chem. 2000; 275(5):3320-3327.
    • (2000) J Biol Chem , vol.275 , Issue.5 , pp. 3320-3327
    • Rezaie, A.R.1
  • 27
    • 0035895875 scopus 로고    scopus 로고
    • Definition of a factor Va binding site in factor Xa
    • Rudolph AE, Porche-Sorbet R, Miletich JP. Definition of a factor Va binding site in factor Xa. J Biol Chem. 2001;276(7):5123-5128.
    • (2001) J Biol Chem , vol.276 , Issue.7 , pp. 5123-5128
    • Rudolph, A.E.1    Porche-Sorbet, R.2    Miletich, J.P.3
  • 29
    • 0031455114 scopus 로고    scopus 로고
    • Antithrombin. A bloody important serpin
    • Björk I, Olson ST. Antithrombin. A bloody important serpin. Adv Exp Med Biol. 1997;425: 17-33.
    • (1997) Adv Exp Med Biol , vol.425 , pp. 17-33
    • Björk, I.1    Olson, S.T.2
  • 30
    • 77952542376 scopus 로고    scopus 로고
    • Recombinant coagulation factor VIIa-from molecular to clinical aspects of a versatile haemostatic agent
    • Persson E, Bolt G, Steenstrup TD, Ezban M. Recombinant coagulation factor VIIa-from molecular to clinical aspects of a versatile haemostatic agent. Thromb Res. 2010;125(6): 483-489.
    • (2010) Thromb Res , vol.125 , Issue.6 , pp. 483-489
    • Persson, E.1    Bolt, G.2    Steenstrup, T.D.3    Ezban, M.4
  • 31
  • 33
    • 0021703070 scopus 로고
    • Studies of Factors V and VIII:C in an animal model of disseminated intravascular coagulation
    • Giles AR, Nesheim ME, Mann KG. Studies of Factors V and VIII:C in an animal model of disseminated intravascular coagulation. J Clin Invest. 1984;74(6):2219-2225.
    • (1984) J Clin Invest , vol.74 , Issue.6 , pp. 2219-2225
    • Giles, A.R.1    Nesheim, M.E.2    Mann, K.G.3
  • 34
    • 0023720558 scopus 로고
    • A combination of factor Xa and phosphatidylcholinephosphatidylserine vesicles bypasses factor VIII in vivo
    • Giles AR, Mann KG, Nesheim ME. A combination of factor Xa and phosphatidylcholinephosphatidylserine vesicles bypasses factor VIII in vivo. Br J Haematol. 1988;69(4):491-497.
    • (1988) Br J Haematol , vol.69 , Issue.4 , pp. 491-497
    • Giles, A.R.1    Mann, K.G.2    Nesheim, M.E.3
  • 35
    • 84905669201 scopus 로고    scopus 로고
    • TM;2 investigators. Recombinant factor VIIa analog in the management of hemophilia with inhibitors: Results from a multicenter, randomized, controlled trial of vatreptacog alfa
    • TM;2 investigators. Recombinant factor VIIa analog in the management of hemophilia with inhibitors: results from a multicenter, randomized, controlled trial of vatreptacog alfa. J Thromb Haemost. 2014; 12(8):1244-1253.
    • (2014) J Thromb Haemost , vol.12 , Issue.8 , pp. 1244-1253
    • Lentz, S.R.1    Ehrenforth, S.2    Karim, F.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.