메뉴 건너뛰기




Volumn 12, Issue 3, 2014, Pages 363-372

Improved hemostasis in hemophilia mice by means of an engineered factor Va mutant

Author keywords

Animal experimentation; Bleeding; Factor V; Hemophilia; Hemostasis

Indexed keywords

ACTIVATED PROTEIN C; BLOOD CLOTTING FACTOR 10A; BLOOD CLOTTING FACTOR 5; BLOOD CLOTTING FACTOR 5A; BLOOD CLOTTING FACTOR 8; THROMBIN;

EID: 84896802437     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1111/jth.12489     Document Type: Article
Times cited : (29)

References (33)
  • 1
    • 0031760564 scopus 로고    scopus 로고
    • Activated factor VII activates factors IX and X on the surface of activated platelets: thoughts on the mechanism of action of high-dose activated factor VII
    • Hoffman M, Monroe DM, Roberts HR. Activated factor VII activates factors IX and X on the surface of activated platelets: thoughts on the mechanism of action of high-dose activated factor VII. Blood Coagul Fibrinolysis 1998; 9 (Suppl. 1): S61-5.
    • (1998) Blood Coagul Fibrinolysis , vol.9 , Issue.Suppl. 1
    • Hoffman, M.1    Monroe, D.M.2    Roberts, H.R.3
  • 2
    • 0033767885 scopus 로고    scopus 로고
    • The regulation of the factor VII-dependent coagulation pathway: rationale for the effectiveness of recombinant factor VIIa in refractory bleeding disorders
    • van't Veer C, Mann KG. The regulation of the factor VII-dependent coagulation pathway: rationale for the effectiveness of recombinant factor VIIa in refractory bleeding disorders. Semin Thromb Hemost 2000; 26: 367-72.
    • (2000) Semin Thromb Hemost , vol.26 , pp. 367-372
    • van't Veer, C.1    Mann, K.G.2
  • 3
    • 33846185403 scopus 로고    scopus 로고
    • A randomized comparison of bypassing agents in hemophilia complicated by an inhibitor: the FEIBA NovoSeven Comparative (FENOC) Study
    • Astermark J, Donfield SM, DiMichele DM, Gringeri A, Gilbert SA, Waters J, Berntorp E, Group FS. A randomized comparison of bypassing agents in hemophilia complicated by an inhibitor: the FEIBA NovoSeven Comparative (FENOC) Study. Blood 2007; 109: 546-51.
    • (2007) Blood , vol.109 , pp. 546-551
    • Astermark, J.1    Donfield, S.M.2    DiMichele, D.M.3    Gringeri, A.4    Gilbert, S.A.5    Waters, J.6    Berntorp, E.7    Group, F.S.8
  • 4
    • 44649185547 scopus 로고    scopus 로고
    • Arthropathy in inhibitor patients: differences in the joint status
    • Hoots WK. Arthropathy in inhibitor patients: differences in the joint status. Semin Hematol 2008; 45: S42-9.
    • (2008) Semin Hematol , vol.45
    • Hoots, W.K.1
  • 6
    • 59049098711 scopus 로고    scopus 로고
    • Evaluation of the safety and pharmacokinetics of a fast-acting recombinant FVIIa analogue, NN1731, in healthy male subjects
    • Møss J, Scharling B, Ezban M, Møller Sørensen T. Evaluation of the safety and pharmacokinetics of a fast-acting recombinant FVIIa analogue, NN1731, in healthy male subjects. J Thromb Haemost 2009; 7: 299-305.
    • (2009) J Thromb Haemost , vol.7 , pp. 299-305
    • Møss, J.1    Scharling, B.2    Ezban, M.3    Møller Sørensen, T.4
  • 9
    • 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: 18627-35.
    • (2008) J Biol Chem , vol.283 , pp. 18627-18635
    • Toso, R.1    Zhu, H.2    Camire, R.M.3
  • 10
    • 0023924910 scopus 로고
    • Cofactor proteins in the assembly and expression of blood clotting enzyme complexes
    • Mann KG, Jenny RJ, Krishnaswamy S. Cofactor proteins in the assembly and expression of blood clotting enzyme complexes. Annu Rev Biochem 1988; 57: 915-56.
    • (1988) Annu Rev Biochem , vol.57 , pp. 915-956
    • Mann, K.G.1    Jenny, R.J.2    Krishnaswamy, S.3
  • 11
    • 0018622772 scopus 로고
    • The contribution of bovine Factor V and Factor Va to the activity of prothrombinase
    • Nesheim ME, Taswell JB, Mann KG. The contribution of bovine Factor V and Factor Va to the activity of prothrombinase. J Biol Chem 1979; 254: 10952-62.
    • (1979) J Biol Chem , vol.254 , pp. 10952-10962
    • Nesheim, M.E.1    Taswell, J.B.2    Mann, K.G.3
  • 12
    • 0036707993 scopus 로고    scopus 로고
    • Interdomain engineered disulfide bond permitting elucidation of mechanisms of inactivation of coagulation factor Va by activated protein C
    • Gale AJ, Xu X, Pellequer JL, Getzoff ED, Griffin JH. Interdomain engineered disulfide bond permitting elucidation of mechanisms of inactivation of coagulation factor Va by activated protein C. Protein Sci 2002; 11: 2091-101.
    • (2002) Protein Sci , vol.11 , pp. 2091-2101
    • Gale, A.J.1    Xu, X.2    Pellequer, J.L.3    Getzoff, E.D.4    Griffin, J.H.5
  • 13
    • 23944516887 scopus 로고    scopus 로고
    • Does activated protein C-resistant factor V contribute to thrombin generation in hemophilic plasma?
    • Bos MH, Meijerman DW, van der Zwaan C, Mertens K. Does activated protein C-resistant factor V contribute to thrombin generation in hemophilic plasma? J Thromb Haemost 2005; 3: 522-30.
    • (2005) J Thromb Haemost , vol.3 , pp. 522-530
    • Bos, M.H.1    Meijerman, D.W.2    van der Zwaan, C.3    Mertens, K.4
  • 16
    • 76449092195 scopus 로고    scopus 로고
    • Factor V Leiden and hemophilia
    • Franchini M, Lippi G. Factor V Leiden and hemophilia. Thromb Res 2010; 125: 119-23.
    • (2010) Thromb Res , vol.125 , pp. 119-123
    • Franchini, M.1    Lippi, G.2
  • 17
    • 0026321606 scopus 로고
    • Identification of a sequence of human activated protein-C (residues 390-404). Essential for its anticoagulant activity
    • Mesters R, Houghten R, Griffin J. Identification of a sequence of human activated protein-C (residues 390-404). Essential for its anticoagulant activity. J Biol Chem 1991; 266: 24514-9.
    • (1991) J Biol Chem , vol.266 , pp. 24514-24519
    • Mesters, R.1    Houghten, R.2    Griffin, J.3
  • 18
    • 85027928249 scopus 로고    scopus 로고
    • Factor V is an anticoagulant cofactor for activated protein C during inactivation of factor Va
    • Cramer TJ, Griffin JH, Gale AJ. Factor V is an anticoagulant cofactor for activated protein C during inactivation of factor Va. Pathophysiol Haemost Thromb 2010; 37: 17-23.
    • (2010) Pathophysiol Haemost Thromb , vol.37 , pp. 17-23
    • Cramer, T.J.1    Griffin, J.H.2    Gale, A.J.3
  • 19
    • 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: 21643-50.
    • (2004) J Biol Chem , vol.279 , pp. 21643-21650
    • Toso, R.1    Camire, R.M.2
  • 20
    • 36349014743 scopus 로고    scopus 로고
    • Activated protein C mutant with minimal anticoagulant activity, normal cytoprotective activity, and preservation of thrombin activable fibrinolysis inhibitor-dependent cytoprotective functions
    • Mosnier LO, Yang XV, Griffin JH. Activated protein C mutant with minimal anticoagulant activity, normal cytoprotective activity, and preservation of thrombin activable fibrinolysis inhibitor-dependent cytoprotective functions. J Biol Chem 2007; 282: 33022-33.
    • (2007) J Biol Chem , vol.282 , pp. 33022-33033
    • Mosnier, L.O.1    Yang, X.V.2    Griffin, J.H.3
  • 22
    • 84875530235 scopus 로고    scopus 로고
    • Antibody SPC-54 provides acute in vivo blockage of the murine protein C system
    • Burnier L, Fernández JA, Griffin JH. Antibody SPC-54 provides acute in vivo blockage of the murine protein C system. Blood Cells Mol Dis 2013; 50: 252-8.
    • (2013) Blood Cells Mol Dis , vol.50 , pp. 252-258
    • Burnier, L.1    Fernández, J.A.2    Griffin, J.H.3
  • 24
    • 2342666603 scopus 로고    scopus 로고
    • An engineered interdomain disulfide bond stabilizes human blood coagulation factor VIIIa
    • Gale AJ, Pellequer JL. An engineered interdomain disulfide bond stabilizes human blood coagulation factor VIIIa. J Thromb Haemost 2003; 1: 1966-71.
    • (2003) J Thromb Haemost , vol.1 , pp. 1966-1971
    • Gale, A.J.1    Pellequer, J.L.2
  • 26
    • 0018786088 scopus 로고
    • The subunit structure of thrombin-activated factor V. Isolation of activated factor V, separation of subunits, and reconstitution of biological activity
    • Esmon CT. The subunit structure of thrombin-activated factor V. Isolation of activated factor V, separation of subunits, and reconstitution of biological activity. J Biol Chem 1979; 254: 964-73.
    • (1979) J Biol Chem , vol.254 , pp. 964-973
    • Esmon, C.T.1
  • 27
    • 22544469092 scopus 로고    scopus 로고
    • Ratcheting of the substrate from the zymogen to proteinase conformations directs the sequential cleavage of prothrombin by prothrombinase
    • Bianchini EP, Orcutt SJ, Panizzi P, Bock PE, Krishnaswamy S. Ratcheting of the substrate from the zymogen to proteinase conformations directs the sequential cleavage of prothrombin by prothrombinase. Proc Natl Acad Sci U S A 2005; 102: 10099-104.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 10099-10104
    • Bianchini, E.P.1    Orcutt, S.J.2    Panizzi, P.3    Bock, P.E.4    Krishnaswamy, S.5
  • 28
    • 36349000220 scopus 로고    scopus 로고
    • Further evidence for two functional forms of prothrombinase each specific for either of the two prothrombin activation cleavages
    • Kim PY, Nesheim ME. Further evidence for two functional forms of prothrombinase each specific for either of the two prothrombin activation cleavages. J Biol Chem 2007; 282: 32568-81.
    • (2007) J Biol Chem , vol.282 , pp. 32568-32581
    • Kim, P.Y.1    Nesheim, M.E.2
  • 30
    • 0030792746 scopus 로고    scopus 로고
    • Factor XI activation by meizothrombin: stimulation by phospholipid vesicles containing both phosphatidylserine and phosphatidylethanolamine
    • von dem Borne PA, Mosnier LO, Tans G, Meijers JC, Bouma BN. Factor XI activation by meizothrombin: stimulation by phospholipid vesicles containing both phosphatidylserine and phosphatidylethanolamine. Thromb Haemost 1997; 78: 834-9.
    • (1997) Thromb Haemost , vol.78 , pp. 834-839
    • von dem Borne, P.A.1    Mosnier, L.O.2    Tans, G.3    Meijers, J.C.4    Bouma, B.N.5
  • 31
    • 80055107829 scopus 로고    scopus 로고
    • Activated protein C inhibitor for correction of thrombin generation in hemophilia A blood and plasma
    • Brummel-Ziedins KE, Whelihan MF, Rivard GE, Butenas S. Activated protein C inhibitor for correction of thrombin generation in hemophilia A blood and plasma. J Thromb Haemost 2011; 9: 2262-7.
    • (2011) J Thromb Haemost , vol.9 , pp. 2262-2267
    • Brummel-Ziedins, K.E.1    Whelihan, M.F.2    Rivard, G.E.3    Butenas, S.4
  • 32
    • 33750058557 scopus 로고    scopus 로고
    • Peptidomimetic inhibitors for activated protein C: implications for hemophilia management
    • Butenas S, Orfeo T, Kalafatis M, Mann KG. Peptidomimetic inhibitors for activated protein C: implications for hemophilia management. J Thromb Haemost 2006; 4: 2411-6.
    • (2006) J Thromb Haemost , vol.4 , pp. 2411-2416
    • Butenas, S.1    Orfeo, T.2    Kalafatis, M.3    Mann, K.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.