메뉴 건너뛰기




Volumn 106, Issue 4, 2011, Pages 665-674

Factor VIII activation by factor VIIa analog (V158D/E296V/M298Q) in tissue factor-independent mechanisms

Author keywords

Activation; Cleavage; Factor viia analog; Factor VIII(a); Tissue factor

Indexed keywords

ARGININE; BLOOD CLOTTING FACTOR 8; NN 1731; RECOMBINANT BLOOD CLOTTING FACTOR 7A; THROMBOPLASTIN; UNCLASSIFIED DRUG;

EID: 80053209848     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH11-04-0264     Document Type: Article
Times cited : (2)

References (34)
  • 1
    • 0025311157 scopus 로고
    • Surface-dependent reactions of the vitamin K-dependent enzyme complexes
    • Mann KG, Nesheim ME, Church WR, et al. Surface-dependent reactions of the vitamin K-dependent enzyme complexes. Blood 1990; 76: 1-16.
    • (1990) Blood , vol.76 , pp. 1-16
    • Mann, K.G.1    Nesheim, M.E.2    Church, W.R.3
  • 2
    • 0021715168 scopus 로고
    • Expression of active human factor VIII from recombinant DNA clones
    • Wood WI, Capon DJ, Simonsen CC, et al. Expression of active human factor VIII from recombinant DNA clones. Nature 1984; 312: 330-337.
    • (1984) Nature , vol.312 , pp. 330-337
    • Wood, W.I.1    Capon, D.J.2    Simonsen, C.C.3
  • 3
    • 0022454539 scopus 로고
    • Proteolytic processing of human factor VIII. Correlation of specific cleavages by thrombin, factor Xa, and activated protein C with activation and inactivation of factor VIII coagulant activity
    • Eaton D, Rodriguez H, Vehar GA. Proteolytic processing of human factor VIII. Correlation of specific cleavages by thrombin, factor Xa, and activated protein C with activation and inactivation of factor VIII coagulant activity. Biochemistry 1986; 25: 505-512.
    • (1986) Biochemistry , vol.25 , pp. 505-512
    • Eaton, D.1    Rodriguez, H.2    Vehar, G.A.3
  • 4
    • 1042276751 scopus 로고    scopus 로고
    • Activation of factor VIII and mechanisms of cofactor action
    • Fay PJ. Activation of factor VIII and mechanisms of cofactor action. Blood Rev 2004; 18: 1-15.
    • (2004) Blood Rev , vol.18 , pp. 1-15
    • Fay, P.J.1
  • 5
    • 0035853784 scopus 로고    scopus 로고
    • Cleavage of factor VIII heavy chain is required for the functional interaction of A2 subunit with factor IXa
    • Fay PJ, Mastri M, Koszelak ME, et al. Cleavage of factor VIII heavy chain is required for the functional interaction of A2 subunit with factor IXa. J Biol Chem 2001; 276: 12434-12439.
    • (2001) J Biol Chem , vol.276 , pp. 12434-12439
    • Fay, P.J.1    Mastri, M.2    Koszelak, M.E.3
  • 6
    • 0023677854 scopus 로고
    • Association of the factor VIII light chain with von Willebrand factor
    • Lollar P, Hill-Eubanks DC, Parker CG. Association of the factor VIII light chain with von Willebrand factor. J Biol Chem 1988; 263: 10451-10455.
    • (1988) J Biol Chem , vol.263 , pp. 10451-10455
    • Lollar, P.1    Hill-Eubanks, D.C.2    Parker, C.G.3
  • 7
    • 0037449806 scopus 로고    scopus 로고
    • Altered interactions between the A1 and A2 subunits of factor VIIIa following cleavage of A1 subunit by factor Xa
    • Nogami K, Wakabayashi H, Schmidt K, et al. Altered interactions between the A1 and A2 subunits of factor VIIIa following cleavage of A1 subunit by factor Xa. J Biol Chem 2003; 278: 1634-1641.
    • (2003) J Biol Chem , vol.278 , pp. 1634-1641
    • Nogami, K.1    Wakabayashi, H.2    Schmidt, K.3
  • 8
    • 0025010978 scopus 로고
    • Proteolytic activation of human factors IX and X by recombinant human factor VIIa: Effects of calcium, phospholipids, and tissue factor
    • Komiyama Y, Pedersen AH, Kisiel W. Proteolytic activation of human factors IX and X by recombinant human factor VIIa: effects of calcium, phospholipids, and tissue factor. Biochemistry 1990; 29: 9418-9425.
    • (1990) Biochemistry , vol.29 , pp. 9418-9425
    • Komiyama, Y.1    Pedersen, A.H.2    Kisiel, W.3
  • 9
    • 1842678190 scopus 로고    scopus 로고
    • Remodeling the blood coagulation cascade
    • Hoffman M. Remodeling the blood coagulation cascade. J Thromb Thrombolysis 2003; 16: 17-20.
    • (2003) J Thromb Thrombolysis , vol.16 , pp. 17-20
    • Hoffman, M.1
  • 11
    • 78149255398 scopus 로고    scopus 로고
    • Mechanisms of factor VIIa-catalyzed activation of factor VIII
    • Soeda T, Nogami K, Matsumoto T, et al. Mechanisms of factor VIIa-catalyzed activation of factor VIII. J Thromb Haemost 2010; 8: 2494-2503.
    • (2010) J Thromb Haemost , vol.8 , pp. 2494-2503
    • Soeda, T.1    Nogami, K.2    Matsumoto, T.3
  • 12
    • 66449121335 scopus 로고    scopus 로고
    • Cleavage at Arg1689 influences heavy chain cleavages during thrombin-catalyzed activation of factor VIII
    • Newell JL, Fay PJ. Cleavage at Arg1689 influences heavy chain cleavages during thrombin-catalyzed activation of factor VIII. J Biol Chem 2009; 284: 11080-11089.
    • (2009) J Biol Chem , vol.284 , pp. 11080-11089
    • Newell, J.L.1    Fay, P.J.2
  • 13
    • 13244291354 scopus 로고    scopus 로고
    • Recombinant human factor VIIa (rFVIIa) can activate factor FIX on activated platelets
    • Gabriel DA, Li X, Monroe DM 3rd, et al. Recombinant human factor VIIa (rFVIIa) can activate factor FIX on activated platelets. J Thromb Haemost 2004; 2: 1816-1822.
    • (2004) J Thromb Haemost , vol.2 , pp. 1816-1822
    • Gabriel, D.A.1    Li, X.2    Monroe III, D.M.3
  • 14
    • 33746021125 scopus 로고    scopus 로고
    • Mechanism of action, development and clinical experience of recombinant FVIIa
    • Hedner U. Mechanism of action, development and clinical experience of recombinant FVIIa. J Biotechnol 2006; 124: 747-757.
    • (2006) J Biotechnol , vol.124 , pp. 747-757
    • Hedner, U.1
  • 15
    • 0030695063 scopus 로고    scopus 로고
    • Platelet activity of high-dose factor VIIa in independent of tissue factor
    • Monroe D, Hoffman M, Oliver J, et al. Platelet activity of high-dose factor VIIa in independent of tissue factor. Br J Haematol 1997; 99: 542-547.
    • (1997) Br J Haematol , vol.99 , pp. 542-547
    • Monroe, D.1    Hoffman, M.2    Oliver, J.3
  • 16
    • 34548317168 scopus 로고    scopus 로고
    • Effect of recombinant factor VIIa variant (NN1731) on platelet function, clot structure and force onset time in whole blood from healthy volunteers and haemophilia patients
    • Brophy DF, Martin EJ, Nolte ME, et al. Effect of recombinant factor VIIa variant (NN1731) on platelet function, clot structure and force onset time in whole blood from healthy volunteers and haemophilia patients. Haemophilia 2007; 13: 533-541.
    • (2007) Haemophilia , vol.13 , pp. 533-541
    • Brophy, D.F.1    Martin, E.J.2    Nolte, M.E.3
  • 17
    • 0035923721 scopus 로고    scopus 로고
    • Rational design of coagulation factor VIIa variants with substantially increased intrinsic activity
    • Persson E, Kjalke M, Olsen OH. Rational design of coagulation factor VIIa variants with substantially increased intrinsic activity. Proc Natl Acad Sci USA 2001; 98: 13583-13588.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 13583-13588
    • Persson, E.1    Kjalke, M.2    Olsen, O.H.3
  • 18
    • 33847054740 scopus 로고    scopus 로고
    • A variant of recombinant factor VIIa with enhanced procoagulant and antifibrinolytic activities in an in vitro model of hemophilia
    • Allen GA, Persson E, Campbell A, et al. A variant of recombinant factor VIIa with enhanced procoagulant and antifibrinolytic activities in an in vitro model of hemophilia. Arterioscler Thromb Vasc Biol 2007; 27: 683-689.
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 683-689
    • Allen, G.A.1    Persson, E.2    Campbell, A.3
  • 19
    • 69249216581 scopus 로고    scopus 로고
    • Faster onset of effect and greater efficacy of NN1731 compared with rFVIIa, aPCC and FVIII in tail bleeding in hemophilic mice
    • Holmberg HL, Lauritzen B, Tranholm M, et al. Faster onset of effect and greater efficacy of NN1731 compared with rFVIIa, aPCC and FVIII in tail bleeding in hemophilic mice. J Thromb Haemost 2009; 7: 1517-1522.
    • (2009) J Thromb Haemost , vol.7 , pp. 1517-1522
    • Holmberg, H.L.1    Lauritzen, B.2    Tranholm, M.3
  • 20
    • 33947494621 scopus 로고    scopus 로고
    • Factor VIIa analogue (V158D/E296V/M298Q-FVIIa) normalises clot formation in whole blood from patients with severe haemophilia A
    • Sorensen B, Persson E, Ingerslev J. Factor VIIa analogue (V158D/E296V/M298Q-FVIIa) normalises clot formation in whole blood from patients with severe haemophilia A. Br J Haematol 2007; 137: 158-165.
    • (2007) Br J Haematol , vol.137 , pp. 158-165
    • Sorensen, B.1    Persson, E.2    Ingerslev, J.3
  • 21
    • 41949109750 scopus 로고    scopus 로고
    • Identification of a plasmin-interactive site within the A2 domain of the factor VIII heavy chain
    • Nogami K, Nishiya K, Saenko EL, et al. Identification of a plasmin-interactive site within the A2 domain of the factor VIII heavy chain. Biochim Biophys Acta 2008; 1784: 753-763.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 753-763
    • Nogami, K.1    Nishiya, K.2    Saenko, E.L.3
  • 22
    • 0030664471 scopus 로고    scopus 로고
    • Characterization of a genetically engineered inactivationresistant coagulation factor VIIIa
    • Pipe SW, Kaufman RJ. Characterization of a genetically engineered inactivationresistant coagulation factor VIIIa. Proc Natl Acad Sci USA 1997; 94: 11851-11856.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11851-11856
    • Pipe, S.W.1    Kaufman, R.J.2
  • 23
    • 0038291903 scopus 로고    scopus 로고
    • The preparation and phospholipid binding property of the C2 domain of human factor VIII
    • Takeshima K, Smith C, Tait J, et al. The preparation and phospholipid binding property of the C2 domain of human factor VIII. Thromb Haemost 2003; 89: 88-94.
    • (2003) Thromb Haemost , vol.89 , pp. 88-94
    • Takeshima, K.1    Smith, C.2    Tait, J.3
  • 24
    • 0027457180 scopus 로고
    • A factor VIII neutralizing monoclonal antibody and a human inhibitor alloantibody recognizing epitopes in the C2 domain inhibit factor VIII binding to von Willebrand factor and to phosphatidylserine
    • Shima M, Scandella D, Yoshioka A, et al. A factor VIII neutralizing monoclonal antibody and a human inhibitor alloantibody recognizing epitopes in the C2 domain inhibit factor VIII binding to von Willebrand factor and to phosphatidylserine. Thromb Haemost 1993; 69: 240-246.
    • (1993) Thromb Haemost , vol.69 , pp. 240-246
    • Shima, M.1    Scandella, D.2    Yoshioka, A.3
  • 25
    • 0023768345 scopus 로고    scopus 로고
    • Localization of the binding regions of a murine monoclonal anti-factor VIII antibody and a human anti-factor VIII alloantibody, both of which inhibit factor VIII procoagulant activity, to amino acid residues threonine351-serine365 of the factor VIII heavy chain
    • Foster PA, Fulcher CA, Houghten RA, et al. Localization of the binding regions of a murine monoclonal anti-factor VIII antibody and a human anti-factor VIII alloantibody, both of which inhibit factor VIII procoagulant activity, to amino acid residues threonine351-serine365 of the factor VIII heavy chain. J Clin Invest 1998; 82: 123-128.
    • (1998) J Clin Invest , vol.82 , pp. 123-128
    • Foster, P.A.1    Fulcher, C.A.2    Houghten, R.A.3
  • 26
    • 0019883158 scopus 로고
    • Phospholipid vesicle formation and transmembrane protein incorporation using octyl glucoside
    • Mimms LT, Zampighi G, Nozaki Y, et al. Phospholipid vesicle formation and transmembrane protein incorporation using octyl glucoside. Biochemistry 1981; 20: 833-840.
    • (1981) Biochemistry , vol.20 , pp. 833-840
    • Mimms, L.T.1    Zampighi, G.2    Nozaki, Y.3
  • 27
    • 0033580639 scopus 로고    scopus 로고
    • Proteolysis of blood coagulation factor VIII by the factor VIIa-tissue factor complex: Generation of an inactive factor VIII cofactor
    • Warren DL, Morrissey JH, Neuenschwander PF. Proteolysis of blood coagulation factor VIII by the factor VIIa-tissue factor complex: generation of an inactive factor VIII cofactor. Biochemistry 1999; 38: 6529-6536.
    • (1999) Biochemistry , vol.38 , pp. 6529-6536
    • Warren, D.L.1    Morrissey, J.H.2    Neuenschwander, P.F.3
  • 28
    • 0030991982 scopus 로고    scopus 로고
    • Incorporation of an active site inhibitor in factor VIIa alters the affinity for tissue factor
    • Sorensen BB, Persson E, Freskgârd PO, et al. Incorporation of an active site inhibitor in factor VIIa alters the affinity for tissue factor. J Biol Chem 1997; 272: 11863-11868.
    • (1997) J Biol Chem , vol.272 , pp. 11863-11868
    • Sorensen, B.B.1    Persson, E.2    Freskgârd, P.O.3
  • 29
    • 0028062901 scopus 로고
    • Kinetics of the inhibition of factor Xa and the tissue factor-factor VIIa complex by the tissue factor pathway inhibitor in the presence and absence of heparin
    • Jesty J, Wun TC, Lorenz A. Kinetics of the inhibition of factor Xa and the tissue factor-factor VIIa complex by the tissue factor pathway inhibitor in the presence and absence of heparin. Biochemistry 1994; 33: 12686-12694.
    • (1994) Biochemistry , vol.33 , pp. 12686-12694
    • Jesty, J.1    Wun, T.C.2    Lorenz, A.3
  • 30
    • 0027932735 scopus 로고
    • Activated factor X and thrombin formation triggered by tissue factor on endothelial cell matrix in a flow model: Effect of the tissue factor pathway inhibitor
    • van 't Veer C, Hackeng TM, Delahaye C, et al. Activated factor X and thrombin formation triggered by tissue factor on endothelial cell matrix in a flow model: effect of the tissue factor pathway inhibitor. Blood 1994; 84: 1132-1142.
    • (1994) Blood , vol.84 , pp. 1132-1142
    • van 't Veer, C.1    Hackeng, T.M.2    Delahaye, C.3
  • 31
    • 63049090494 scopus 로고    scopus 로고
    • Differential response to bypassing agents complicates treatment in patients with haemophilia and inhibitors
    • Berntorp E. Differential response to bypassing agents complicates treatment in patients with haemophilia and inhibitors. Haemophilia 2009; 15: 3-10.
    • (2009) Haemophilia , vol.15 , pp. 3-10
    • Berntorp, E.1
  • 32
    • 4043142885 scopus 로고    scopus 로고
    • Effectiveness of factor VIII infusions in haemophilia A patients with high responding inhibitors
    • Kasuda S, Tanaka I, Shima M, et al. Effectiveness of factor VIII infusions in haemophilia A patients with high responding inhibitors. Haemophilia 2004; 10: 341-346.
    • (2004) Haemophilia , vol.10 , pp. 341-346
    • Kasuda, S.1    Tanaka, I.2    Shima, M.3
  • 33
    • 39649102400 scopus 로고    scopus 로고
    • Anti-human factor VIII C2 domain antibodies in hemophilia A mice recognize a functionally complex continuous spectrum of epitopes dominated by inhibitors of factor VIII activation
    • Meeks SL, Healey JF, Parker ET, et al. Anti-human factor VIII C2 domain antibodies in hemophilia A mice recognize a functionally complex continuous spectrum of epitopes dominated by inhibitors of factor VIII activation. Blood 2007; 110: 4234-4242.
    • (2007) Blood , vol.110 , pp. 4234-4242
    • Meeks, S.L.1    Healey, J.F.2    Parker, E.T.3
  • 34
    • 79958153738 scopus 로고    scopus 로고
    • Effects of anti-factor VIII inhibitor antibodies on factor VIIa/tissue factor-catalyzed activation and inactivation of factor VIII
    • Yada K, Nogami K, Ogiwara K, et al. Effects of anti-factor VIII inhibitor antibodies on factor VIIa/tissue factor-catalyzed activation and inactivation of factor VIII. Thromb Haemost 2011; 106: 989-998.
    • (2011) Thromb Haemost , vol.106 , pp. 989-998
    • Yada, K.1    Nogami, K.2    Ogiwara, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.