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Volumn 422, Issue 2, 2009, Pages 257-264

Differential contributions of Glu96, Asp102 and Asp111 to coagulation Factor V/Va metal ion binding and subunit stability

Author keywords

B domain; Calcium; Coagulation; Copper; Factor V; Subunit

Indexed keywords

ACTIVATED PLATELETS; B DOMAIN; BLOOD COAGULATION; COAGULATION FACTOR; DIFFERENTIAL CONTRIBUTION; FACTOR V; HETERODIMERS; INDIRECT EFFECTS; METAL ION BINDING; NORMAL METALS; SUBUNIT; SUBUNIT DISSOCIATION; SUBUNIT INTERFACES; WILD TYPES;

EID: 70149084537     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20090405     Document Type: Article
Times cited : (7)

References (38)
  • 3
    • 0023918199 scopus 로고
    • Blood coagulation factors V and VIII: Structural and functional similarities and their relationship to hemorrhagic and thrombotic disorders
    • Kane, W. H. and Davie, E. W. (1988) Blood coagulation factors V and VIII: structural and functional similarities and their relationship to hemorrhagic and thrombotic disorders. Blood 71, 539-555
    • (1988) Blood , vol.71 , pp. 539-555
    • Kane, W.H.1    Davie, E.W.2
  • 4
    • 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. and Camire R. M. (2004) Removal of B-domain sequences from factor V rather than specific proteolysis underlies the mechanism by which cofactor function is realized. J. Biol. Chem. 21643-21650
    • (2004) J. Biol. Chem , pp. 21643-21650
    • Toso, R.1    Camire, R.M.2
  • 5
    • 0020320628 scopus 로고
    • Thrombin-calalyzed activation of human coagulation factor V
    • Suzuki, K., Dahlback, B. and Stenflo, J. (1982) Thrombin-calalyzed activation of human coagulation factor V. J. Biol. Chem. 257, 6556-6564
    • (1982) J. Biol. Chem , vol.257 , pp. 6556-6564
    • Suzuki, K.1    Dahlback, B.2    Stenflo, J.3
  • 6
    • 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, C. T. (1979) The subunit structure of thrombin-activated factor V. Isolation of activated factor V, separation of subunits, and reconstitution of biological activity. J. Biol. Chem. 254, 964-973
    • (1979) J. Biol. Chem , vol.254 , pp. 964-973
    • Esmon, C.T.1
  • 7
    • 0024509988 scopus 로고
    • The reassociation of factor Va from its isolated subunits
    • Krishnaswamy, S., Russell, G. D. and Mann, K. G. (1989) The reassociation of factor Va from its isolated subunits. J. Biol. Chem. 254, 3160-3168
    • (1989) J. Biol. Chem , vol.254 , pp. 3160-3168
    • Krishnaswamy, S.1    Russell, G.D.2    Mann, K.G.3
  • 8
    • 0018822977 scopus 로고
    • The calcium-binding properties of bovine factor V
    • Hibbard, L. S. and Mann, K. G. (1980) The calcium-binding properties of bovine factor V. J. Biol. Chem. 255, 638-645
    • (1980) J. Biol. Chem , vol.255 , pp. 638-645
    • Hibbard, L.S.1    Mann, K.G.2
  • 9
    • 0020414822 scopus 로고
    • Formation of a calcium-binding site on bovine activated factor V following recombination of the isolated subunits
    • Guinto, E. R. and Esmon, C. T. (1982) Formation of a calcium-binding site on bovine activated factor V following recombination of the isolated subunits. J. Biol. Chem. 257, 10038-10043
    • (1982) J. Biol. Chem , vol.257 , pp. 10038-10043
    • Guinto, E.R.1    Esmon, C.T.2
  • 11
    • 2942669901 scopus 로고    scopus 로고
    • The crystal structure of activated protein C-inactivated bovine factor Va: Implications for cofactor function
    • Adams, T. E., Hockin, M. F., Mann, K. G. and Everse, S. J. (2004) The crystal structure of activated protein C-inactivated bovine factor Va: Implications for cofactor function. Proc. Nat. Acad. Sci. U.S.A. 101, 8918-8923
    • (2004) Proc. Nat. Acad. Sci. U.S.A , vol.101 , pp. 8918-8923
    • Adams, T.E.1    Hockin, M.F.2    Mann, K.G.3    Everse, S.J.4
  • 13
    • 2642679231 scopus 로고    scopus 로고
    • Structural investigation of the A domains of human blood coagulation factor V by molecular modeling
    • Villoutreix, B. O. and Dahlback, B. (1998) Structural investigation of the A domains of human blood coagulation factor V by molecular modeling. Prot. Sci. 7, 1317-1325
    • (1998) Prot. Sci , vol.7 , pp. 1317-1325
    • Villoutreix, B.O.1    Dahlback, B.2
  • 14
    • 0033709870 scopus 로고    scopus 로고
    • Three-dimensional model of coagulation factor Va bound to activated protein C
    • Pellequer, J.-L., Gale, A. J., Getzoff, E. D. and Griffin, J. H. (2000) Three-dimensional model of coagulation factor Va bound to activated protein C. Thromb. Haemost. 84, 849-857
    • (2000) Thromb. Haemost , vol.84 , pp. 849-857
    • Pellequer, J.-L.1    Gale, A.J.2    Getzoff, E.D.3    Griffin, J.H.4
  • 16
    • 25444438704 scopus 로고    scopus 로고
    • Completed three-dimensional model of human coagulation factor Va. Molecular dynamics simulations and structural analyses
    • Orban, T., Kalafatis, M. and Gogonea, V. (2005) Completed three-dimensional model of human coagulation factor Va. Molecular dynamics simulations and structural analyses. Biochemistry 44, 13082-13090
    • (2005) Biochemistry , vol.44 , pp. 13082-13090
    • Orban, T.1    Kalafatis, M.2    Gogonea, V.3
  • 17
    • 0035827682 scopus 로고    scopus 로고
    • 2+-dependent complex of fragments bound to phospholipid
    • 2+-dependent complex of fragments bound to phospholipid. J. Biol. Chem. 276 (23), 19929-19936
    • (2001) J. Biol. Chem , vol.276 , Issue.23 , pp. 19929-19936
    • Zeibdawi, A.R.1    Pryzdial, E.L.G.2
  • 18
    • 1642535321 scopus 로고    scopus 로고
    • Coagulation factor Va Glu96-Asp111:A chelator-sensitive site involved in function and subunit association
    • Zeibdawi, A. R., Grundy, J. E., Lasia, B. and Pryzdial, E. L. G. (2004) Coagulation factor Va Glu96-Asp111:A chelator-sensitive site involved in function and subunit association. Biochem. J. 377, 141-148
    • (2004) Biochem. J , vol.377 , pp. 141-148
    • Zeibdawi, A.R.1    Grundy, J.E.2    Lasia, B.3    Pryzdial, E.L.G.4
  • 20
    • 0035967527 scopus 로고    scopus 로고
    • Binding of plasminogen and tissue plasminogen activator to plasmin-modulated factor X and factor Xa
    • Grundy, J. E., Lavigne, N., Hirama, T., MacKenzie, C. R. and Pryzdial, E. L. G. (2001) Binding of plasminogen and tissue plasminogen activator to plasmin-modulated factor X and factor Xa. Biochemistry 40, 6293-6302
    • (2001) Biochemistry , vol.40 , pp. 6293-6302
    • Grundy, J.E.1    Lavigne, N.2    Hirama, T.3    MacKenzie, C.R.4    Pryzdial, E.L.G.5
  • 21
    • 0018780186 scopus 로고
    • Phospholipid-binding properties of bovine factor V and factor Va
    • Bloom, J. W., Nesheim, M. E. and Mann, K. G. (1979) Phospholipid-binding properties of bovine factor V and factor Va. Biochemistry 18, 4419-4425
    • (1979) Biochemistry , vol.18 , pp. 4419-4425
    • Bloom, J.W.1    Nesheim, M.E.2    Mann, K.G.3
  • 22
    • 0020633335 scopus 로고
    • The interaction of bovine factor V and factor V-derived peptides with phospholipid vesicles
    • Higgins, D. L. and Mann, K. G. (1983) The interaction of bovine factor V and factor V-derived peptides with phospholipid vesicles. J. Biol. Chem. 258, 6503-6508
    • (1983) J. Biol. Chem , vol.258 , pp. 6503-6508
    • Higgins, D.L.1    Mann, K.G.2
  • 23
    • 0037166290 scopus 로고    scopus 로고
    • A model for the stoichiometric regulation of blood coagulation
    • Hockin, M. F., Jones, K. C., Everse, S. J. and Mann, K. G. (2002) A model for the stoichiometric regulation of blood coagulation. J. Biol. Chem. 277, 18322-18333
    • (2002) J. Biol. Chem , vol.277 , pp. 18322-18333
    • Hockin, M.F.1    Jones, K.C.2    Everse, S.J.3    Mann, K.G.4
  • 24
    • 0030843304 scopus 로고    scopus 로고
    • Activated protein C cleavage of factor Va leads to dissociation of the A2 domain
    • Mann, K. G., Hockin, M. F., Begin, K. J. and Kalafatis, M. (1997) Activated protein C cleavage of factor Va leads to dissociation of the A2 domain. J. Biol. Chem. 272, 20678-20683
    • (1997) J. Biol. Chem , vol.272 , pp. 20678-20683
    • Mann, K.G.1    Hockin, M.F.2    Begin, K.J.3    Kalafatis, M.4
  • 25
    • 0026337077 scopus 로고
    • The coagulation cascade: Initiation, maintenance, and regulation
    • Davie, E. W., Fujikawa, K. and Kisiel, W. (1991) The coagulation cascade: initiation, maintenance, and regulation. Biochemistry 30, 1030-1037
    • (1991) Biochemistry , vol.30 , pp. 1030-1037
    • Davie, E.W.1    Fujikawa, K.2    Kisiel, W.3
  • 27
    • 0037220079 scopus 로고    scopus 로고
    • Factor V: A combination of Dr Jekyll and Mr Hyde
    • Mann, K. G. and Kalafatis, M. (2003) Factor V: a combination of Dr Jekyll and Mr Hyde. Blood 101, 20-30
    • (2003) Blood , vol.101 , pp. 20-30
    • Mann, K.G.1    Kalafatis, M.2
  • 28
    • 0035964179 scopus 로고    scopus 로고
    • Metal ion-independent association of factor VIII subunits and the roles of calcium and copper ions for cofactor activity and inter-subunit affinity
    • Wakabayashi, H., Koszelak, M. E., Mastri, M. and Fay, P. J. (2001) Metal ion-independent association of factor VIII subunits and the roles of calcium and copper ions for cofactor activity and inter-subunit affinity. Biochemistry 40, 10293-10300
    • (2001) Biochemistry , vol.40 , pp. 10293-10300
    • Wakabayashi, H.1    Koszelak, M.E.2    Mastri, M.3    Fay, P.J.4
  • 31
    • 0026779133 scopus 로고
    • Characterization of the interaction between the heavy and light chains of bovine factor Va
    • Walker, F. J. (1992) Characterization of the interaction between the heavy and light chains of bovine factor Va. J. Biol. Chem. 267, 19896-19900
    • (1992) J. Biol. Chem , vol.267 , pp. 19896-19900
    • Walker, F.J.1
  • 32
    • 0031611747 scopus 로고    scopus 로고
    • Protein truncation test: Detection of severe haemophilia A mutation and analysis of factor VIII transcripts
    • Maugard, C., Tuffery, S., Aguilar-Martinez, R, Schved, J. F., Gris, J. C., Demaille, J. and Claustres, M. (1998) Protein truncation test: detection of severe haemophilia A mutation and analysis of factor VIII transcripts. Hum. Mutat. 11, 18-22
    • (1998) Hum. Mutat , vol.11 , pp. 18-22
    • Maugard, C.1    Tuffery, S.2    Aguilar-Martinez, R.3    Schved, J.F.4    Gris, J.C.5    Demaille, J.6    Claustres, M.7
  • 33
    • 34250727983 scopus 로고    scopus 로고
    • Factor VIII (FVIII) gene mutations in 120 patients with hemophilia A: Detection of 26 novel mutations and correlation with FVIII inhibitor development
    • Repesse, Y., Slaoui, M., Ferrandiz, D., Gautier, P., Costa, C., Costa, J. M., Lavergne, J. M. and Borel-Derlon, A. (2007) Factor VIII (FVIII) gene mutations in 120 patients with hemophilia A: detection of 26 novel mutations and correlation with FVIII inhibitor development. J. Thromb. Haemost. 5, 1476
    • (2007) J. Thromb. Haemost , vol.5 , pp. 1476
    • Repesse, Y.1    Slaoui, M.2    Ferrandiz, D.3    Gautier, P.4    Costa, C.5    Costa, J.M.6    Lavergne, J.M.7    Borel-Derlon, A.8
  • 34
    • 0034925129 scopus 로고    scopus 로고
    • Theophilus, B. D. M., Enayat, M. S.. Williams. M. D. and Hill, G. H. (2001) Site and type of mutations in the factor VIII gene in patients and carriers of Hemolphilia A, Haemophilia 7, 381-391
    • Theophilus, B. D. M., Enayat, M. S.. Williams. M. D. and Hill, G. H. (2001) Site and type of mutations in the factor VIII gene in patients and carriers of Hemolphilia A, Haemophilia 7, 381-391
  • 35
    • 0344142373 scopus 로고    scopus 로고
    • A domain mutations in 65 haemophilia A families and molecular modelling of dysfunctional factor VIII proteins
    • Liu, M. L., Murphy, M. E. P. and Thompson, A. R. (1998) A domain mutations in 65 haemophilia A families and molecular modelling of dysfunctional factor VIII proteins. Brit. J. Haematol. 103, 1051-1060
    • (1998) Brit. J. Haematol , vol.103 , pp. 1051-1060
    • Liu, M.L.1    Murphy, M.E.P.2    Thompson, A.R.3
  • 36
    • 0035254221 scopus 로고    scopus 로고
    • Hemophilia A mutations associated with 1-stage/ 2-stage activity discrepancy disrupt protein-protein interactions within the triplicated A domains of thrombin-activated factor VIIIa
    • Pipe, S. W., Saenko, E. L., Eickhorst, A. N., Kemball-Cook, G. and Kaufman, R. J. (2001) Hemophilia A mutations associated with 1-stage/ 2-stage activity discrepancy disrupt protein-protein interactions within the triplicated A domains of thrombin-activated factor VIIIa. Blood 97, 665-691
    • (2001) Blood , vol.97 , pp. 665-691
    • Pipe, S.W.1    Saenko, E.L.2    Eickhorst, A.N.3    Kemball-Cook, G.4    Kaufman, R.J.5
  • 37
    • 0036845615 scopus 로고    scopus 로고
    • Hemophilla A mutations within the factor VIII A2-A3 subunit interface destabilize factor VIIIa and cause one-stage/two-stage activity discrepancy
    • Hakeos, W. H., Miao, H., Sirachainan, N., Kemball-Cook, G., Saenko, E. L., Kaufman, R. J. and Pipe, S. W. (2002) Hemophilla A mutations within the factor VIII A2-A3 subunit interface destabilize factor VIIIa and cause one-stage/two-stage activity discrepancy. Thromb. Haemost. 88, 781-787
    • (2002) Thromb. Haemost , vol.88 , pp. 781-787
    • Hakeos, W.H.1    Miao, H.2    Sirachainan, N.3    Kemball-Cook, G.4    Saenko, E.L.5    Kaufman, R.J.6    Pipe, S.W.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.