메뉴 건너뛰기




Volumn 106, Issue 3, 1999, Pages 792-800

Substitution of Arg527 and Arg531 in factor VIII associated with mild haemophilia A: Characterization in terms of subunit interaction and cofactor function

Author keywords

Factor IXa binding; Factor VIII mutants; Factor VIIIa stability; Factor VIIIa factor IXa complex assembly; Haemophilia A

Indexed keywords

BLOOD CLOTTING FACTOR 8; BLOOD CLOTTING FACTOR 10;

EID: 0033192464     PISSN: 00071048     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2141.1999.01590.x     Document Type: Article
Times cited : (21)

References (33)
  • 1
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0022454539 scopus 로고
    • Proteolytic processing of human factor VIII
    • Eaton, D., Rodriguez, H. & Vehar, G.A. (1986) Proteolytic processing of human factor VIII. Biochemistry, 25, 505-512.
    • (1986) Biochemistry , vol.25 , pp. 505-512
    • Eaton, D.1    Rodriguez, H.2    Vehar, G.A.3
  • 4
    • 0027938728 scopus 로고
    • Factor VIIIa A2 subunit residues 558-565 represent a factor IXa interactive site
    • Fay, P.J., Beattie, T., Huggins, C.F. & Regan, L.M. (1994) Factor VIIIa A2 subunit residues 558-565 represent a factor IXa interactive site. Journal of Biological Chemistry, 269, 20522-20527.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 20522-20527
    • Fay, P.J.1    Beattie, T.2    Huggins, C.F.3    Regan, L.M.4
  • 5
    • 0009739073 scopus 로고    scopus 로고
    • Two mutations of the factor VIII (FVIII) gene, R527W and R531H, are identified in four unrelated haemophilia A patients with discrepancy in one-and two-stage assays of FVIII coagulant activity
    • abstract 223
    • Gaucher, C., Jorieux, S., Parquet-Gernez, A. & Mazurier, C. (1996) Two mutations of the factor VIII (FVIII) gene, R527W and R531H, are identified in four unrelated haemophilia A patients with discrepancy in one-and two-stage assays of FVIII coagulant activity. Haemophilia, 2, (Suppl. 1), 59, abstract 223.
    • (1996) Haemophilia , vol.2 , Issue.SUPPL. 1 , pp. 59
    • Gaucher, C.1    Jorieux, S.2    Parquet-Gernez, A.3    Mazurier, C.4
  • 6
    • 0022626746 scopus 로고
    • The production of a panel of ten murine monoclonal antibodies to human procoagulant factor VIII
    • Griffin, B.D., Micklem, L.R., McCann, M.C., James, K. & Pepper, D.S. (1986) The production of a panel of ten murine monoclonal antibodies to human procoagulant factor VIII. Thrombosis and Haemostasis, 55, 40-46.
    • (1986) Thrombosis and Haemostasis , vol.55 , pp. 40-46
    • Griffin, B.D.1    Micklem, L.R.2    McCann, M.C.3    James, K.4    Pepper, D.S.5
  • 8
    • 0023918719 scopus 로고
    • Synthesis, processing and secretion of recombinant human factor VIII expressed in mammalian cells
    • Kaufman, R.J., Wasley, L.C. & Dorner, A.J. (1988) Synthesis, processing and secretion of recombinant human factor VIII expressed in mammalian cells. Journal of Biological Chemistry, 263, 6352-6362.
    • (1988) Journal of Biological Chemistry , vol.263 , pp. 6352-6362
    • Kaufman, R.J.1    Wasley, L.C.2    Dorner, A.J.3
  • 9
    • 0031804517 scopus 로고    scopus 로고
    • The factor VIII structure and mutation resource site: HAMSTeRS version 4
    • Kemball-Cook, G., Tuddenham, E.G.D. & Wacey, A.I. (1998) The factor VIII structure and mutation resource site: HAMSTeRS version 4. Nucleic Acids Research, 26, 216-219.
    • (1998) Nucleic Acids Research , vol.26 , pp. 216-219
    • Kemball-Cook, G.1    Tuddenham, E.G.D.2    Wacey, A.I.3
  • 10
    • 0031027575 scopus 로고    scopus 로고
    • Localization of a factor X interactive site in the A1 subunit of factor VIIIa
    • Lapan, K.A. & Fay, P.J. (1997) Localization of a factor X interactive site in the A1 subunit of factor VIIIa. Journal of Biological Chemistry, 272, 2082-2088.
    • (1997) Journal of Biological Chemistry , vol.272 , pp. 2082-2088
    • Lapan, K.A.1    Fay, P.J.2
  • 11
    • 0028239173 scopus 로고
    • Identification of a binding site for blood coagulation factor IXa on the light chain of human factor VIII
    • Lenting, P.J., Donath, M.J.S.H., van Mourik, J.A. & Mertens, K. (1994) Identification of a binding site for blood coagulation factor IXa on the light chain of human factor VIII. Journal of Biological Chemistry, 269, 7150-7155.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 7150-7155
    • Lenting, P.J.1    Donath, M.J.S.H.2    Van Mourik, J.A.3    Mertens, K.4
  • 14
    • 0032402122 scopus 로고    scopus 로고
    • The life cycle of coagulation factor VIII in view of its structure and function
    • Lenting, P.J., van Mourik, J.A. & Mertens, K. (1998) The life cycle of coagulation factor VIII in view of its structure and function. Blood, 92, 3983-3996.
    • (1998) Blood , vol.92 , pp. 3983-3996
    • Lenting, P.J.1    Van Mourik, J.A.2    Mertens, K.3
  • 16
    • 0025866980 scopus 로고
    • Structural basis for the decreased procoagulant activity of human FVIII compared to the porcine homolog
    • Lollar, P. & Parker, E.T. (1991) Structural basis for the decreased procoagulant activity of human FVIII compared to the porcine homolog. Journal of Biological Chemistry, 266, 12481-12486.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 12481-12486
    • Lollar, P.1    Parker, E.T.2
  • 18
    • 0020048708 scopus 로고
    • Activation of human coagulation factor VIII by activated factor X, the common product of the intrinsic and the extrinsic pathway of blood coagulation
    • Mertens, K. & Bertina, R.M. (1982) Activation of human coagulation factor VIII by activated factor X, the common product of the intrinsic and the extrinsic pathway of blood coagulation. Thrombosis and Haemostasis, 47, 96-100.
    • (1982) Thrombosis and Haemostasis , vol.47 , pp. 96-100
    • Mertens, K.1    Bertina, R.M.2
  • 20
    • 0022354412 scopus 로고
    • The role of factor VIII in the activation of human blood coagulation factor X by activated factor IX
    • Mertens, K., van Wijngaarden, A. & Bertina, R.M. (1985a) The role of factor VIII in the activation of human blood coagulation factor X by activated factor IX. Thrombosis and Haemostasis, 54, 654-660.
    • (1985) Thrombosis and Haemostasis , vol.54 , pp. 654-660
    • Mertens, K.1    Van Wijngaarden, A.2    Bertina, R.M.3
  • 21
    • 0022358562 scopus 로고
    • The functional defect of factor VIII leiden, a genetic variant of coagulation factor VIII
    • Mertens, K., van Wijngaarden, A., Bertina, R.M. & Veltkamp, J.J. (1985b) The functional defect of factor VIII Leiden, a genetic variant of coagulation factor VIII. Thrombosis and Haemostasis, 54, 650-653.
    • (1985) Thrombosis and Haemostasis , vol.54 , pp. 650-653
    • Mertens, K.1    Van Wijngaarden, A.2    Bertina, R.M.3    Veltkamp, J.J.4
  • 22
    • 0025055279 scopus 로고
    • The use of acetylated factor X to prevent feedback activation of factor VIII during factor X activation: A tool for kinetic studies
    • Neuenschwander, P. & Jesty, J. (1990) The use of acetylated factor X to prevent feedback activation of factor VIII during factor X activation: a tool for kinetic studies. Analytical Biochemistry, 184, 347-352.
    • (1990) Analytical Biochemistry , vol.184 , pp. 347-352
    • Neuenschwander, P.1    Jesty, J.2
  • 23
    • 0030832791 scopus 로고    scopus 로고
    • Interacting regions in the A1 and A2 subunits of factor VIIIa identified by zero-length cross-linking
    • O'Brien, L.M., Huggins, C.F. & Fay, P.J. (1997) Interacting regions in the A1 and A2 subunits of factor VIIIa identified by zero-length cross-linking. Blood, 90, 3943-3950.
    • (1997) Blood , vol.90 , pp. 3943-3950
    • O'Brien, L.M.1    Huggins, C.F.2    Fay, P.J.3
  • 24
    • 0030903424 scopus 로고    scopus 로고
    • A molecular model for the triplicated a domains of human factor VIII based on the crystal structure of human caeruloplasmin
    • Pemberton, S., Lindley, P., Zaitsev, V., Card, G., Tuddenham, E.G.D. & Kemball-Cook, G. (1997) A molecular model for the triplicated A domains of human factor VIII based on the crystal structure of human caeruloplasmin. Blood, 89, 2413-2421.
    • (1997) Blood , vol.89 , pp. 2413-2421
    • Pemberton, S.1    Lindley, P.2    Zaitsev, V.3    Card, G.4    Tuddenham, E.G.D.5    Kemball-Cook, G.6
  • 25
    • 0028849679 scopus 로고
    • 2+ concentration, heparin, and activated protein C-catalyzed proteolysis
    • 2+ concentration, heparin, and activated protein C-catalyzed proteolysis. Biochemistry, 34, 12775-12781.
    • (1995) Biochemistry , vol.34 , pp. 12775-12781
    • Persson, E.1    Ezban, M.2    Shymko, R.M.3
  • 26
    • 0032932325 scopus 로고    scopus 로고
    • Mild hemophilia A caused by increased rate of factor VIII A2 subunit dissociation: Evidence for non-proteolytic inactivation of FVIIIa in vivo
    • Pipe, S.W., Eickenhorst, A.N., McKinley, S.H., Saenko, E.L. & Kaufman, R.J. (1999) Mild hemophilia A caused by increased rate of factor VIII A2 subunit dissociation: evidence for non-proteolytic inactivation of FVIIIa in vivo. Blood, 93, 176-183.
    • (1999) Blood , vol.93 , pp. 176-183
    • Pipe, S.W.1    Eickenhorst, A.N.2    McKinley, S.H.3    Saenko, E.L.4    Kaufman, R.J.5
  • 27
    • 0029886287 scopus 로고    scopus 로고
    • Mutations in a subgroup of patients with mild haemophilia A and familial discrepancy between one-stage and two-stage factor VIII:C methods
    • Rudzki, Z., Duncan, E.M., Casey, G.J., Neumann, M., Favaloro, E.J. & Lloyd, J.V. (1996) Mutations in a subgroup of patients with mild haemophilia A and familial discrepancy between one-stage and two-stage factor VIII:C methods. British Journal of Haematology, 94, 400-406.
    • (1996) British Journal of Haematology , vol.94 , pp. 400-406
    • Rudzki, Z.1    Duncan, E.M.2    Casey, G.J.3    Neumann, M.4    Favaloro, E.J.5    Lloyd, J.V.6
  • 29
    • 0021249145 scopus 로고
    • Characterisation of 25 monoclonal antibodies to factor VIII-von Willebrand factor: Relationship between ristocetin-induced platelet aggregation and platelet adherence to subendothelium
    • Stel, H.V., Sakariassen, K.S., Scholte, B.J., Veerman, E.C.I., van der Kwast, T.H., de Groot, P.G., Sixma, J.J. & van Mourik, J.A. (1984) Characterisation of 25 monoclonal antibodies to factor VIII-von Willebrand factor: relationship between ristocetin-induced platelet aggregation and platelet adherence to subendothelium. Blood, 163, 1408-1415.
    • (1984) Blood , vol.163 , pp. 1408-1415
    • Stel, H.V.1    Sakariassen, K.S.2    Scholte, B.J.3    Veerman, E.C.I.4    Van Der Kwast, T.H.5    De Groot, P.G.6    Sixma, J.J.7    Van Mourik, J.A.8
  • 30
    • 0003136888 scopus 로고
    • Mutagenesis by PCR
    • ed. by H. G. Griffin and A. M. Griffin, CRC Press, Boca Raton
    • Tao, B.Y. & Lee, K.C.P. (1994) Mutagenesis by PCR. PCR Technology: Current Innovations (ed. by H. G. Griffin and A. M. Griffin), pp. 71-72. CRC Press, Boca Raton.
    • (1994) PCR Technology: Current Innovations , pp. 71-72
    • Tao, B.Y.1    Lee, K.C.P.2
  • 32
    • 0019831499 scopus 로고
    • The role of phospholipid and factor VIIIa in the activation of bovine factor X
    • Van Dieijen, G., Tans, G., Rosing, J. & Hemker, H.C. (1981) The role of phospholipid and factor VIIIa in the activation of bovine factor X. Journal of Biological Chemistry, 256, 3433-3442.
    • (1981) Journal of Biological Chemistry , vol.256 , pp. 3433-3442
    • Van Dieijen, G.1    Tans, G.2    Rosing, J.3    Hemker, H.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.