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Volumn 5, Issue 5, 2007, Pages 996-1001

A3 domain residue Glu1829 contributes to A2 subunit retention in factor VIIIa

Author keywords

Factor IXa; Factor VIII; Factor VIIIa subunits; Factor Xa generation; Factor Xase; Subunit dissociation

Indexed keywords

ALANINE; BLOOD CLOTTING FACTOR 8A; GLUTAMIC ACID;

EID: 34247857684     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1111/j.1538-7836.2007.02458.x     Document Type: Article
Times cited : (3)

References (37)
  • 1
    • 0029086642 scopus 로고
    • Biochemical and molecular aspects of the coagulation cascade
    • Davie EW. Biochemical and molecular aspects of the coagulation cascade. Thromb Haemost 1995; 74: 1-6.
    • (1995) Thromb Haemost , vol.74 , pp. 1-6
    • Davie, E.W.1
  • 2
    • 0029550056 scopus 로고
    • Structure and function of Factor VIII
    • Lollar P. Structure and function of Factor VIII. Adv Exp Med Biol 1995; 386: 3-17.
    • (1995) Adv Exp Med Biol , vol.386 , pp. 3-17
    • Lollar, P.1
  • 6
    • 0020043657 scopus 로고
    • Monoclonal antibodies to porcine factor VIII coagulant and their use in the isolation of active coagulant protein
    • Fass DN, Knutson GJ, Katzmann JA. Monoclonal antibodies to porcine factor VIII coagulant and their use in the isolation of active coagulant protein. Blood 1982; 59: 594-600.
    • (1982) Blood , vol.59 , pp. 594-600
    • Fass, D.N.1    Knutson, G.J.2    Katzmann, J.A.3
  • 8
    • 0022445266 scopus 로고
    • The size of human factor VIII heterodimers and the effects produced by thrombin
    • Fay PJ, Anderson MT, Chavin SI, Marder VJ. The size of human factor VIII heterodimers and the effects produced by thrombin. Biochim Biophys Acta 1986; 871: 268-78.
    • (1986) Biochim Biophys Acta , vol.871 , pp. 268-278
    • Fay, P.J.1    Anderson, M.T.2    Chavin, S.I.3    Marder, V.J.4
  • 9
    • 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: 505-12.
    • (1986) Biochemistry , vol.25 , pp. 505-512
    • Eaton, D.1    Rodriguez, H.2    Vehar, G.A.3
  • 10
    • 0025923490 scopus 로고
    • Human factor VIIIa subunit structure. Reconstruction of factor VIIIa from the isolated A1/A3-C1-C2 dimer and A2 subunit
    • Fay PJ, Haidaris PJ, Smudzin TM. Human factor VIIIa subunit structure. Reconstruction of factor VIIIa from the isolated A1/A3-C1-C2 dimer and A2 subunit. J Biol Chem 1991; 266: 8957-62.
    • (1991) J Biol Chem , vol.266 , pp. 8957-8962
    • Fay, P.J.1    Haidaris, P.J.2    Smudzin, T.M.3
  • 11
    • 0025101070 scopus 로고
    • pH-dependent denaturation of thrombin-activated porcine factor VIII
    • Lollar P, Parker CG. pH-dependent denaturation of thrombin-activated porcine factor VIII. J Biol Chem 1990; 265: 1688-92.
    • (1990) J Biol Chem , vol.265 , pp. 1688-1692
    • Lollar, P.1    Parker, C.G.2
  • 12
    • 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. 1966-19671
    • Gale, A.J.1    Pellequer, J.L.2
  • 13
    • 0030664471 scopus 로고    scopus 로고
    • Characterization of a genetically engineered inactivation-resistant coagulation factor VIIIa
    • Pipe SW, Kaufman RJ. Characterization of a genetically engineered inactivation-resistant coagulation factor VIIIa. Proc Natl Acad Sci U S A 1997; 94: 11851-6.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 11851-11856
    • Pipe, S.W.1    Kaufman, R.J.2
  • 14
    • 0032932325 scopus 로고    scopus 로고
    • Mild hemophilia A caused by increased rate of factor VIII A2 subunit dissociation: Evidence for nonproteolytic inactivation of factor VIIIa in vivo
    • Pipe SW, Eickhorst AN, McKinley SH, Saenko EL, Kaufman RJ. Mild hemophilia A caused by increased rate of factor VIII A2 subunit dissociation: Evidence for nonproteolytic inactivation of factor VIIIa in vivo. Blood 1999; 93: 176-83.
    • (1999) Blood , vol.93 , pp. 176-183
    • Pipe, S.W.1    Eickhorst, A.N.2    McKinley, S.H.3    Saenko, E.L.4    Kaufman, R.J.5
  • 15
    • 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 SW, Saenko EL, Eickhorst AN, Kemball-Cook G, Kaufman RJ. 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 2001; 97: 685-91.
    • (2001) Blood , vol.97 , pp. 685-691
    • Pipe, S.W.1    Saenko, E.L.2    Eickhorst, A.N.3    Kemball-Cook, G.4    Kaufman, R.J.5
  • 16
    • 0036845615 scopus 로고    scopus 로고
    • Hemophilia A mutations within the factor VIII A2-A3 subunit interface destabilize factor VIIIa and cause one-stage/two-stage activity discrepancy
    • Hakeos WH, Miao H, Sirachainan N, Kemball-Cook G, Saenko EL, Kaufman RJ, Pipe SW. Hemophilia A mutations within the factor VIII A2-A3 subunit interface destabilize factor VIIIa and cause one-stage/two-stage activity discrepancy. Thromb Haemost 2002; 88: 781-7.
    • (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
  • 17
    • 0024316693 scopus 로고
    • Intersubunit fluorescence energy transfer in human factor VIII
    • Fay PJ, Smudzin TM. Intersubunit fluorescence energy transfer in human factor VIII. J Biol Chem 1989; 264: 14005-10.
    • (1989) J Biol Chem , vol.264 , pp. 14005-14010
    • Fay, P.J.1    Smudzin, T.M.2
  • 18
    • 0023918416 scopus 로고
    • Reconstitution of human factor VIII from isolated subunits
    • Fay PJ. Reconstitution of human factor VIII from isolated subunits. Arch Biochem Biophys 1988; 262: 525-31.
    • (1988) Arch Biochem Biophys , vol.262 , pp. 525-531
    • Fay, P.J.1
  • 19
    • 0023864433 scopus 로고
    • Generation of active coagulation factor VIII from isolated subunits
    • Nordfang O, Ezban M. Generation of active coagulation factor VIII from isolated subunits. J Biol Chem 1988; 263: 1115-8.
    • (1988) J Biol Chem , vol.263 , pp. 1115-1158
    • Nordfang, O.1    Ezban, M.2
  • 20
    • 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 ME, Mastri M, Fay PJ. Metal ion-independent association of factor VIII subunits and the roles of calcium and copper ions for cofactor activity and inter-subunit affinity. Biochemistry 2001; 40: 10293-300.
    • (2001) Biochemistry , vol.40 , pp. 10293-10300
    • Wakabayashi, H.1    Koszelak, M.E.2    Mastri, M.3    Fay, P.J.4
  • 21
    • 1842581996 scopus 로고    scopus 로고
    • Residues 110-126 in the A1 domain of factor VIII contain a Ca2+-binding site required for cofactor activity
    • Wakabayashi H, Freas J, Zhou Q, Fay PJ. Residues 110-126 in the A1 domain of factor VIII contain a Ca2+-binding site required for cofactor activity. J Biol Chem 2004; 279: 12677-84.
    • (2004) J Biol Chem , vol.279 , pp. 12677-12684
    • Wakabayashi, H.1    Freas, J.2    Zhou, Q.3    Fay, P.J.4
  • 22
    • 0019883158 scopus 로고
    • Phospholipid vesicle formation and transmembrane protein incorporation using octyl glucoside
    • Mimms LT, Zampighi G, Nozaki Y, Tanford C, Reynolds JA. Phospholipid vesicle formation and transmembrane protein incorporation using octyl glucoside. Biochemistry 1981; 20: 833-40.
    • (1981) Biochemistry , vol.20 , pp. 833-840
    • Mimms, L.T.1    Zampighi, G.2    Nozaki, Y.3    Tanford, C.4    Reynolds, J.A.5
  • 23
    • 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, Wakabayashi H. Cleavage of factor VIII heavy chain is required for the functional interaction of a2 subunit with factor IXA. J Biol Chem 2001; 276: 12434-9.
    • (2001) J Biol Chem , vol.276 , pp. 12434-12439
    • Fay, P.J.1    Mastri, M.2    Koszelak, M.E.3    Wakabayashi, H.4
  • 24
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72: 248-54.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 25
    • 23044498602 scopus 로고    scopus 로고
    • A Glu113Ala mutation within a factor VIII Ca(2 +)-binding site enhances cofactor interactions in factor Xase
    • Wakabayashi H, Su YC, Ahmad SS, Walsh PN, Fay PJ. A Glu113Ala mutation within a factor VIII Ca(2 +)-binding site enhances cofactor interactions in factor Xase. Biochemistry 2005; 44: 10298-304.
    • (2005) Biochemistry , vol.44 , pp. 10298-10304
    • Wakabayashi, H.1    Su, Y.C.2    Ahmad, S.S.3    Walsh, P.N.4    Fay, P.J.5
  • 26
    • 0021752980 scopus 로고
    • Methodology of the one-stage assay of Factor VIII (VIII:C)
    • Over J. Methodology of the one-stage assay of Factor VIII (VIII:C). Scand J Haematol Suppl 1984; 41: 13-24.
    • (1984) Scand J Haematol Suppl , vol.41 , pp. 13-24
    • Over, J.1
  • 28
    • 0037007964 scopus 로고    scopus 로고
    • Ca(2 +) binding to both the heavy and light chains of factor VIII is required for cofactor activity
    • Wakabayashi H, Schmidt KM, Fay PJ. Ca(2 +) binding to both the heavy and light chains of factor VIII is required for cofactor activity. Biochemistry 2002; 41: 8485-92.
    • (2002) Biochemistry , vol.41 , pp. 8485-8492
    • Wakabayashi, H.1    Schmidt, K.M.2    Fay, P.J.3
  • 29
    • 0021252593 scopus 로고
    • Stabilization of thrombin-activated porcine factor VIII:C by factor IXa phospholipid
    • Lollar P, Knutson GJ, Fass DN. Stabilization of thrombin-activated porcine factor VIII:C by factor IXa phospholipid. Blood 1984; 63: 1303-8.
    • (1984) Blood , vol.63 , pp. 1303-1308
    • Lollar, P.1    Knutson, G.J.2    Fass, D.N.3
  • 30
    • 0026784526 scopus 로고
    • Factor IXa enhances reconstitution of factor VIIIa from isolated A2 subunit and A1/A3-C1-C2 dimer
    • Lamphear BJ, Fay PJ. Factor IXa enhances reconstitution of factor VIIIa from isolated A2 subunit and A1/A3-C1-C2 dimer. J Biol Chem 1992; 267: 3725-30.
    • (1992) J Biol Chem , vol.267 , pp. 3725-3730
    • Lamphear, B.J.1    Fay, P.J.2
  • 31
    • 0029919613 scopus 로고    scopus 로고
    • Model for the factor VIIIa-dependent decay of the intrinsic factor Xase. Role of subunit dissociation and factor IXa-catalyzed proteolysis
    • Fay PJ, Beattie TL, Regan LM, O'Brien LM, Kaufman RJ. Model for the factor VIIIa-dependent decay of the intrinsic factor Xase. Role of subunit dissociation and factor IXa-catalyzed proteolysis. J Biol Chem 1996; 271: 6027-32.
    • (1996) J Biol Chem , vol.271 , pp. 6027-6032
    • Fay, P.J.1    Beattie, T.L.2    Regan, L.M.3    O'Brien, L.M.4    Kaufman, R.J.5
  • 32
    • 0031804517 scopus 로고    scopus 로고
    • The factor VIII structure and mutation resource site: HAMSTeRS version 4
    • Kemball-Cook G, Tuddenham EG, Wacey AI. The factor VIII structure and mutation resource site: HAMSTeRS version 4. Nucleic Acids Res 1998; 26: 216-9.
    • (1998) Nucleic Acids Res , vol.26 , pp. 216-219
    • Kemball-Cook, G.1    Tuddenham, E.G.2    Wacey, A.I.3
  • 33
    • 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, Fay PJ. Altered interactions between the A1 and A2 subunits of factor VIIIa following cleavage of A1 subunit by factor Xa. J Biol Chem 2003; 278: 1634-41.
    • (2003) J Biol Chem , vol.278 , pp. 1634-1641
    • Nogami, K.1    Wakabayashi, H.2    Schmidt, K.3    Fay, P.J.4
  • 34
    • 4344614078 scopus 로고    scopus 로고
    • Localization of a pH-dependent, A2 subunit-interactive surface within the factor VIIIa A1 subunit
    • Nogami K, Wakabayashi H, Ansong C, Fay PJ. Localization of a pH-dependent, A2 subunit-interactive surface within the factor VIIIa A1 subunit. Biochim Biophys Acta 2004; 1701: 25-35.
    • (2004) Biochim Biophys Acta , vol.1701 , pp. 25-35
    • Nogami, K.1    Wakabayashi, H.2    Ansong, C.3    Fay, P.J.4
  • 35
    • 33744919584 scopus 로고    scopus 로고
    • A1 subunit-mediated regulation of thrombin-activated factor VIII A2 subunit dissociation
    • Parker ET, Doering CB, Lollar P. A1 subunit-mediated regulation of thrombin-activated factor VIII A2 subunit dissociation. J Biol Chem 2006; 281: 13922-30.
    • (2006) J Biol Chem , vol.281 , pp. 13922-13930
    • Parker, E.T.1    Doering, C.B.2    Lollar, P.3
  • 36
    • 0026708655 scopus 로고
    • Characterization of the interaction between the A2 subunit and A1/ A3-C1-C2 dimer in human factor VIIIa
    • Fay PJ, Smudzin TM. Characterization of the interaction between the A2 subunit and A1/A3-C1-C2 dimer in human factor VIIIa. J Biol Chem 1992; 267: 13246-50.
    • (1992) J Biol Chem , vol.267 , pp. 13246-13250
    • Fay, P.J.1    Smudzin, T.M.2
  • 37
    • 0030903424 scopus 로고    scopus 로고
    • A molecular model for the triplicated A domains of human factor VIII based on the crystal structure of human ceruloplasmin
    • Pemberton S, Lindley P, Zaitsev V, Card G, Tuddenham EG, Kemball-Cook G. A molecular model for the triplicated A domains of human factor VIII based on the crystal structure of human ceruloplasmin. Blood 1997; 89: 2413-21.
    • (1997) Blood , vol.89 , pp. 2413-2421
    • Pemberton, S.1    Lindley, P.2    Zaitsev, V.3    Card, G.4    Tuddenham, E.G.5    Kemball-Cook, G.6


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