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Volumn 287, Issue 45, 2012, Pages 38200-38209

A sequential mechanism for exosite-mediated factor IX activation by factor XIa

Author keywords

[No Author keywords available]

Indexed keywords

DATA SUPPORT; SEQUENTIAL MECHANISM; SUBSTRATE BINDING;

EID: 84868325413     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.376343     Document Type: Article
Times cited : (28)

References (38)
  • 1
    • 84855844168 scopus 로고    scopus 로고
    • (Hoffman, R., Benz, E. J., Shattil, S. J., Furie, B., Silberstein, L. E., McGlave, P., and Heslop, H., eds) 5th Ed. Churchill Livingstone-Elsevier, Philadelphia, PA
    • Roth, D. A., Freeman, S. J., and Furie, B. (2009) in Hematology: Basic Principles and Practice (Hoffman, R., Benz, E. J., Shattil, S. J., Furie, B., Silberstein, L. E., McGlave, P., and Heslop, H., eds) 5th Ed., pp. 1899-1910, Churchill Livingstone-Elsevier, Philadelphia, PA
    • (2009) Hematology: Basic Principles and Practice , pp. 1899-1910
    • Roth, D.A.1    Freeman, S.J.2    Furie, B.3
  • 2
    • 34247158056 scopus 로고    scopus 로고
    • (Colman, R. W., Marder, V. J., Clowes, A. W., George, J. N., and Goldhaber, S. Z., eds) 5th Ed Lippincott, Williams & Wilkins, Philadelphia, PA
    • Bajaj, S. P., and Thompson, A. R. (2006) in Hemostasis and Thrombosis: Basic Principles and Clinical Practice (Colman, R. W., Marder, V. J., Clowes, A. W., George, J. N., and Goldhaber, S. Z., eds) 5th Ed., pp. 131-150, Lippincott, Williams & Wilkins, Philadelphia, PA
    • (2006) Hemostasis and Thrombosis: Basic Principles and Clinical Practice , pp. 131-150
    • Bajaj, S.P.1    Thompson, A.R.2
  • 3
    • 64249133477 scopus 로고    scopus 로고
    • (Hoffman, R., Benz, E. J., Shattil, S. J., Furie, B., Silberstein, L. E., McGlave, P., and Heslop, H., eds) 5th Ed. Churchill Livingstone-Elsevier, Philadelphia, PA
    • Furie, B., and Furie, B. C. (2009) Hematology: Basic Principles and Practice (Hoffman, R., Benz, E. J., Shattil, S. J., Furie, B., Silberstein, L. E., McGlave, P., and Heslop, H., eds) 5th Ed., pp. 1819-1836, Churchill Livingstone- Elsevier, Philadelphia, PA
    • (2009) Hematology: Basic Principles and Practice , pp. 1819-1836
    • Furie, B.1    Furie, B.C.2
  • 4
    • 0018170804 scopus 로고
    • Activation of bovine factor IX (Christmas factor) by factor XIa (activated plasma thromboplastin antecedent) and a protease from Russell's viper venom
    • Lindquist, P. A., Fujikawa, K., and Davie, E. W. (1978) Activation of bovine factor IX (Christmas factor) by factor XIa (activated plasma thromboplastin antecedent) and a protease from Russell's viper venom. J. Biol. Chem. 253, 1902-1909 (Pubitemid 8299515)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.6 , pp. 1902-1909
    • Lindquist, P.A.1    Fujikawa, K.2    Davie, E.W.3
  • 5
    • 67949112120 scopus 로고    scopus 로고
    • Update on the physiology and pathology of factor IX activation by factor XIa
    • Smith, S. B., and Gailani, D. (2008) Update on the physiology and pathology of factor IX activation by factor XIa. Expert Rev. Hematol. 1, 87-98
    • (2008) Expert Rev. Hematol. , vol.1 , pp. 87-98
    • Smith, S.B.1    Gailani, D.2
  • 6
    • 0018938967 scopus 로고
    • Kinetics of Factor IX activation via the extrinsic pathway. Dependence of K(m) on tissue factor
    • Zur, M., and Nemerson, Y. (1980) Kinetics of factor IX activation via the extrinsic pathway. Dependence of Km on tissue factor. J. Biol. Chem. 255, 5703-5707 (Pubitemid 10023591)
    • (1980) Journal of Biological Chemistry , vol.255 , Issue.12 , pp. 5703-5707
    • Zur, M.1    Nemerson, Y.2
  • 7
    • 0026752675 scopus 로고
    • The tissue factor pathway of blood coagulation
    • Nemerson, Y. (1992) The tissue factor pathway of blood coagulation. Semin. Hematol. 29, 170-176
    • (1992) Semin. Hematol. , vol.29 , pp. 170-176
    • Nemerson, Y.1
  • 8
    • 0025772165 scopus 로고
    • Cooperative activation of human factor IX by the human extrinsic pathway of blood coagulation
    • Lawson, J. H., and Mann, K. G. (1991) Cooperative activation of human factor IX by the human extrinsic pathway of blood coagulation. J. Biol. Chem. 266, 11317-11327 (Pubitemid 21906949)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.17 , pp. 11317-11327
    • Lawson, J.H.1    Mann, K.G.2
  • 9
    • 0017740353 scopus 로고
    • Human blood coagulation factor XI. Purification, properties, and mechanism of activation by activated factor XII
    • Bouma, B. N., and Griffin, J. H. (1977) Human blood coagulation factor XI. Purification, properties, and mechanisms of activated factor XII. J. Biol. Chem. 252, 6432-6437 (Pubitemid 8193790)
    • (1977) Journal of Biological Chemistry , vol.252 , Issue.18 , pp. 6432-6437
    • Bouma, B.N.1    Griffin, J.H.2
  • 10
    • 0023043178 scopus 로고
    • Amino acid sequence of human factor XI, a blood coagulation factor with four tandem repeats that are highly homologous with plasma prekallikrein
    • Fujikawa, K., Chung, D. W., Hendrickson, L. E., and Davie, E. W. (1986) Amino acid sequence of human factor XI, a blood coagulation factor with four tandem repeats that are highly homologous with plasma prekallikrein. Biochemistry 25, 2417-2424
    • (1986) Biochemistry , vol.25 , pp. 2417-2424
    • Fujikawa, K.1    Chung, D.W.2    Hendrickson, L.E.3    Davie, E.W.4
  • 11
    • 0025975587 scopus 로고
    • Location of the disulfide bonds in human coagulation factor XI. The presence of tandem apple domains
    • McMullen, B. A., Fujikawa, K., and Davie, E. W. (1991) Location of the disulfide bonds in human coagulation factor XI. The presence of tandem apple domains. Biochemistry 30, 2056-2060
    • (1991) Biochemistry , vol.30 , pp. 2056-2060
    • McMullen, B.A.1    Fujikawa, K.2    Davie, E.W.3
  • 12
    • 33744927154 scopus 로고    scopus 로고
    • Crystal structure of the factor XI zymogen reveals a pathway for transactivation
    • DOI 10.1038/nsmb1095, PII N1095
    • Papagrigoriou, E., McEwan, P. A., Walsh, P. N., and Emsley, J. (2006) Crystal structure of the factor XI zymogen reveals a pathway for transactivation. Nat. Struct. Mol. Biol. 13, 557-558 (Pubitemid 43848912)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.6 , pp. 557-558
    • Papagrigoriou, E.1    McEwan, P.A.2    Walsh, P.N.3    Emsley, J.4
  • 13
    • 0030899507 scopus 로고    scopus 로고
    • Factor IX activation by factor XIa proceeds without release of a free intermediate
    • DOI 10.1021/bi962274y
    • Wolberg, A. S., Morris, D. P., and Stafford, D. W. (1997) Factor IX activation by factor XIa proceeds without release of a free intermediate. Biochemistry 36, 4074-4079 (Pubitemid 27171578)
    • (1997) Biochemistry , vol.36 , Issue.14 , pp. 4074-4079
    • Wolberg, A.S.1    Morris, D.P.2    Stafford, D.W.3
  • 14
    • 43749120294 scopus 로고    scopus 로고
    • Characterization of novel forms of coagulation factor XIa. Independence of factor XIa subunits in factor IX activation
    • Smith, S. B., Verhamme, I. M., Sun, M. F., Bock, P. E., and Gailani, D. (2008) Characterization of novel forms of coagulation factor XIa. Independence of factor XIa subunits in factor IX activation. J. Biol. Chem. 283, 6696-6705
    • (2008) J. Biol. Chem. , vol.283 , pp. 6696-6705
    • Smith, S.B.1    Verhamme, I.M.2    Sun, M.F.3    Bock, P.E.4    Gailani, D.5
  • 15
    • 49649099783 scopus 로고    scopus 로고
    • Factor XI homodimer structure is essential for normal proteolytic activation by factor XIIa, thrombin, and factor XIa
    • Wu, W., Sinha, D., Shikov, S., Yip, C. K., Walz, T., Billings, P. C., Lear, J. D., and Walsh, P. N. (2008) Factor XI homodimer structure is essential for normal proteolytic activation by factor XIIa, thrombin, and factor XIa. J. Biol. Chem. 283, 18655-18664
    • (2008) J. Biol. Chem. , vol.283 , pp. 18655-18664
    • Wu, W.1    Sinha, D.2    Shikov, S.3    Yip, C.K.4    Walz, T.5    Billings, P.C.6    Lear, J.D.7    Walsh, P.N.8
  • 16
    • 11144229671 scopus 로고    scopus 로고
    • Binding of substrate in two conformations to human prothrombinase drives consecutive cleavage at two sites in prothrombin
    • DOI 10.1074/jbc.M410866200
    • Orcutt, S. J., and Krishnaswamy, S. (2004) Binding of substrate in two conformations to human prothrombinase drives consecutive cleavage at two sites in prothrombin. J. Biol. Chem. 279, 54927-54936 (Pubitemid 40053239)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.52 , pp. 54927-54936
    • Orcutt, S.J.1    Krishnaswamy, S.2
  • 17
    • 34548274439 scopus 로고    scopus 로고
    • Macromolecular substrate-binding exosites on both the heavy and light chains of factor XIa mediate the formation of the Michaelis complex required for factor IX-activation
    • DOI 10.1021/bi062296c
    • Sinha, D., Marcinkiewicz, M., Navaneetham, D., and Walsh, P. N. (2007) Macromolecular substrate-binding exosites on both the heavy and light chains of factor XIa mediate the formation of the Michaelis complex required for factor IX activation. Biochemistry 46, 9830-9839 (Pubitemid 47328589)
    • (2007) Biochemistry , vol.46 , Issue.34 , pp. 9830-9839
    • Sinha, D.1    Marcinkiewicz, M.2    Navaneetham, D.3    Walsh, P.N.4
  • 18
    • 21244476861 scopus 로고    scopus 로고
    • Exosite-mediated substrate recognition of factor IX by factor XIa: The factor XIa heavy chain is required for initial recognition of factor IX
    • DOI 10.1074/jbc.M500894200
    • Ogawa, T., Verhamme, I. M., Sun, M. F., Bock, P. E., and Gailani, D. (2005) Exosite-mediated substrate recognition of factor IX by factor XIa. The factor XIa heavy chain is required for initial recognition of factor IX. J. Biol. Chem. 280, 23523-23530 (Pubitemid 40884830)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.25 , pp. 23523-23530
    • Ogawa, T.1    Verhamme, I.M.2    Sun, M.-F.3    Bock, P.E.4    Gailani, D.5
  • 19
    • 0023198922 scopus 로고
    • Role of calcium ions and the heavy chain of factor XIa in the activation of human coagulation factor IX
    • Sinha, D., Seaman, F. S., and Walsh, P. N. (1987) Role of calcium ions and the heavy chain of factor XIa in the activation of human coagulation factor IX. Biochemistry 26, 3768-3775 (Pubitemid 17127449)
    • (1987) Biochemistry , vol.26 , Issue.13 , pp. 3768-3775
    • Sinha, D.1    Seaman, F.S.2    Walsh, P.N.3
  • 20
    • 0024360044 scopus 로고
    • Functional domains in the heavy-chain region of factor XI: A high molecular weight kininogen-binding site and a substrate-binding site for factor IX
    • Baglia, F. A., Sinha, D., and Walsh, P. N. (1989) Functional domains in the heavy-chain region of factor XI. A high molecular weight kininogen-binding site and a substrate-binding site for factor IX. Blood 74, 244-251 (Pubitemid 19187436)
    • (1989) Blood , vol.74 , Issue.1 , pp. 244-251
    • Baglia, F.A.1    Sinha, D.2    Walsh, P.N.3
  • 21
    • 0026354477 scopus 로고
    • Identification and chemical synthesis of a substrate-binding site for factor IX on coagulation factor XIa
    • Baglia, F. A., Jameson, B. A., and Walsh, P. N. (1991) Identification and chemical synthesis of a substrate-binding site for factor IX on coagulation factor XIa. J. Biol. Chem. 266, 24190-24197 (Pubitemid 21908923)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.35 , pp. 24190-24197
    • Bagliat, F.A.1    Jameson, B.A.2    Walsh, P.N.3
  • 22
    • 0029826460 scopus 로고    scopus 로고
    • Identification of a factor IX binding site on the third apple domain of activated factor XI
    • DOI 10.1074/jbc.271.46.29023
    • Sun, Y., and Gailani, D. (1996) Identification of a factor IX binding site on the third apple domain of activated factor XI. J. Biol. Chem. 271, 29023-29028 (Pubitemid 26382607)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.46 , pp. 29023-29028
    • Sun, Y.1    Gailani, D.2
  • 23
    • 0033579471 scopus 로고    scopus 로고
    • Identification of amino acids in the factor XI apple 3 domain required for activation of factor IX
    • Sun, M. F., Zhao, M., and Gailani, D. (1999) Identification of amino acids in the factor XI apple 3 domain required for activation of factor IX. J. Biol. Chem. 274, 36373-36378
    • (1999) J. Biol. Chem. , vol.274 , pp. 36373-36378
    • Sun, M.F.1    Zhao, M.2    Gailani, D.3
  • 25
    • 0037424508 scopus 로고    scopus 로고
    • The factor IX γ-carboxyglutamic acid (Gla) domain is involved in interactions between factor IX and factor XIa
    • DOI 10.1074/jbc.M212748200
    • Aktimur, A., Gabriel, M. A., Gailani, D., and Toomey, J. R. (2003) The factor IX γ-carboxyglutamic acid (Gla) domain is involved in interactions between factor IX and factor XIa. J. Biol. Chem. 278, 7981-7987 (Pubitemid 36800536)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.10 , pp. 7981-7987
    • Aktimur, A.1    Gabriel, M.A.2    Gailani, D.3    Toomey, J.R.4
  • 27
    • 60549105802 scopus 로고    scopus 로고
    • Global kinetic explorer. A new computer program for dynamic simulation and fitting of kinetic data
    • Johnson, K. A., Simpson, Z. B., and Blom, T. (2009) Global kinetic explorer. A new computer program for dynamic simulation and fitting of kinetic data. Anal. Biochem. 387, 20-29
    • (2009) Anal. Biochem. , vol.387 , pp. 20-29
    • Johnson, K.A.1    Simpson, Z.B.2    Blom, T.3
  • 28
    • 0025640853 scopus 로고
    • Kinetic intermediates in prothrombin activation: Bovine prethrombin 1 conversion to thrombin by factor X
    • Carlisle, T. L., Bock, P. E., and Jackson, C. M. (1990) Kinetic intermediates in prothrombin activation. Bovine prethrombin 1 conversion to thrombin by factor X. J. Biol. Chem. 265, 22044-22055 (Pubitemid 120023918)
    • (1990) Journal of Biological Chemistry , vol.265 , Issue.35 , pp. 22044-22055
    • Carlisle, T.L.1    Bock, P.E.2    Jackson, C.M.3
  • 29
    • 0032562804 scopus 로고    scopus 로고
    • Regions remote from the site of cleavage determine macromolecular substrate recognition by the prothrombinase complex
    • DOI 10.1074/jbc.273.17.10709
    • Betz, A., and Krishnaswamy, S. (1998) Regions remote from the site of cleavage determine macromolecular substrate recognition by the prothrombinase complex. J. Biol. Chem. 273, 10709-10718 (Pubitemid 28227686)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.17 , pp. 10709-10718
    • Betz, A.1    Krishnaswamy, S.2
  • 30
    • 2242455930 scopus 로고    scopus 로고
    • Extended interactions with prothrombinase enforce affinity and specificity for its macromolecular substrate
    • DOI 10.1074/jbc.M208677200
    • Orcutt, S. J., Pietropaolo, C., and Krishnaswamy, S. (2002) Extended interactions with prothrombinase enforce affinity and specificity for its macromolecular substrate. J. Biol. Chem. 277, 46191-46196 (Pubitemid 35417610)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.48 , pp. 46191-46196
    • Orcutt, S.J.1    Pietropaolo, C.2    Krishnaswamy, S.3
  • 31
    • 17644371341 scopus 로고    scopus 로고
    • Exosite-driven substrate specificity and function in coagulation
    • DOI 10.1111/j.1538-7836.2004.01021.x
    • Krishnaswamy, S. (2005) Exosite-driven substrate specificity and function in coagulation. J. Thromb. Haemost. 3, 54-67 (Pubitemid 41647115)
    • (2005) Journal of Thrombosis and Haemostasis , vol.3 , Issue.1 , pp. 54-67
    • Krishnaswamy, S.1
  • 33
    • 34250778996 scopus 로고    scopus 로고
    • Exosites in the substrate specificity of blood coagulation reactions
    • DOI 10.1111/j.1538-7836.2007.02496.x, State of the Art 2007: XXI Congress of the International Society on Thrombosis and Haemostasis
    • Bock, P. E., Panizzi, P., and Verhamme, I. M. (2007) Exosites in the substrate specificity of blood coagulation reactions. J. Thromb. Haemost. 5, 81-94 (Pubitemid 46958821)
    • (2007) Journal of Thrombosis and Haemostasis , vol.5 , Issue.SUPPL. 1 , pp. 81-94
    • Bock, P.E.1    Panizzi, P.2    Verhamme, I.M.A.3
  • 34
    • 0034665994 scopus 로고    scopus 로고
    • Exosite interactions determine the affinity of factor X for the extrinsic Xase complex
    • Baugh, R. J., Dickinson, C. D., Ruf, W., and Krishnaswamy, S. (2000) Exosite interactions determine the affinity of factor X for the extrinsic Xase complex. J. Biol. Chem. 275, 28826-28833
    • (2000) J. Biol. Chem. , vol.275 , pp. 28826-28833
    • Baugh, R.J.1    Dickinson, C.D.2    Ruf, W.3    Krishnaswamy, S.4
  • 35
    • 80052394097 scopus 로고    scopus 로고
    • The role of factor XIa (FXIa) catalytic domain exosite residues in substrate catalysis and inhibition by the Kunitz protease inhibitor domain of protease nexin 2
    • Su, Y. C., Miller, T. N., Navaneetham, D., Schoonmaker, R. T., Sinha, D., and Walsh, P. N. (2011) The role of factor XIa (FXIa) catalytic domain exosite residues in substrate catalysis and inhibition by the Kunitz protease inhibitor domain of protease nexin 2. J. Biol. Chem. 286, 31904-31914
    • (2011) J. Biol. Chem. , vol.286 , pp. 31904-31914
    • Su, Y.C.1    Miller, T.N.2    Navaneetham, D.3    Schoonmaker, R.T.4    Sinha, D.5    Walsh, P.N.6
  • 36
    • 84868311685 scopus 로고    scopus 로고
    • Structural and functional significance of amino acid lysine 192 (chymotrypsin numbering) in factor XIa and factor VIIa
    • (abstract 2011)
    • Schmidt, A. E., Agah, S., Sun, M. F., Padmanabhan, K., Cascio, D., Gailani, D., and Bajaj, S. P. (2008) Structural and functional significance of amino acid lysine 192 (chymotrypsin numbering) in factor XIa and factor VIIa. Blood 112, 708a (abstract 2011)
    • (2008) Blood , vol.112
    • Schmidt, A.E.1    Agah, S.2    Sun, M.F.3    Padmanabhan, K.4    Cascio, D.5    Gailani, D.6    Bajaj, S.P.7
  • 37
    • 84857496038 scopus 로고    scopus 로고
    • Productive recognition of factor IX by factor XIa exosites requires disulfide linkage between the heavy and light chains of factor XIa
    • Marcinkiewicz, M. M., Sinha, D., and Walsh, P. N. (2012) Productive recognition of factor IX by factor XIa exosites requires disulfide linkage between the heavy and light chains of factor XIa. J. Biol. Chem. 287, 6187-6195
    • (2012) J. Biol. Chem. , vol.287 , pp. 6187-6195
    • Marcinkiewicz, M.M.1    Sinha, D.2    Walsh, P.N.3
  • 38
    • 54149087827 scopus 로고    scopus 로고
    • Evolution of the contact phase of vertebrate blood coagulation
    • Ponczek, M. B., Gailani, D., and Doolittle, R. F. (2008) Evolution of the contact phase of vertebrate blood coagulation. J. Thromb. Haemost. 6, 1876-1883
    • (2008) J. Thromb. Haemost. , vol.6 , pp. 1876-1883
    • Ponczek, M.B.1    Gailani, D.2    Doolittle, R.F.3


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