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Volumn 11, Issue 11, 2013, Pages 2020-2028

Factor XI anion-binding sites are required for productive interactions with polyphosphate

Author keywords

Blood coagulation; Factor XI; Factor XIa; Heparin; PolyPhosphates

Indexed keywords

ANION; ANTITHROMBIN; BLOOD CLOTTING FACTOR 11; BLOOD CLOTTING FACTOR 11A; HEPARIN; POLYANION; POLYPHOSPHATE; RECOMBINANT THROMBIN; BLOOD CLOTTING FACTOR 9; POLYANIONS; POLYMER; RECOMBINANT PROTEIN; THROMBIN;

EID: 84887510096     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1111/jth.12414     Document Type: Article
Times cited : (40)

References (38)
  • 1
    • 84880430089 scopus 로고    scopus 로고
    • Molecular basis of blood coagulation
    • 6th Ed., Philadelphia, PA: Churchill Livingstone-Elsevier
    • Brummel-Ziedens K, Mann KG. Molecular basis of blood coagulation, In: Hematology: Basic Principles and Practice, 6th Ed., Philadelphia, PA: Churchill Livingstone-Elsevier, 2013: 1821-41.
    • (2013) Hematology: Basic Principles and Practice , pp. 1821-1841
    • Brummel-Ziedens, K.1    Mann, K.G.2
  • 3
    • 0017740353 scopus 로고
    • Human blood coagulation factor XI. Purification, properties, and mechanism of activation by activated factor XII
    • Bouma BN, Griffin JH. Human blood coagulation factor XI. Purification, properties, and mechanism of activation by activated factor XII. J Biol Chem 1977; 252: 6432-7.
    • (1977) J Biol Chem , vol.252 , pp. 6432-6437
    • Bouma, B.N.1    Griffin, J.H.2
  • 4
    • 0025975587 scopus 로고
    • Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains
    • McMullen BA, Fujikawa K, Davie EW. Location of the disulfide bonds in human coagulation factor XI: the presence of tandem apple domains. Biochemistry 1991; 30: 2056-60.
    • (1991) Biochemistry , vol.30 , pp. 2056-2060
    • McMullen, B.A.1    Fujikawa, K.2    Davie, E.W.3
  • 5
    • 77950978248 scopus 로고    scopus 로고
    • Structure and function of factor XI
    • Emsley J, McEwan PA, Gailani D. Structure and function of factor XI. Blood 2010; 115: 2569-77.
    • (2010) Blood , vol.115 , pp. 2569-2577
    • Emsley, J.1    McEwan, P.A.2    Gailani, D.3
  • 7
    • 0025874052 scopus 로고
    • Factor XI in a revised model of blood coagulation
    • Gailani D, Broze GJ. Factor XI in a revised model of blood coagulation. Science 1991; 253: 909-12.
    • (1991) Science , vol.253 , pp. 909-912
    • Gailani, D.1    Broze, G.J.2
  • 9
    • 84255201932 scopus 로고    scopus 로고
    • Polyphosphate is a cofactor for the activation of factor XI by thrombin
    • Choi SH, Smith SA, Morrissey JH. Polyphosphate is a cofactor for the activation of factor XI by thrombin. Blood 2011; 118: 6963-70.
    • (2011) Blood , vol.118 , pp. 6963-6970
    • Choi, S.H.1    Smith, S.A.2    Morrissey, J.H.3
  • 10
    • 0032836258 scopus 로고    scopus 로고
    • Inorganic phosphate: a molecule of many functions
    • Kornberg A, Rao NN, Ault-Riché D. Inorganic phosphate: a molecule of many functions. Ann Rev Biochem 1999; 68: 89-125.
    • (1999) Ann Rev Biochem , vol.68 , pp. 89-125
    • Kornberg, A.1    Rao, N.N.2    Ault-Riché, D.3
  • 11
    • 7244225025 scopus 로고    scopus 로고
    • Human platelet dense granules contain polyPhosphate and are similar to acidocalcisomes of bacteria and unicellular eukaryotes
    • Ruiz FA, Lea CR, Oldfield E, Docampo R. Human platelet dense granules contain polyPhosphate and are similar to acidocalcisomes of bacteria and unicellular eukaryotes. J Biol Chem 2004; 279: 44250-7.
    • (2004) J Biol Chem , vol.279 , pp. 44250-44257
    • Ruiz, F.A.1    Lea, C.R.2    Oldfield, E.3    Docampo, R.4
  • 13
    • 52449108966 scopus 로고    scopus 로고
    • Polyphosphate as a general procoagulant substance
    • Smith SA, Morrissey JH. Polyphosphate as a general procoagulant substance. J Thromb Haemost 2008; 6: 1750-6.
    • (2008) J Thromb Haemost , vol.6 , pp. 1750-1756
    • Smith, S.A.1    Morrissey, J.H.2
  • 15
    • 0032553436 scopus 로고    scopus 로고
    • Characterization of a heparin binding site on the heavy chain of factor XI
    • Zhao M, Abdel-Razek T, Sun MF, Gailani D. Characterization of a heparin binding site on the heavy chain of factor XI. J Biol Chem 1998; 273: 31153-9.
    • (1998) J Biol Chem , vol.273 , pp. 31153-31159
    • Zhao, M.1    Abdel-Razek, T.2    Sun, M.F.3    Gailani, D.4
  • 16
    • 61749093027 scopus 로고    scopus 로고
    • Characterization of a heparin-binding site on the catalytic domain of factor XIa: mechanism of heparin acceleration of factor XIa inhibition by the serpins antithrombin and C1-inhibitor
    • Yang L, Sun MF, Gailani D, Rezaie AR. Characterization of a heparin-binding site on the catalytic domain of factor XIa: mechanism of heparin acceleration of factor XIa inhibition by the serpins antithrombin and C1-inhibitor. Biochemistry 2009; 48: 1517-24.
    • (2009) Biochemistry , vol.48 , pp. 1517-1524
    • Yang, L.1    Sun, M.F.2    Gailani, D.3    Rezaie, A.R.4
  • 18
    • 0028332939 scopus 로고
    • Molecular mapping of the heparin-binding exosite of thrombin
    • Sheehan JP, Sadler JE. Molecular mapping of the heparin-binding exosite of thrombin. Proc Natl Acad Sci USA 1994; 91: 5518-22.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5518-5522
    • Sheehan, J.P.1    Sadler, J.E.2
  • 19
    • 0023930337 scopus 로고
    • Transient kinetics of heparin-catalyzed protease inactivation by antithrombin III. Linkage of protease-inhibitor-heparin interactions in the reaction with thrombin
    • Olson ST. Transient kinetics of heparin-catalyzed protease inactivation by antithrombin III. Linkage of protease-inhibitor-heparin interactions in the reaction with thrombin. J Biol Chem 1988; 263: 1698-708.
    • (1988) J Biol Chem , vol.263 , pp. 1698-1708
    • Olson, S.T.1
  • 21
    • 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 CK, Walz T, Billings PC, Lear JD, Walsh PN. Factor XI homodimer structure is essential for normal proteolytic activation by factor XIIa, thrombin, and factor XIa. J Biol Chem 2008; 283: 18655-64.
    • (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
  • 24
    • 79953167472 scopus 로고    scopus 로고
    • Heparin is a major activator of the anticoagulant serpin, protein Z-dependent protease inhibitor
    • Huang X, Rezaie AR, Broze GJ Jr, Olson ST. Heparin is a major activator of the anticoagulant serpin, protein Z-dependent protease inhibitor. J Biol Chem 2011; 286: 8740-51.
    • (2011) J Biol Chem , vol.286 , pp. 8740-8751
    • Huang, X.1    Rezaie, A.R.2    Broze Jr, G.J.3    Olson, S.T.4
  • 25
    • 0023695042 scopus 로고
    • Antithrombin action of phosvitin and other phosphate-containing polyanions is mediated by heparin cofactor II
    • Church FC, Pratt CW, Treanor RE, Whinna HC. Antithrombin action of phosvitin and other phosphate-containing polyanions is mediated by heparin cofactor II. FEBS Lett 1988; 237: 26-30.
    • (1988) FEBS Lett , vol.237 , pp. 26-30
    • Church, F.C.1    Pratt, C.W.2    Treanor, R.E.3    Whinna, H.C.4
  • 27
    • 84887509772 scopus 로고    scopus 로고
    • Heparin and vascular glycosaminoglycans
    • Marder VJ, Aird WC, Bennet JS, Schulman S, White GC, eds., 6th Ed., Philadelphia, PA: Lippincott, Williams & Wilkins
    • Tollefsen DM, Zhang L. Heparin and vascular glycosaminoglycans, In: Marder VJ, Aird WC, Bennet JS, Schulman S, White GC, eds. Hemostasis and Thrombosis: Basic Principles and Clinical Practice, 6th Ed., Philadelphia, PA: Lippincott, Williams & Wilkins, 2013: 585-97.
    • (2013) Hemostasis and Thrombosis: Basic Principles and Clinical Practice , pp. 585-597
    • Tollefsen, D.M.1    Zhang, L.2
  • 28
    • 85009653153 scopus 로고    scopus 로고
    • The blood coagulation factors and inhibitors: their primary structure, complementary DNAs, Genes, and Expression
    • 6th Ed., Philadelphia, PA: Lippincott, Williams & Wilkins
    • Chung DW, Xu W, Davie EW. The blood coagulation factors and inhibitors: their primary structure, complementary DNAs, Genes, and Expression, In: Hemostasis and Thrombosis: Basic Principles and Clinical Practice, 6th Ed., Philadelphia, PA: Lippincott, Williams & Wilkins, 2013: 110-4.
    • (2013) Hemostasis and Thrombosis: Basic Principles and Clinical Practice , pp. 110-114
    • Chung, D.W.1    Xu, W.2    Davie, E.W.3
  • 29
    • 54149087827 scopus 로고    scopus 로고
    • Evolution of the contact phase of vertebrate blood coagulation
    • Ponczek MB, Gailani D, Doolittle RF. Evolution of the contact phase of vertebrate blood coagulation. J Thromb Haemost 2008; 6: 1876-83.
    • (2008) J Thromb Haemost , vol.6 , pp. 1876-1883
    • Ponczek, M.B.1    Gailani, D.2    Doolittle, R.F.3
  • 30
    • 0026082814 scopus 로고
    • Location of the disulfide bonds in human plasma prekallikrein: the presence of four novel apple domains in the amino-terminal portion of the molecule
    • McMullen BA, Fujikawa K, Davie EW. Location of the disulfide bonds in human plasma prekallikrein: the presence of four novel apple domains in the amino-terminal portion of the molecule. Biochemistry 1991; 30: 2050-6.
    • (1991) Biochemistry , vol.30 , pp. 2050-2056
    • McMullen, B.A.1    Fujikawa, K.2    Davie, E.W.3
  • 32
    • 0021235057 scopus 로고
    • In vitro activation of the contact (Hageman factor) system of plasma by heparin and chondroitin sulfate E
    • Hojima Y, Cochrane CG, Wiggins RC, Austen KF, Stevens RL. In vitro activation of the contact (Hageman factor) system of plasma by heparin and chondroitin sulfate E. Blood 1984; 63: 1453-9.
    • (1984) Blood , vol.63 , pp. 1453-1459
    • Hojima, Y.1    Cochrane, C.G.2    Wiggins, R.C.3    Austen, K.F.4    Stevens, R.L.5
  • 33
    • 0030851598 scopus 로고    scopus 로고
    • Mast cell derived heparin activates the contact system: a link to kinin generation in allergic reactions
    • Brunnée T, Reddigari SR, Shibayama Y, Kaplan AP, Silverberg M. Mast cell derived heparin activates the contact system: a link to kinin generation in allergic reactions. Clin Exp Allergy 1997; 27: 653-63.
    • (1997) Clin Exp Allergy , vol.27 , pp. 653-663
    • Brunnée, T.1    Reddigari, S.R.2    Shibayama, Y.3    Kaplan, A.P.4    Silverberg, M.5
  • 34
    • 84871528525 scopus 로고    scopus 로고
    • Inhibition of polyPhosphate as a novel strategy for preventing thrombosis and inflammation
    • Smith SA, Choi SH, Collins JN, Travers RJ, Cooley BC, Morrissey JH. Inhibition of polyPhosphate as a novel strategy for preventing thrombosis and inflammation. Blood 2012; 120: 5103-10.
    • (2012) Blood , vol.120 , pp. 5103-5110
    • Smith, S.A.1    Choi, S.H.2    Collins, J.N.3    Travers, R.J.4    Cooley, B.C.5    Morrissey, J.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.