메뉴 건너뛰기




Volumn 35, Issue 6, 2015, Pages 1298-1305

2013 Scientific Sessions Sol Sherry Distinguished Lecture in Thrombosis Polyphosphate: A Novel Modulator of Hemostasis and Thrombosis

Author keywords

blood coagulation; blood platelets; hemostasis; polyphosphates; thrombosis

Indexed keywords

ANTICOAGULANT AGENT; BLOOD CLOTTING FACTOR 5; HEMOSTATIC AGENT; HEPARIN; POLYPHOSPHATE; POLYPHOSPHATE INHIBITOR; PROTEINASE; THROMBIN; TISSUE FACTOR PATHWAY INHIBITOR; UNCLASSIFIED DRUG; BLOOD CLOTTING FACTOR 11; FIBRIN; THROMBOPLASTIN;

EID: 84933048438     PISSN: 10795642     EISSN: 15244636     Source Type: Journal    
DOI: 10.1161/ATVBAHA.115.301927     Document Type: Review
Times cited : (13)

References (91)
  • 1
    • 0031944979 scopus 로고    scopus 로고
    • Novel assay reveals multiple pathways regulating stress-induced accumulations of inorganic polyphosphate in Escherichia coli
    • Ault-Riché D, Fraley CD, Tzeng CM, Kornberg A. Novel assay reveals multiple pathways regulating stress-induced accumulations of inorganic polyphosphate in Escherichia coli. J Bacteriol. 1998;180:1841-1847.
    • (1998) J Bacteriol , vol.180 , pp. 1841-1847
    • Ault-Riché, D.1    Fraley, C.D.2    Tzeng, C.M.3    Kornberg, A.4
  • 2
    • 9244221616 scopus 로고    scopus 로고
    • Inorganic polyphosphate in the origin and survival of species
    • Brown MR, Kornberg A. Inorganic polyphosphate in the origin and survival of species. Proc Natl Acad Sci U S A. 2004;101:16085-16087. doi: 10.1073/pnas.0406909101.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 16085-16087
    • Brown, M.R.1    Kornberg, A.2
  • 3
    • 67650759738 scopus 로고    scopus 로고
    • Inorganic polyphosphate: Essential for growth and survival
    • Rao NN, Gómez-García MR, Kornberg A. Inorganic polyphosphate: essential for growth and survival. Annu Rev Biochem. 2009;78:605-647. doi: 10.1146/annurev.biochem.77.083007.093039.
    • (2009) Annu Rev Biochem , vol.78 , pp. 605-647
    • Rao, N.N.1    Gómez-García, M.R.2    Kornberg, A.3
  • 4
    • 80051469362 scopus 로고    scopus 로고
    • Acidocalcisomes
    • Docampo R, Moreno SN. Acidocalcisomes. Cell Calcium. 2011;50:113-119. doi: 10.1016/j.ceca.2011.05.012.
    • (2011) Cell Calcium , vol.50 , pp. 113-119
    • Docampo, R.1    Moreno, S.N.2
  • 5
    • 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;279:44250-44257. doi: 10.1074/jbc.M406261200.
    • (2004) J Biol Chem , vol.279 , pp. 44250-44257
    • Ruiz, F.A.1    Lea, C.R.2    Oldfield, E.3    Docampo, R.4
  • 7
    • 0032836258 scopus 로고    scopus 로고
    • Inorganic polyphosphate: A molecule of many functions
    • Kornberg A, Rao NN, Ault-Riché D. Inorganic polyphosphate: a molecule of many functions. Annu Rev Biochem. 1999;68:89-125. doi: 10.1146/annurev.biochem.68.1.89.
    • (1999) Annu Rev Biochem , vol.68 , pp. 89-125
    • Kornberg, A.1    Rao, N.N.2    Ault-Riché, D.3
  • 8
    • 0020546624 scopus 로고
    • Isolation of a high molecular weight polyphosphate from Neisseria gonorrhoeae
    • Noegel A, Gotschlich EC. Isolation of a high molecular weight polyphosphate from Neisseria gonorrhoeae. J Exp Med. 1983;157:2049-2060.
    • (1983) J Exp Med , vol.157 , pp. 2049-2060
    • Noegel, A.1    Gotschlich, E.C.2
  • 9
    • 0027169698 scopus 로고
    • Purification and characterization of polyphosphate kinase from Neisseria meningitidis
    • Tinsley CR, Manjula BN, Gotschlich EC. Purification and characterization of polyphosphate kinase from Neisseria meningitidis. Infect Immun. 1993;61:3703-3710.
    • (1993) Infect Immun , vol.61 , pp. 3703-3710
    • Tinsley, C.R.1    Manjula, B.N.2    Gotschlich, E.C.3
  • 10
    • 84865240181 scopus 로고    scopus 로고
    • Polyphosphate is a novel pro-inflammatory regulator of mast cells and is located in acidocalcisomes
    • Moreno-Sanchez D, Hernandez-Ruiz L, Ruiz FA, Docampo R. Polyphosphate is a novel pro-inflammatory regulator of mast cells and is located in acidocalcisomes. J Biol Chem. 2012;287:28435-28444. doi: 10.1074/jbc.M112.385823.
    • (2012) J Biol Chem , vol.287 , pp. 28435-28444
    • Moreno-Sanchez, D.1    Hernandez-Ruiz, L.2    Ruiz, F.A.3    Docampo, R.4
  • 12
    • 0034145547 scopus 로고    scopus 로고
    • Transmembrane ion transport by polyphosphate/poly-3-hydroxybutyrate complexes
    • Reusch RN. Transmembrane ion transport by polyphosphate/poly-3-hydroxybutyrate complexes. Biochemistry (Mosc). 2000; 65:280-295.
    • (2000) Biochemistry (Mosc) , vol.65 , pp. 280-295
    • Reusch, R.N.1
  • 13
    • 0030851916 scopus 로고    scopus 로고
    • Novel components and enzymatic activities of the human erythrocyte plasma membrane calcium pump
    • Reusch RN, Huang R, Kosk-Kosicka D. Novel components and enzymatic activities of the human erythrocyte plasma membrane calcium pump. FEBS Lett. 1997;412:592-596.
    • (1997) FEBS Lett , vol.412 , pp. 592-596
    • Reusch, R.N.1    Huang, R.2    Kosk-Kosicka, D.3
  • 15
    • 0028908588 scopus 로고
    • Inorganic polyphosphate in mammalian cells and tissues
    • Kumble KD, Kornberg A. Inorganic polyphosphate in mammalian cells and tissues. J Biol Chem. 1995;270:5818-5822.
    • (1995) J Biol Chem , vol.270 , pp. 5818-5822
    • Kumble, K.D.1    Kornberg, A.2
  • 16
    • 0026610639 scopus 로고
    • Incorporation of [32P]orthophosphate into long chains of inorganic polyphosphate within lysosomes of human fibroblasts
    • Pisoni RL, Lindley ER. Incorporation of [32P]orthophosphate into long chains of inorganic polyphosphate within lysosomes of human fibroblasts. J Biol Chem. 1992;267:3626-3631.
    • (1992) J Biol Chem , vol.267 , pp. 3626-3631
    • Pisoni, R.L.1    Lindley, E.R.2
  • 17
    • 84861120098 scopus 로고    scopus 로고
    • Inorganic polyphosphate is a potent activator of the mitochondrial permeability transition pore in cardiac myocytes
    • Seidlmayer LK, Gomez-Garcia MR, Blatter LA, Pavlov E, Dedkova EN. Inorganic polyphosphate is a potent activator of the mitochondrial permeability transition pore in cardiac myocytes. J Gen Physiol. 2012;139:321-331. doi: 10.1085/jgp.201210788.
    • (2012) J Gen Physiol , vol.139 , pp. 321-331
    • Seidlmayer, L.K.1    Gomez-Garcia, M.R.2    Blatter, L.A.3    Pavlov, E.4    Dedkova, E.N.5
  • 18
    • 84878522215 scopus 로고    scopus 로고
    • Polyphosphate and its diverse functions in host cells and pathogens
    • Moreno SN, Docampo R. Polyphosphate and its diverse functions in host cells and pathogens. PLoS Pathog. 2013;9:e1003230. doi: 10.1371/journal. ppat.1003230.
    • (2013) PLoS Pathog , vol.9 , pp. e1003230
    • Moreno, S.N.1    Docampo, R.2
  • 20
    • 0035844728 scopus 로고    scopus 로고
    • Mammalian intestinal alkaline phosphatase acts as highly active exopolyphosphatase
    • Lorenz B, Schröder HC. Mammalian intestinal alkaline phosphatase acts as highly active exopolyphosphatase. Biochim Biophys Acta. 2001;1547:254-261.
    • (2001) Biochim Biophys Acta , vol.1547 , pp. 254-261
    • Lorenz, B.1    Schröder, H.C.2
  • 21
    • 0029909659 scopus 로고    scopus 로고
    • Endopolyphosphatases for long chain inorganic polyphosphate in yeast and mammals
    • Kumble KD, Kornberg A. Endopolyphosphatases for long chain inorganic polyphosphate in yeast and mammals. J Biol Chem. 1996;271:27146-27151.
    • (1996) J Biol Chem , vol.271 , pp. 27146-27151
    • Kumble, K.D.1    Kornberg, A.2
  • 24
    • 0141594599 scopus 로고    scopus 로고
    • Inorganic polyphosphate stimulates mammalian TOR, a kinase involved in the proliferation of mammary cancer cells
    • Wang L, Fraley CD, Faridi J, Kornberg A, Roth RA. Inorganic polyphosphate stimulates mammalian TOR, a kinase involved in the proliferation of mammary cancer cells. Proc Natl Acad Sci U S A. 2003;100:11249-11254. doi: 10.1073/pnas.1534805100.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 11249-11254
    • Wang, L.1    Fraley, C.D.2    Faridi, J.3    Kornberg, A.4    Roth, R.A.5
  • 26
    • 70449704799 scopus 로고    scopus 로고
    • The Nm23-H1-h-Prune complex in cellular physiology: A 'tip of the iceberg' protein network perspective
    • Galasso A, Zollo M. The Nm23-H1-h-Prune complex in cellular physiology: a 'tip of the iceberg' protein network perspective. Mol Cell Biochem. 2009;329:149-159. doi: 10.1007/s11010-009-0115-4.
    • (2009) Mol Cell Biochem , vol.329 , pp. 149-159
    • Galasso, A.1    Zollo, M.2
  • 32
    • 84908536962 scopus 로고    scopus 로고
    • The factor XII-driven plasma contact system
    • In: Marder VJ, Aird WC, Bennett JS, Schulman S, White GC II, eds.. Philadelphia: Lippincott Williams & Wilkins
    • Renné T. The factor XII-driven plasma contact system. In: Marder VJ, Aird WC, Bennett JS, Schulman S, White GC II, eds. Hemostasis and Thrombosis: Basic Principles and Clinical Practice. Philadelphia: Lippincott Williams & Wilkins; 2013:242-253.
    • (2013) Hemostasis and Thrombosis: Basic Principles and Clinical Practice , pp. 242-253
    • Renné, T.1
  • 33
    • 78149432362 scopus 로고    scopus 로고
    • Phosphoramidate end labeling of inorganic polyphosphates: Facile manipulation of polyphosphate for investigating and modulating its biological activities
    • Choi SH, Collins JN, Smith SA, Davis-Harrison RL, Rienstra CM, Morrissey JH. Phosphoramidate end labeling of inorganic polyphosphates: facile manipulation of polyphosphate for investigating and modulating its biological activities. Biochemistry. 2010;49:9935-9941. doi: 10.1021/bi1014437.
    • (2010) Biochemistry , vol.49 , pp. 9935-9941
    • Choi, S.H.1    Collins, J.N.2    Smith, S.A.3    Davis-Harrison, R.L.4    Rienstra, C.M.5    Morrissey, J.H.6
  • 35
    • 84908555957 scopus 로고    scopus 로고
    • Single-chain factor XII exhibits activity when complexed to polyphosphate
    • Engel R, Brain CM, Paget J, Lionikiene AS, Mutch NJ. Single-chain factor XII exhibits activity when complexed to polyphosphate. J Thromb Haemost. 2014;12:1513-1522. doi: 10.1111/jth.12663.
    • (2014) J Thromb Haemost , vol.12 , pp. 1513-1522
    • Engel, R.1    Brain, C.M.2    Paget, J.3    Lionikiene, A.S.4    Mutch, N.J.5
  • 36
    • 36349018844 scopus 로고    scopus 로고
    • The plasma kallikrein-kinin system: Its evolution from contact activation
    • Schmaier AH, McCrae KR. The plasma kallikrein-kinin system: its evolution from contact activation. J Thromb Haemost. 2007;5:2323-2329. doi: 10.1111/j.1538-7836.2007.02770.x.
    • (2007) J Thromb Haemost , vol.5 , pp. 2323-2329
    • Schmaier, A.H.1    McCrae, K.R.2
  • 38
    • 0018378387 scopus 로고
    • Isolation and characterization of single chain bovine factor v
    • Nesheim ME, Myrmel KH, Hibbard L, Mann KG. Isolation and characterization of single chain bovine factor V. J Biol Chem. 1979;254:508-517.
    • (1979) J Biol Chem , vol.254 , pp. 508-517
    • Nesheim, M.E.1    Myrmel, K.H.2    Hibbard, L.3    Mann, K.G.4
  • 39
    • 0025139882 scopus 로고
    • Activation of human factor v by factor Xa and thrombin
    • Monkovic DD, Tracy PB. Activation of human factor V by factor Xa and thrombin. Biochemistry. 1990;29:1118-1128.
    • (1990) Biochemistry , vol.29 , pp. 1118-1128
    • Monkovic, D.D.1    Tracy, P.B.2
  • 40
    • 0021046120 scopus 로고
    • The factor Xa-catalyzed activation of factor v
    • Foster WB, Nesheim ME, Mann KG. The factor Xa-catalyzed activation of factor V. J Biol Chem. 1983;258:13970-13977.
    • (1983) J Biol Chem , vol.258 , pp. 13970-13977
    • Foster, W.B.1    Nesheim, M.E.2    Mann, K.G.3
  • 42
    • 0020320628 scopus 로고
    • Thrombin-catalyzed activation of human coagulation factor v
    • Suzuki K, Dahlbäck B, Stenflo J. Thrombin-catalyzed activation of human coagulation factor V. J Biol Chem. 1982;257:6556-6564.
    • (1982) J Biol Chem , vol.257 , pp. 6556-6564
    • Suzuki, K.1    Dahlbäck, B.2    Stenflo, J.3
  • 45
    • 0018622772 scopus 로고
    • The contribution of bovine Factor v and Factor Va to the activity of prothrombinase
    • Nesheim ME, Taswell JB, Mann KG. The contribution of bovine Factor V and Factor Va to the activity of prothrombinase. J Biol Chem. 1979;254:10952-10962.
    • (1979) J Biol Chem , vol.254 , pp. 10952-10962
    • Nesheim, M.E.1    Taswell, J.B.2    Mann, K.G.3
  • 46
    • 0019862464 scopus 로고
    • Purification and characterization of human coagulation factor v
    • Kane WH, Majerus PW. Purification and characterization of human coagulation factor V. J Biol Chem. 1981;256:1002-1007.
    • (1981) J Biol Chem , vol.256 , pp. 1002-1007
    • Kane, W.H.1    Majerus, P.W.2
  • 47
    • 84925310761 scopus 로고    scopus 로고
    • Polyphosphate accelerates factor v activation by factor XIa
    • Choi SH, Smith SA, Morrissey JH. Polyphosphate accelerates factor V activation by factor XIa. Thromb Haemost. 2015;113:599-604. doi: 10.1160/TH14-06-0515.
    • (2015) Thromb Haemost , vol.113 , pp. 599-604
    • Choi, S.H.1    Smith, S.A.2    Morrissey, J.H.3
  • 48
    • 0029039574 scopus 로고
    • Tissue factor pathway inhibitor and the current concept of blood coagulation
    • Broze GJ Jr. Tissue factor pathway inhibitor and the current concept of blood coagulation. Blood Coagul Fibrinolysis. 1995;6 Suppl 1:S7-13.
    • (1995) Blood Coagul Fibrinolysis , vol.6 , pp. S7-13
    • Broze, G.J.1
  • 49
    • 0030039385 scopus 로고    scopus 로고
    • Physiological concentrations of tissue factor pathway inhibitor do not inhibit prothrombinase
    • Mast AE, Broze GJ Jr. Physiological concentrations of tissue factor pathway inhibitor do not inhibit prothrombinase. Blood. 1996;87:1845-1850.
    • (1996) Blood , vol.87 , pp. 1845-1850
    • Mast, A.E.1    Broze, G.J.2
  • 50
    • 84887103363 scopus 로고    scopus 로고
    • Tissue factor pathway inhibitor-alpha inhibits prothrombinase during the initiation of blood coagulation
    • Wood JP, Bunce MW, Maroney SA, Tracy PB, Camire RM, Mast AE. Tissue factor pathway inhibitor-alpha inhibits prothrombinase during the initiation of blood coagulation. Proc Natl Acad Sci U S A. 2013;110:17838-17843. doi: 10.1073/pnas.1310444110.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 17838-17843
    • Wood, J.P.1    Bunce, M.W.2    Maroney, S.A.3    Tracy, P.B.4    Camire, R.M.5    Mast, A.E.6
  • 52
    • 0025874052 scopus 로고
    • Factor XI activation in a revised model of blood coagulation
    • Gailani D, Broze GJ Jr. Factor XI activation in a revised model of blood coagulation. Science. 1991;253:909-912.
    • (1991) Science , vol.253 , pp. 909-912
    • Gailani, D.1    Broze, G.J.2
  • 53
    • 84859707412 scopus 로고    scopus 로고
    • The procoagulant and proinflammatory plasma contact system
    • Renné T. The procoagulant and proinflammatory plasma contact system. Semin Immunopathol. 2012;34:31-41. doi: 10.1007/s00281-011-0288-2.
    • (2012) Semin Immunopathol , vol.34 , pp. 31-41
    • Renné, T.1
  • 54
    • 67849097372 scopus 로고    scopus 로고
    • Factor XI deficiency in humans
    • Seligsohn U. Factor XI deficiency in humans. J Thromb Haemost. 2009;7(suppl 1):84-87. doi: 10.1111/j.1538-7836.2009.03395.x.
    • (2009) J Thromb Haemost , vol.7 , pp. 84-87
    • Seligsohn, U.1
  • 55
    • 0027169993 scopus 로고
    • Factor XII-independent activation of factor XI in plasma: Effects of sulfatides on tissue factor-induced coagulation
    • Gailani D, Broze GJ Jr. Factor XII-independent activation of factor XI in plasma: effects of sulfatides on tissue factor-induced coagulation. Blood. 1993;82:813-819.
    • (1993) Blood , vol.82 , pp. 813-819
    • Gailani, D.1    Broze, G.J.2
  • 56
    • 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;118:6963-6970. doi: 10.1182/blood-2011-07-368811.
    • (2011) Blood , vol.118 , pp. 6963-6970
    • Choi, S.H.1    Smith, S.A.2    Morrissey, J.H.3
  • 59
    • 0029842962 scopus 로고    scopus 로고
    • Proneness to formation of tight and rigid fibrin gel structures in men with myocardial infarction at a young age
    • Fatah K, Silveira A, Tornvall P, Karpe F, Blombäck M, Hamsten A. Proneness to formation of tight and rigid fibrin gel structures in men with myocardial infarction at a young age. Thromb Haemost. 1996;76:535-540.
    • (1996) Thromb Haemost , vol.76 , pp. 535-540
    • Fatah, K.1    Silveira, A.2    Tornvall, P.3    Karpe, F.4    Blombäck, M.5    Hamsten, A.6
  • 60
    • 77953521329 scopus 로고    scopus 로고
    • Plasma and cellular contributions to fibrin network formation, structure and stability
    • Wolberg AS. Plasma and cellular contributions to fibrin network formation, structure and stability. Haemophilia. 2010;16 Suppl 3:7-12. doi: 10.1111/j.1365-2516.2010.02253.x.
    • (2010) Haemophilia , vol.16 , pp. 7-12
    • Wolberg, A.S.1
  • 61
    • 50349100313 scopus 로고    scopus 로고
    • Polyphosphate enhances fibrin clot structure
    • Smith SA, Morrissey JH. Polyphosphate enhances fibrin clot structure. Blood. 2008;112:2810-2816. doi: 10.1182/blood-2008-03-145755.
    • (2008) Blood , vol.112 , pp. 2810-2816
    • Smith, S.A.1    Morrissey, J.H.2
  • 62
    • 77952974521 scopus 로고    scopus 로고
    • Polyphosphate modifies the fibrin network and down-regulates fibrinolysis by attenuating binding of tPA and plasminogen to fibrin
    • Mutch NJ, Engel R, Uitte de Willige S, Philippou H, Ariëns RA. Polyphosphate modifies the fibrin network and down-regulates fibrinolysis by attenuating binding of tPA and plasminogen to fibrin. Blood. 2010;115:3980-3988. doi: 10.1182/blood-2009-11-254029.
    • (2010) Blood , vol.115 , pp. 3980-3988
    • Mutch, N.J.1    Engel, R.2    Uitte De Willige, S.3    Philippou, H.4    Ariëns, R.A.5
  • 64
    • 84886805114 scopus 로고    scopus 로고
    • Inositol hexakisphosphate kinase 1 maintains hemostasis in mice by regulating platelet polyphosphate levels
    • Ghosh S, Shukla D, Suman K, Lakshmi BJ, Manorama R, Kumar S, Bhandari R. Inositol hexakisphosphate kinase 1 maintains hemostasis in mice by regulating platelet polyphosphate levels. Blood. 2013;122:1478-1486. doi: 10.1182/blood-2013-01-481549.
    • (2013) Blood , vol.122 , pp. 1478-1486
    • Ghosh, S.1    Shukla, D.2    Suman, K.3    Lakshmi, B.J.4    Manorama, R.5    Kumar, S.6    Bhandari, R.7
  • 66
    • 84908594708 scopus 로고    scopus 로고
    • Nontoxic polyphosphate inhibitors reduce thrombosis while sparing hemostasis
    • Travers RJ, Shenoi RA, Kalathottukaren MT, Kizhakkedathu JN, Morrissey JH. Nontoxic polyphosphate inhibitors reduce thrombosis while sparing hemostasis. Blood. 2014;124:3183-3190. doi: 10.1182/blood-2014-05-577932.
    • (2014) Blood , vol.124 , pp. 3183-3190
    • Travers, R.J.1    Shenoi, R.A.2    Kalathottukaren, M.T.3    Kizhakkedathu, J.N.4    Morrissey, J.H.5
  • 67
    • 84871505285 scopus 로고    scopus 로고
    • Thrombosis as an intravascular effector of innate immunity
    • Engelmann B, Massberg S. Thrombosis as an intravascular effector of innate immunity. Nat Rev Immunol. 2013;13:34-45. doi: 10.1038/nri3345.
    • (2013) Nat Rev Immunol , vol.13 , pp. 34-45
    • Engelmann, B.1    Massberg, S.2
  • 68
    • 0036269750 scopus 로고    scopus 로고
    • Activated factor XII levels and factor XII 46C>T genotype in relation to coronary artery calcification in patients with type 1 diabetes and healthy subjects
    • Colhoun HM, Zito F, Norman Chan N, Rubens MB, Fuller JH, Humphries SE. Activated factor XII levels and factor XII 46C>T genotype in relation to coronary artery calcification in patients with type 1 diabetes and healthy subjects. Atherosclerosis. 2002;163:363-369.
    • (2002) Atherosclerosis , vol.163 , pp. 363-369
    • Colhoun, H.M.1    Zito, F.2    Norman Chan, N.3    Rubens, M.B.4    Fuller, J.H.5    Humphries, S.E.6
  • 69
    • 0842325878 scopus 로고    scopus 로고
    • Activated factor 12 (FXIIa) predicts recurrent coronary events after an acute myocardial infarction
    • Grundt H, Nilsen DW, Hetland Ø, Valente E, Fagertun HE. Activated factor 12 (FXIIa) predicts recurrent coronary events after an acute myocardial infarction. Am Heart J. 2004;147:260-266.
    • (2004) Am Heart J , vol.147 , pp. 260-266
    • Grundt, H.1    Nilsen, D.W.2    Hetland Ø.3    Valente, E.4    Fagertun, H.E.5
  • 70
    • 33845497457 scopus 로고    scopus 로고
    • Levels of intrinsic coagulation factors and the risk of myocardial infarction among men: Opposite and synergistic effects of factors XI and XII
    • Doggen CJ, Rosendaal FR, Meijers JC. Levels of intrinsic coagulation factors and the risk of myocardial infarction among men: Opposite and synergistic effects of factors XI and XII. Blood. 2006;108:4045-4051. doi: 10.1182/blood-2005-12-023697.
    • (2006) Blood , vol.108 , pp. 4045-4051
    • Doggen, C.J.1    Rosendaal, F.R.2    Meijers, J.C.3
  • 72
    • 43249088304 scopus 로고    scopus 로고
    • Reduced incidence of ischemic stroke in patients with severe factor XI deficiency
    • Salomon O, Steinberg DM, Koren-Morag N, Tanne D, Seligsohn U. Reduced incidence of ischemic stroke in patients with severe factor XI deficiency. Blood. 2008;111:4113-4117. doi: 10.1182/blood-2007-10-120139.
    • (2008) Blood , vol.111 , pp. 4113-4117
    • Salomon, O.1    Steinberg, D.M.2    Koren-Morag, N.3    Tanne, D.4    Seligsohn, U.5
  • 73
    • 79851476826 scopus 로고    scopus 로고
    • Patients with severe factor XI deficiency have a reduced incidence of deepvein thrombosis
    • Salomon O, Steinberg DM, Zucker M, Varon D, Zivelin A, Seligsohn U. Patients with severe factor XI deficiency have a reduced incidence of deepvein thrombosis. Thromb Haemost. 2011;105:269-273. doi: 10.1160/TH10-05-0307.
    • (2011) Thromb Haemost , vol.105 , pp. 269-273
    • Salomon, O.1    Steinberg, D.M.2    Zucker, M.3    Varon, D.4    Zivelin, A.5    Seligsohn, U.6
  • 74
    • 36349012420 scopus 로고    scopus 로고
    • Intrinsic pathway of coagulation and arterial thrombosis
    • Gailani D, Renné T. Intrinsic pathway of coagulation and arterial thrombosis. Arterioscler Thromb Vasc Biol. 2007;27:2507-2513. doi: 10.1161/ATVBAHA.107.155952.
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 2507-2513
    • Gailani, D.1    Renné, T.2
  • 75
    • 55249100301 scopus 로고    scopus 로고
    • Novel roles for factor XII-driven plasma contact activation system
    • Müller F, Renné T. Novel roles for factor XII-driven plasma contact activation system. Curr Opin Hematol. 2008;15:516-521. doi: 10.1097/MOH.0b013e328309ec85.
    • (2008) Curr Opin Hematol , vol.15 , pp. 516-521
    • Müller, F.1    Renné, T.2
  • 77
    • 84876542457 scopus 로고    scopus 로고
    • Hierarchical organization in the hemostatic response and its relationship to the platelet-signaling network
    • Stalker TJ, Traxler EA, Wu J, Wannemacher KM, Cermignano SL, Voronov R, Diamond SL, Brass LF. Hierarchical organization in the hemostatic response and its relationship to the platelet-signaling network. Blood. 2013;121:1875-1885. doi: 10.1182/blood-2012-09-457739.
    • (2013) Blood , vol.121 , pp. 1875-1885
    • Stalker, T.J.1    Traxler, E.A.2    Wu, J.3    Wannemacher, K.M.4    Cermignano, S.L.5    Voronov, R.6    Diamond, S.L.7    Brass, L.F.8
  • 78
    • 34447322451 scopus 로고    scopus 로고
    • Extracellular RNA constitutes a natural procoagulant cofactor in blood coagulation
    • Kannemeier C, Shibamiya A, Nakazawa F, et al. Extracellular RNA constitutes a natural procoagulant cofactor in blood coagulation. Proc Natl Acad Sci U S A. 2007;104:6388-6393. doi: 10.1073/pnas.0608647104.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 6388-6393
    • Kannemeier, C.1    Shibamiya, A.2    Nakazawa, F.3
  • 80
    • 80051884192 scopus 로고    scopus 로고
    • Extracellular histones promote thrombin generation through platelet-dependent mechanisms: Involvement of platelet TLR2 and TLR4
    • Semeraro F, Ammollo CT, Morrissey JH, Dale GL, Friese P, Esmon NL, Esmon CT. Extracellular histones promote thrombin generation through platelet-dependent mechanisms: involvement of platelet TLR2 and TLR4. Blood. 2011;118:1952-1961. doi: 10.1182/blood-2011-03-343061.
    • (2011) Blood , vol.118 , pp. 1952-1961
    • Semeraro, F.1    Ammollo, C.T.2    Morrissey, J.H.3    Dale, G.L.4    Friese, P.5    Esmon, N.L.6    Esmon, C.T.7
  • 81
    • 84861664297 scopus 로고    scopus 로고
    • Polyphosphate elicits pro-inflammatory responses that are counteracted by activated protein C in both cellular and animal models
    • Bae JS, Lee W, Rezaie AR. Polyphosphate elicits pro-inflammatory responses that are counteracted by activated protein C in both cellular and animal models. J Thromb Haemost. 2012;10:1145-1151. doi: 10.1111/j.1538-7836.2012.04671.x.
    • (2012) J Thromb Haemost , vol.10 , pp. 1145-1151
    • Bae, J.S.1    Lee, W.2    Rezaie, A.R.3
  • 82
    • 39749193872 scopus 로고    scopus 로고
    • Activation of the FGF signaling pathway and subsequent induction of mesenchymal stem cell differentiation by inorganic polyphosphate
    • Kawazoe Y, Katoh S, Onodera Y, Kohgo T, Shindoh M, Shiba T. Activation of the FGF signaling pathway and subsequent induction of mesenchymal stem cell differentiation by inorganic polyphosphate. Int J Biol Sci. 2008;4:37-47.
    • (2008) Int J Biol Sci , vol.4 , pp. 37-47
    • Kawazoe, Y.1    Katoh, S.2    Onodera, Y.3    Kohgo, T.4    Shindoh, M.5    Shiba, T.6
  • 83
    • 84883216057 scopus 로고    scopus 로고
    • Plasma kallikrein: The bradykinin-producing enzyme
    • Björkqvist J, Jämsä A, Renné T. Plasma kallikrein: the bradykinin-producing enzyme. Thromb Haemost. 2013;110:399-407. doi: 10.1160/TH13-03-0258.
    • (2013) Thromb Haemost , vol.110 , pp. 399-407
    • Björkqvist, J.1    Jämsä, A.2    Renné, T.3
  • 84
    • 0020529790 scopus 로고
    • Mechanisms of activation of the classical pathway of complement by Hageman factor fragment
    • Ghebrehiwet B, Randazzo BP, Dunn JT, Silverberg M, Kaplan AP. Mechanisms of activation of the classical pathway of complement by Hageman factor fragment. J Clin Invest. 1983;71:1450-1456.
    • (1983) J Clin Invest , vol.71 , pp. 1450-1456
    • Ghebrehiwet, B.1    Randazzo, B.P.2    Dunn, J.T.3    Silverberg, M.4    Kaplan, A.P.5
  • 85
    • 0020047810 scopus 로고
    • The activation of the alternative pathway C3 convertase by human plasma kallikrein
    • DiScipio RG. The activation of the alternative pathway C3 convertase by human plasma kallikrein. Immunology. 1982;45:587-595.
    • (1982) Immunology , vol.45 , pp. 587-595
    • Discipio, R.G.1
  • 86
    • 0019440292 scopus 로고
    • Chemotactic activity generated from the fifth component of complement by plasma kallikrein of the rabbit
    • Wiggins RC, Giclas PC, Henson PM. Chemotactic activity generated from the fifth component of complement by plasma kallikrein of the rabbit. J Exp Med. 1981;153:1391-1404.
    • (1981) J Exp Med , vol.153 , pp. 1391-1404
    • Wiggins, R.C.1    Giclas, P.C.2    Henson, P.M.3
  • 88
    • 50349090460 scopus 로고    scopus 로고
    • Development of a chitosan-based wound dressing with improved hemostatic and antimicrobial properties
    • Ong SY, Wu J, Moochhala SM, Tan MH, Lu J. Development of a chitosan-based wound dressing with improved hemostatic and antimicrobial properties. Biomaterials. 2008;29:4323-4332. doi: 10.1016/j. biomaterials.2008.07.034.
    • (2008) Biomaterials , vol.29 , pp. 4323-4332
    • Ong, S.Y.1    Wu, J.2    Moochhala, S.M.3    Tan, M.H.4    Lu, J.5
  • 90
    • 52449108966 scopus 로고    scopus 로고
    • Polyphosphate as a general procoagulant agent
    • Smith SA, Morrissey JH. Polyphosphate as a general procoagulant agent. J Thromb Haemost. 2008;6:1750-1756. doi: 10.1111/j.1538-7836.2008.03104.x.
    • (2008) J Thromb Haemost , vol.6 , pp. 1750-1756
    • Smith, S.A.1    Morrissey, J.H.2
  • 91
    • 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;120:5103-5110. doi: 10.1182/blood-2012-07-444935.
    • (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.