메뉴 건너뛰기




Volumn 9, Issue 9, 2011, Pages 1791-1794

From neutrophil extracellular traps release to thrombosis: An overshooting host-defense mechanism?

Author keywords

[No Author keywords available]

Indexed keywords

ANTITHROMBIN; BLOOD CLOTTING FACTOR 12; MYELOPEROXIDASE; PROTEIN C; THROMBOMODULIN; THROMBOPLASTIN; TISSUE FACTOR PATHWAY INHIBITOR;

EID: 80052403217     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1111/j.1538-7836.2011.04425.x     Document Type: Note
Times cited : (42)

References (42)
  • 1
    • 70350512348 scopus 로고    scopus 로고
    • Coagulation and innate immune responses: can we view them separately?
    • Delvaeye M, Conway EM. Coagulation and innate immune responses: can we view them separately? Blood 2009; 114: 2367-74.
    • (2009) Blood , vol.114 , pp. 2367-2374
    • Delvaeye, M.1    Conway, E.M.2
  • 2
    • 33344468233 scopus 로고    scopus 로고
    • Neutrophils and immunity: challenges and opportunities
    • Nathan C. Neutrophils and immunity: challenges and opportunities. Nat Rev Immunol 2006; 6: 173-82.
    • (2006) Nat Rev Immunol , vol.6 , pp. 173-182
    • Nathan, C.1
  • 3
    • 77955368237 scopus 로고    scopus 로고
    • Neutrophils release brakes of coagulation
    • Ruf W, Ruggeri ZM. Neutrophils release brakes of coagulation. Nat Med 2010; 16: 851-2.
    • (2010) Nat Med , vol.16 , pp. 851-852
    • Ruf, W.1    Ruggeri, Z.M.2
  • 4
    • 34250736946 scopus 로고    scopus 로고
    • Fibrin and fibrinolysis in infection and host defense
    • Degen JL, Bugge TH, Goguen JD. Fibrin and fibrinolysis in infection and host defense. J Thromb Haemost 2007; 5(Suppl 1): 24-31.
    • (2007) J Thromb Haemost , vol.5 , Issue.SUPPL. 1 , pp. 24-31
    • Degen, J.L.1    Bugge, T.H.2    Goguen, J.D.3
  • 6
    • 2942545798 scopus 로고    scopus 로고
    • Bidirectional relation between inflammation and coagulation
    • Levi M, van der Poll T, Buller HR. Bidirectional relation between inflammation and coagulation. Circulation 2004; 109: 2698-704.
    • (2004) Circulation , vol.109 , pp. 2698-2704
    • Levi, M.1    van der Poll, T.2    Buller, H.R.3
  • 7
    • 79955706734 scopus 로고    scopus 로고
    • The hemostatic system as a modulator of atherosclerosis
    • Borissoff JI, Spronk HM, ten Cate H. The hemostatic system as a modulator of atherosclerosis. N Engl J Med 2011; 364: 1746-60.
    • (2011) N Engl J Med , vol.364 , pp. 1746-1760
    • Borissoff, J.I.1    Spronk, H.M.2    ten Cate, H.3
  • 8
    • 79952213893 scopus 로고    scopus 로고
    • The paradox of the neutrophil's role in tissue injury
    • Segel GB, Halterman MW, Lichtman MA. The paradox of the neutrophil's role in tissue injury. J Leukoc Biol 2011; 89: 359-72.
    • (2011) J Leukoc Biol , vol.89 , pp. 359-372
    • Segel, G.B.1    Halterman, M.W.2    Lichtman, M.A.3
  • 9
    • 77952426261 scopus 로고    scopus 로고
    • Role of polymorphonuclear neutrophils in atherosclerosis: current state and future perspectives
    • Baetta R, Corsini A. Role of polymorphonuclear neutrophils in atherosclerosis: current state and future perspectives. Atherosclerosis 2010; 210: 1-13.
    • (2010) Atherosclerosis , vol.210 , pp. 1-13
    • Baetta, R.1    Corsini, A.2
  • 11
    • 34247526815 scopus 로고    scopus 로고
    • Relative value of inflammatory, hemostatic, and rheological factors for incident myocardial infarction and stroke: the Edinburgh Artery Study
    • Tzoulaki I, Murray GD, Lee AJ, Rumley A, Lowe GD, Fowkes FG. Relative value of inflammatory, hemostatic, and rheological factors for incident myocardial infarction and stroke: the Edinburgh Artery Study. Circulation 2007; 115: 2119-27.
    • (2007) Circulation , vol.115 , pp. 2119-2127
    • Tzoulaki, I.1    Murray, G.D.2    Lee, A.J.3    Rumley, A.4    Lowe, G.D.5    Fowkes, F.G.6
  • 13
    • 25844477448 scopus 로고    scopus 로고
    • Pathogenesis of thrombosis in essential thrombocythemia and polycythemia vera: the role of neutrophils
    • Falanga A, Marchetti M, Barbui T, Smith CW. Pathogenesis of thrombosis in essential thrombocythemia and polycythemia vera: the role of neutrophils. Semin Hematol 2005; 42: 239-47.
    • (2005) Semin Hematol , vol.42 , pp. 239-247
    • Falanga, A.1    Marchetti, M.2    Barbui, T.3    Smith, C.W.4
  • 14
    • 80051757801 scopus 로고    scopus 로고
    • Peculiarities of cell death mechanisms in neutrophils
    • Geering B, Simon HU. Peculiarities of cell death mechanisms in neutrophils. Cell Death Differ 2011; doi.
    • (2011) Cell Death Differ
    • Geering, B.1    Simon, H.U.2
  • 16
    • 70350001718 scopus 로고    scopus 로고
    • Viable neutrophils release mitochondrial DNA to form neutrophil extracellular traps
    • Yousefi S, Mihalache C, Kozlowski E, Schmid I, Simon HU. Viable neutrophils release mitochondrial DNA to form neutrophil extracellular traps. Cell Death Differ 2009; 16: 1438-44.
    • (2009) Cell Death Differ , vol.16 , pp. 1438-1444
    • Yousefi, S.1    Mihalache, C.2    Kozlowski, E.3    Schmid, I.4    Simon, H.U.5
  • 17
    • 78049496216 scopus 로고    scopus 로고
    • Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps
    • Papayannopoulos V, Metzler KD, Hakkim A, Zychlinsky A. Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps. J Cell Biol 2010; 191: 677-91.
    • (2010) J Cell Biol , vol.191 , pp. 677-691
    • Papayannopoulos, V.1    Metzler, K.D.2    Hakkim, A.3    Zychlinsky, A.4
  • 20
    • 77955018917 scopus 로고    scopus 로고
    • Neutrophil granulocyte-dependent proteolysis enhances platelet adhesion to the arterial wall under high-shear flow
    • Wohner N, Keresztes Z, Sotonyi P, Szabo L, Komorowicz E, Machovich R, Kolev K. Neutrophil granulocyte-dependent proteolysis enhances platelet adhesion to the arterial wall under high-shear flow. J Thromb Haemost 2010; 8: 1624-31.
    • (2010) J Thromb Haemost , vol.8 , pp. 1624-1631
    • Wohner, N.1    Keresztes, Z.2    Sotonyi, P.3    Szabo, L.4    Komorowicz, E.5    Machovich, R.6    Kolev, K.7
  • 22
    • 80051884192 scopus 로고    scopus 로고
    • Extracellular histones promote thrombin generation through platelet-dependent mechanisms: involvement of platelet TLR2 and 4
    • in press.
    • 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 4. Blood 2011; in press.
    • (2011) Blood
    • 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
  • 25
    • 0020362213 scopus 로고
    • Proteolytic cleavage and inactivation of alpha 2-plasmin inhibitor and C1 inactivator by human polymorphonuclear leukocyte elastase
    • Brower MS, Harpel PC. Proteolytic cleavage and inactivation of alpha 2-plasmin inhibitor and C1 inactivator by human polymorphonuclear leukocyte elastase. J Biol Chem 1982; 257: 9849-54.
    • (1982) J Biol Chem , vol.257 , pp. 9849-9854
    • Brower, M.S.1    Harpel, P.C.2
  • 28
    • 0037646493 scopus 로고    scopus 로고
    • Neutrophil cathepsin G promotes prothrombinase and fibrin formation under flow conditions by activating fibrinogen-adherent platelets
    • Goel MS, Diamond SL. Neutrophil cathepsin G promotes prothrombinase and fibrin formation under flow conditions by activating fibrinogen-adherent platelets. J Biol Chem 2003; 278: 9458-63.
    • (2003) J Biol Chem , vol.278 , pp. 9458-9463
    • Goel, M.S.1    Diamond, S.L.2
  • 31
    • 0026594204 scopus 로고
    • The effect of leukocyte elastase on tissue factor pathway inhibitor
    • Higuchi DA, Wun TC, Likert KM, Broze GJ Jr. The effect of leukocyte elastase on tissue factor pathway inhibitor. Blood 1992; 79: 1712-9.
    • (1992) Blood , vol.79 , pp. 1712-1719
    • Higuchi, D.A.1    Wun, T.C.2    Likert, K.M.3    Broze Jr, G.J.4
  • 32
    • 0023227857 scopus 로고
    • Heparin promotes the inactivation of antithrombin by neutrophil elastase
    • Jordan RE, Kilpatrick J, Nelson RM. Heparin promotes the inactivation of antithrombin by neutrophil elastase. Science 1987; 237: 777-9.
    • (1987) Science , vol.237 , pp. 777-779
    • Jordan, R.E.1    Kilpatrick, J.2    Nelson, R.M.3
  • 36
    • 80052395881 scopus 로고    scopus 로고
    • Extracellular histones increase plasma thrombin generation by impairing thrombomodulin-dependent protein C activation
    • Ammollo CT, Semeraro F, Xu J, Esmon NL, Esmon CT. Extracellular histones increase plasma thrombin generation by impairing thrombomodulin-dependent protein C activation. J Thromb Haemost 2011; 9: 1795-803.
    • (2011) J Thromb Haemost , vol.9 , pp. 1795-1803
    • Ammollo, C.T.1    Semeraro, F.2    Xu, J.3    Esmon, N.L.4    Esmon, C.T.5
  • 42
    • 77950666255 scopus 로고    scopus 로고
    • Proteomic identification of interactions between histones and plasma proteins: implications for cytoprotection
    • Pemberton AD, Brown JK, Inglis NF. Proteomic identification of interactions between histones and plasma proteins: implications for cytoprotection. Proteomics 2010; 10: 1484-93.
    • (2010) Proteomics , vol.10 , pp. 1484-1493
    • Pemberton, A.D.1    Brown, J.K.2    Inglis, N.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.