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Volumn 91, Issue 2, 1998, Pages 516-528

High molecular weight kininogen regulates prekallikrein assembly and activation on endothelial cells: A novel mechanism for contact activation

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 12; KALLIKREIN; KININOGEN; PLASMIN; PLASMINOGEN; PREKALLIKREIN; PROUROKINASE; THIOL PROTEINASE;

EID: 0031973492     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v91.2.516.516_516_528     Document Type: Article
Times cited : (169)

References (54)
  • 1
    • 0020565895 scopus 로고
    • Thrombosis or myocardial infarction in congenital clotting factor abnormalities and chronic thrombocytopenias: A report of 21 patients and a review of 50 previously reported cases
    • Goodnough LT, Saito H, Ratnoff OD: Thrombosis or myocardial infarction in congenital clotting factor abnormalities and chronic thrombocytopenias: a report of 21 patients and a review of 50 previously reported cases. Medicine 62:248, 1983
    • (1983) Medicine , vol.62 , pp. 248
    • Goodnough, L.T.1    Saito, H.2    Ratnoff, O.D.3
  • 2
    • 0028054973 scopus 로고
    • The prevalence of moderate and severe factor XII (Hageman factor) deficiency among the normal population: Evaluation of the incidence of factor XII deficiency among 300 healthy blood donors
    • Halbmayer WM, Haushofer A, Schon A, Mannhalter C, Stromer E, Baumgarter K, Fischer M: The prevalence of moderate and severe factor XII (Hageman factor) deficiency among the normal population: Evaluation of the incidence of factor XII deficiency among 300 healthy blood donors. Thromb Haemost 71:68, 1994
    • (1994) Thromb Haemost , vol.71 , pp. 68
    • Halbmayer, W.M.1    Haushofer, A.2    Schon, A.3    Mannhalter, C.4    Stromer, E.5    Baumgarter, K.6    Fischer, M.7
  • 3
    • 0026065260 scopus 로고
    • Thromboembolism and bleeding tendency in congenital factor XII deficiency-A study on 74 subjects from 14 Swiss families
    • Lammle B, Wuillemin WA, Huber I, Krauskopf M, Zurcher C, Pflugshaupt R, Furlan M: Thromboembolism and bleeding tendency in congenital factor XII deficiency-A study on 74 subjects from 14 Swiss families. Thromb Haemost 65:117, 1991
    • (1991) Thromb Haemost , vol.65 , pp. 117
    • Lammle, B.1    Wuillemin, W.A.2    Huber, I.3    Krauskopf, M.4    Zurcher, C.5    Pflugshaupt, R.6    Furlan, M.7
  • 4
    • 0026803207 scopus 로고
    • The prevalence of factor XII deficiency in 103 orally anticoagulated outpatients suffering from recurrent venous and/or arterial thromboembolism
    • Halbmayer WM, Mannhalter C, Feichtinger C, Rubi K, Fisher M: The prevalence of factor XII deficiency in 103 orally anticoagulated outpatients suffering from recurrent venous and/or arterial thromboembolism. Thromb Haemost 68:285, 1992
    • (1992) Thromb Haemost , vol.68 , pp. 285
    • Halbmayer, W.M.1    Mannhalter, C.2    Feichtinger, C.3    Rubi, K.4    Fisher, M.5
  • 5
    • 0026458603 scopus 로고
    • Factor XII clotting activity and antigen levels in patients with thromboembolic disease
    • Von Kanel R, Wuillemin WA, Furlan M, Lammle B: Factor XII clotting activity and antigen levels in patients with thromboembolic disease. Blood Coag Fibrinol 3:555, 1992
    • (1992) Blood Coag Fibrinol , vol.3 , pp. 555
    • Von Kanel, R.1    Wuillemin, W.A.2    Furlan, M.3    Lammle, B.4
  • 6
    • 0027057953 scopus 로고
    • Evidence for a role of factor XII-dependent fibrinolysis in cardiovascular diseases
    • Jespersen J, Munkvad S, Pedersen OD, Gram J: Evidence for a role of factor XII-dependent fibrinolysis in cardiovascular diseases. Ann NY Acad Sci 667:454, 1992
    • (1992) Ann NY Acad Sci , vol.667 , pp. 454
    • Jespersen, J.1    Munkvad, S.2    Pedersen, O.D.3    Gram, J.4
  • 7
    • 44949281924 scopus 로고
    • Long-lasting depression of the factor XII-dependent fibrinolytic system in patients with myocardial infarction undergoing thrombolytic therapy with recombinant tissue-type plasminogen activator: A randomized placebo-controlled study
    • Munkvad S, Jespersen J, Gram J, Kluft C: Long-lasting depression of the factor XII-dependent fibrinolytic system in patients with myocardial infarction undergoing thrombolytic therapy with recombinant tissue-type plasminogen activator: A randomized placebo-controlled study. J Am College Cardiol 17:957, 1991
    • (1991) J Am College Cardiol , vol.17 , pp. 957
    • Munkvad, S.1    Jespersen, J.2    Gram, J.3    Kluft, C.4
  • 9
    • 0026050749 scopus 로고
    • Reduction of contact activation related fibrinolytic activity in factor XII deficient patients. Further evidence for the role of the contact system in fibrinolysis in vivo
    • Levi M, Hack CE, de Boer JP, Brandjes DPM, Buller HR, ten Cate JW: Reduction of contact activation related fibrinolytic activity in factor XII deficient patients. Further evidence for the role of the contact system in fibrinolysis in vivo. J Clin Invest 88:1155, 1991
    • (1991) J Clin Invest , vol.88 , pp. 1155
    • Levi, M.1    Hack, C.E.2    De Boer, J.P.3    Brandjes, D.P.M.4    Buller, H.R.5    Ten Cate, J.W.6
  • 10
    • 0014694698 scopus 로고
    • Activation of plasminogen by human plasma kallikrein
    • Colman RW: Activation of plasminogen by human plasma kallikrein. Biochem Biophys Res Commun 35:273, 1969
    • (1969) Biochem Biophys Res Commun , vol.35 , pp. 273
    • Colman, R.W.1
  • 11
    • 0017738854 scopus 로고
    • Hageman factor substrates. Human plasma prekallikrein: Mechanism of activation by Hageman factor and participation in Hageman-factor-dependent fibrinolysis
    • Mandle RJ Jr, Kaplan AP: Hageman factor substrates. Human plasma prekallikrein: Mechanism of activation by Hageman factor and participation in Hageman-factor-dependent fibrinolysis. J Biol Chem 252:6097, 1977
    • (1977) J Biol Chem , vol.252 , pp. 6097
    • Mandle Jr., R.J.1    Kaplan, A.P.2
  • 12
    • 0018103306 scopus 로고
    • The activation of plasminogen by Hageman factor (factor XII) and Hageman factor fragments
    • Goldsmith G, Saito H, Ratnoff OD: The activation of plasminogen by Hageman factor (factor XII) and Hageman factor fragments. J Clin Invest 62:54, 1978
    • (1978) J Clin Invest , vol.62 , pp. 54
    • Goldsmith, G.1    Saito, H.2    Ratnoff, O.D.3
  • 13
    • 0018716550 scopus 로고
    • Hageman-factor-dependent fibrinolysis: Generation of fibrinolytic activity by the interaction of human activated factor XI and plasminogen
    • Mandle RJ Jr, Kaplan AP: Hageman-factor-dependent fibrinolysis: Generation of fibrinolytic activity by the interaction of human activated factor XI and plasminogen. Blood 54:850, 1979
    • (1979) Blood , vol.54 , pp. 850
    • Mandle Jr., R.J.1    Kaplan, A.P.2
  • 14
    • 0020673587 scopus 로고
    • A comparison of the abilities of plasma kallikrein, beta-factor XIIa, factor XIa and urokinase to activate plasminogen
    • Miles LA, Greengard JS, Griffin JH: A comparison of the abilities of plasma kallikrein, beta-factor XIIa, factor XIa and urokinase to activate plasminogen. Thromb Res 29:407, 1983
    • (1983) Thromb Res , vol.29 , pp. 407
    • Miles, L.A.1    Greengard, J.S.2    Griffin, J.H.3
  • 15
    • 0023022473 scopus 로고
    • The activation of prourokinase by plasma kallikrein and its inactivation by thrombin
    • Ichinose A, Fujikawa K, Suyama T: The activation of prourokinase by plasma kallikrein and its inactivation by thrombin. J Biol Chem 261:3486, 1986
    • (1986) J Biol Chem , vol.261 , pp. 3486
    • Ichinose, A.1    Fujikawa, K.2    Suyama, T.3
  • 16
    • 0027419518 scopus 로고
    • Pro-urokinase and prekallikrein are both associated with platelets. Implications for the intrinsic pathway of fibrinolysis and for therapeutic thrombolysis
    • Gurewich V, Johnstone M, Loza J-P, Pannell R: Pro-urokinase and prekallikrein are both associated with platelets. Implications for the intrinsic pathway of fibrinolysis and for therapeutic thrombolysis. FEES Lett 318:317, 1993
    • (1993) FEES Lett , vol.318 , pp. 317
    • Gurewich, V.1    Johnstone, M.2    Loza, J.-P.3    Pannell, R.4
  • 17
    • 0028211344 scopus 로고
    • Platelet-bound prekallikrein promotes pro-urokinase-induced clot lysis: A mechanism for targeting the factor XII dependent intrinsic pathway of fibrinolysis
    • Loza J-P, Gurewich V, Johnstone M, Pannell R: Platelet-bound prekallikrein promotes pro-urokinase-induced clot lysis: a mechanism for targeting the factor XII dependent intrinsic pathway of fibrinolysis. Thromb Haemost 71:347, 1994
    • (1994) Thromb Haemost , vol.71 , pp. 347
    • Loza, J.-P.1    Gurewich, V.2    Johnstone, M.3    Pannell, R.4
  • 18
    • 0029028074 scopus 로고
    • Assembly and activation of the intrinsic fibrinolytic pathway on the surface of human endothelial cells in culture
    • Lenich C, Pannell R, Gurewich V: Assembly and activation of the intrinsic fibrinolytic pathway on the surface of human endothelial cells in culture. Thromb Haemost 74:698, 1995
    • (1995) Thromb Haemost , vol.74 , pp. 698
    • Lenich, C.1    Pannell, R.2    Gurewich, V.3
  • 19
    • 0021739735 scopus 로고
    • Receptors for high molecular weight kininogen on stimulated washed human platelets
    • Greengard JS, Griffin JH: Receptors for high molecular weight kininogen on stimulated washed human platelets. Biochemistry 23: 6863, 1984
    • (1984) Biochemistry , vol.23 , pp. 6863
    • Greengard, J.S.1    Griffin, J.H.2
  • 21
    • 0023797442 scopus 로고
    • Expression of high molecular weight kininogen on human umbilical vein endothelial cells
    • Schmaier AH, Kuo A, Lundberg D, Murray S, Cines DB: Expression of high molecular weight kininogen on human umbilical vein endothelial cells. J Biol Chem 263:16327, 1988
    • (1988) J Biol Chem , vol.263 , pp. 16327
    • Schmaier, A.H.1    Kuo, A.2    Lundberg, D.3    Murray, S.4    Cines, D.B.5
  • 22
    • 0023926495 scopus 로고
    • The binding of high molecular weight kininogen to cultured human endothelial cells
    • Van Iwaarden F, de Groot PG, Bouma BN: The binding of high molecular weight kininogen to cultured human endothelial cells. J Biol Chem 263:4698, 1988
    • (1988) J Biol Chem , vol.263 , pp. 4698
    • Van Iwaarden, F.1    De Groot, P.G.2    Bouma, B.N.3
  • 23
    • 0025834590 scopus 로고
    • Low molecular weight kininogen binds to platelets to modulate thrombin-induced platelet activation
    • Meloni FJ, Schmaier AH: Low molecular weight kininogen binds to platelets to modulate thrombin-induced platelet activation. J Biol Chem 266:6786, 1991
    • (1991) J Biol Chem , vol.266 , pp. 6786
    • Meloni, F.J.1    Schmaier, A.H.2
  • 24
    • 0026784525 scopus 로고
    • Domain 3 of kininogens contains a cell binding site and a site that modifies thrombin activation of platelets
    • Jiang Y, Muller-Esterl W, Schmaier AH: Domain 3 of kininogens contains a cell binding site and a site that modifies thrombin activation of platelets. J Biol Chem 267:3712, 1992
    • (1992) J Biol Chem , vol.267 , pp. 3712
    • Jiang, Y.1    Muller-Esterl, W.2    Schmaier, A.H.3
  • 25
    • 0029076637 scopus 로고
    • High molecular weight kininogen is exclusively membrane bound on endothelial cells to influence activation of vascular endothelial cells
    • Hasan AAK, Cines DB, Ngaiza JR, Jaffe EA, Schmaier AH: High molecular weight kininogen is exclusively membrane bound on endothelial cells to influence activation of vascular endothelial cells. Blood 85:3134, 1995
    • (1995) Blood , vol.85 , pp. 3134
    • Hasan, A.A.K.1    Cines, D.B.2    Ngaiza, J.R.3    Jaffe, E.A.4    Schmaier, A.H.5
  • 26
    • 0028034957 scopus 로고
    • The C-terminus of bradykinin and N-terminus of the light chain of kininogens comprise an endothelial cell binding domain
    • Hasan AAK, Cines DB, Zhang J, Schmaier AH: The C-terminus of bradykinin and N-terminus of the light chain of kininogens comprise an endothelial cell binding domain. J Biol Chem 269;31822, 1994
    • (1994) J Biol Chem , vol.269 , pp. 31822
    • Hasan, A.A.K.1    Cines, D.B.2    Zhang, J.3    Schmaier, A.H.4
  • 29
    • 0017149563 scopus 로고
    • Identification of prekallikrein and high molecular weight kininogen as a complex in human plasma
    • Mandle R Jr, Colman RW, Kaplan AP: Identification of prekallikrein and high molecular weight kininogen as a complex in human plasma. Proc Natl Acad Sci USA 73:4179, 1976
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 4179
    • Mandle Jr., R.1    Colman, R.W.2    Kaplan, A.P.3
  • 30
    • 0018842614 scopus 로고
    • Function and immunochemistry of prekallikrein-high molecular weight kininogen complex in plasma
    • Scott CF, Colman RW: Function and immunochemistry of prekallikrein-high molecular weight kininogen complex in plasma. J Clin Invest 65:413, 1980
    • (1980) J Clin Invest , vol.65 , pp. 413
    • Scott, C.F.1    Colman, R.W.2
  • 31
    • 0023003707 scopus 로고
    • Identification of the binding site for plasma prekallikrein in human high molecular weight kininogen. a region from residues 185 to 224 of the kininogen light chain retains full binding activity
    • Tait JF, Fujikawa K: Identification of the binding site for plasma prekallikrein in human high molecular weight kininogen. A region from residues 185 to 224 of the kininogen light chain retains full binding activity. J Biol Chem 261:15396, 1986
    • (1986) J Biol Chem , vol.261 , pp. 15396
    • Tait, J.F.1    Fujikawa, K.2
  • 32
    • 0027212538 scopus 로고
    • Human Hageman factor (factor XII) and high molecular weight kininogen compete for the same binding site on human umbilical vein endothelial cells
    • Reddigari SR, Shibayama Y, Brunnee T, Kaplan AP: Human Hageman factor (factor XII) and high molecular weight kininogen compete for the same binding site on human umbilical vein endothelial cells. J Biol Chem 268:11982, 1993
    • (1993) J Biol Chem , vol.268 , pp. 11982
    • Reddigari, S.R.1    Shibayama, Y.2    Brunnee, T.3    Kaplan, A.P.4
  • 33
    • 0020055028 scopus 로고
    • Assay of prekallikrein: Comparison of amidolytic, esterolytic, coagulation and immunochemical assays
    • Fisher CA, Schmaier AH, Addonizio VP, Colman RW: Assay of prekallikrein: Comparison of amidolytic, esterolytic, coagulation and immunochemical assays. Blood 59:963, 1982
    • (1982) Blood , vol.59 , pp. 963
    • Fisher, C.A.1    Schmaier, A.H.2    Addonizio, V.P.3    Colman, R.W.4
  • 34
    • 0021893770 scopus 로고
    • Platelet C1 inhibitor: A secreted alpha granule protein
    • Schmaier AH, Smith PM, Colman RW: Platelet C1 inhibitor: A secreted alpha granule protein. J Clin Invest 75:242, 1985
    • (1985) J Clin Invest , vol.75 , pp. 242
    • Schmaier, A.H.1    Smith, P.M.2    Colman, R.W.3
  • 35
    • 0027418773 scopus 로고
    • Structural dissection of the multidomain kininogens. Fine mapping of the target epitopes of antibodies interfering with their functional properties
    • Kaufmann J, Haasemann M, Modrow S, Muller-Esterl W: Structural dissection of the multidomain kininogens. Fine mapping of the target epitopes of antibodies interfering with their functional properties. J Biol Chem 268:9079, 1993
    • (1993) J Biol Chem , vol.268 , pp. 9079
    • Kaufmann, J.1    Haasemann, M.2    Modrow, S.3    Muller-Esterl, W.4
  • 36
    • 0025368839 scopus 로고
    • High molecular weight kininogen-binding site of prekallikrein probed by monoclonal antibodies
    • Hock J, Vogel R, Linke RP, Muller-Esterl W: High molecular weight kininogen-binding site of prekallikrein probed by monoclonal antibodies. J Biol Chem 265:12005, 1990
    • (1990) J Biol Chem , vol.265 , pp. 12005
    • Hock, J.1    Vogel, R.2    Linke, R.P.3    Muller-Esterl, W.4
  • 37
    • 0026488297 scopus 로고
    • Human plasma kallikrein processing: Proteolysis as an alternative control
    • Motta G, Fink E, Sampaio MV, Sampaio CAM: Human plasma kallikrein processing: proteolysis as an alternative control. Agents Actions Suppl 38:265, 1992
    • (1992) Agents Actions Suppl , vol.38 , pp. 265
    • Motta, G.1    Fink, E.2    Sampaio, M.V.3    Sampaio, C.A.M.4
  • 38
    • 0024601825 scopus 로고
    • Platelet high molecular weight kininogen: Identification and mechanisms of availability
    • Schmaier AH, Colman RW: Platelet high molecular weight kininogen: Identification and mechanisms of availability. Methods Enzymol 169:276, 1989
    • (1989) Methods Enzymol , vol.169 , pp. 276
    • Schmaier, A.H.1    Colman, R.W.2
  • 39
    • 0028879618 scopus 로고
    • Conformational changes in low molecular weight kininogen alters its ability to bind to endothelial cells
    • Hasan AAK, Zhang J, Samuels M, Schmaier AH: Conformational changes in low molecular weight kininogen alters its ability to bind to endothelial cells. Thromb Haemost 74:1088, 1995
    • (1995) Thromb Haemost , vol.74 , pp. 1088
    • Hasan, A.A.K.1    Zhang, J.2    Samuels, M.3    Schmaier, A.H.4
  • 40
    • 0021090449 scopus 로고
    • Protein-protein interactions in contact activation of blood coagulation. Characterization of ftuorescein-labeled human high molecular weight kininogen-light chain as a probe
    • Bock PE, Shore JD: Protein-protein interactions in contact activation of blood coagulation. Characterization of ftuorescein-labeled human high molecular weight kininogen-light chain as a probe. J Biol Chem 258:15079, 1983
    • (1983) J Biol Chem , vol.258 , pp. 15079
    • Bock, P.E.1    Shore, J.D.2
  • 41
    • 78651196598 scopus 로고
    • A spectrophotometric assay for avidin and biotin on binding of dyes by avidin
    • Green NM: A spectrophotometric assay for avidin and biotin on binding of dyes by avidin. Biochem J 94:23, 1965
    • (1965) Biochem J , vol.94 , pp. 23
    • Green, N.M.1
  • 42
    • 84969001783 scopus 로고
    • The attraction of proteins for small molecules and ions
    • Scatchard G: The attraction of proteins for small molecules and ions. Ann NY Acad Sci 51:660, 1949
    • (1949) Ann NY Acad Sci , vol.51 , pp. 660
    • Scatchard, G.1
  • 43
    • 0020971366 scopus 로고
    • Determination of affinity and specificity of anti-hapten antibodies by competitive radioimmunoassay
    • Müller R: Determination of affinity and specificity of anti-hapten antibodies by competitive radioimmunoassay. Methods Enzymol 92: 589, 1983
    • (1983) Methods Enzymol , vol.92 , pp. 589
    • Müller, R.1
  • 44
    • 0023684099 scopus 로고
    • Structural changes of plasma high molecular weight kininogen afterin vitro activation and, in sepsis
    • Schmaier AH, Farber A, Schein R, Sprung C: Structural changes of plasma high molecular weight kininogen afterin vitro activation and, in sepsis. J Lab Clin Med 112:182, 1988
    • (1988) J Lab Clin Med , vol.112 , pp. 182
    • Schmaier, A.H.1    Farber, A.2    Schein, R.3    Sprung, C.4
  • 46
    • 0022407110 scopus 로고
    • Protein-protein interactions in contact activation of blood coagulation. Binding of high molecular weight kininogen and the 5-(iodoacetamido) fluorescein-labeled kininogen light chain to prekallikrein, kallikrein, and the separated kallikrein heavy and light chains
    • Bock PE, Shore JD, Tans G, Griffin JH: Protein-protein interactions in contact activation of blood coagulation. Binding of high molecular weight kininogen and the 5-(iodoacetamido) fluorescein-labeled kininogen light chain to prekallikrein, kallikrein, and the separated kallikrein heavy and light chains. J Biol Chem 260:12434, 1985
    • (1985) J Biol Chem , vol.260 , pp. 12434
    • Bock, P.E.1    Shore, J.D.2    Tans, G.3    Griffin, J.H.4
  • 47
    • 0025122795 scopus 로고
    • Kinetics of inhibition of platelet calpain II by human kininogens
    • Bradford HN, Schmaier AH, Colman RW: Kinetics of inhibition of platelet calpain II by human kininogens. Biochem J 270:83, 1990
    • (1990) Biochem J , vol.270 , pp. 83
    • Bradford, H.N.1    Schmaier, A.H.2    Colman, R.W.3
  • 48
    • 0018913292 scopus 로고
    • Activation of rabbit Hageman factor by homogenates of cultured rabbit endothelial cells
    • Wiggins RC, Loskutoff DJ, Cochrane CG, Girffin JH: Activation of rabbit Hageman factor by homogenates of cultured rabbit endothelial cells. J Clin Invest 65:197, 1980
    • (1980) J Clin Invest , vol.65 , pp. 197
    • Wiggins, R.C.1    Loskutoff, D.J.2    Cochrane, C.G.3    Girffin, J.H.4
  • 49
    • 0026516038 scopus 로고
    • High molecular weight kininogen binds to platelets by its heavy and light chains and when bound has altered susceptibility to kallikrein cleavage
    • Meloni FJ, Gustafson EJ, Schmaier AH: High molecular weight kininogen binds to platelets by its heavy and light chains and when bound has altered susceptibility to kallikrein cleavage. Blood 79:1233, 1992
    • (1992) Blood , vol.79 , pp. 1233
    • Meloni, F.J.1    Gustafson, E.J.2    Schmaier, A.H.3
  • 50
    • 84931128415 scopus 로고
    • Bradykinin, hypotensive and smooth muscle stimulator released from plasma globulin by snake venoms and by trypsin
    • Rocha E, Suva M, Beraldo WT, Rosenfeld G: Bradykinin, hypotensive and smooth muscle stimulator released from plasma globulin by snake venoms and by trypsin. Am J Physiol 156:261, 1949
    • (1949) Am J Physiol , vol.156 , pp. 261
    • Rocha, E.1    Suva, M.2    Beraldo, W.T.3    Rosenfeld, G.4
  • 51
    • 0021930258 scopus 로고
    • Tissue plasminogen activator release in vivo in response to vasoactive agents
    • Smith D, Gilbert M, Owen WG: Tissue plasminogen activator release in vivo in response to vasoactive agents. Blood 66:835, 1983
    • (1983) Blood , vol.66 , pp. 835
    • Smith, D.1    Gilbert, M.2    Owen, W.G.3
  • 52
    • 0030951836 scopus 로고    scopus 로고
    • Selective stimulation of tissue-type plasminogen activator (t-PA) in vivo by infusion of bradykinin
    • Brown NJ, Nadeau JH, Vaughan DE: Selective stimulation of tissue-type plasminogen activator (t-PA) in vivo by infusion of bradykinin. Thromb Haemost 77:522, 1997
    • (1997) Thromb Haemost , vol.77 , pp. 522
    • Brown, N.J.1    Nadeau, J.H.2    Vaughan, D.E.3
  • 53
    • 0029102856 scopus 로고
    • Gene targeting and gene transfer studies of the plasminogen/plasmin system: Implications in thrombosis, hemostasis, neointima formation, and atherosclerosis
    • Carmeliet P, Collen D: Gene targeting and gene transfer studies of the plasminogen/plasmin system: Implications in thrombosis, hemostasis, neointima formation, and atherosclerosis. FASEB J 9:934, 1995
    • (1995) FASEB J , vol.9 , pp. 934
    • Carmeliet, P.1    Collen, D.2
  • 54
    • 0029149373 scopus 로고
    • Enhancement of the enzymatic activity of single-chain urokinase plasminogen activator by soluble urokinase receptor
    • Higazi A, Cohen RL, Henkin J, Kniss D, Schwartz BS, Cines DB Enhancement of the enzymatic activity of single-chain urokinase plasminogen activator by soluble urokinase receptor. J Biol Chem 270:17375, 1995
    • (1995) J Biol Chem , vol.270 , pp. 17375
    • Higazi, A.1    Cohen, R.L.2    Henkin, J.3    Kniss, D.4    Schwartz, B.S.5    Cines, D.B.6


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