메뉴 건너뛰기




Volumn 86, Issue , 2005, Pages 159-208

Formation of bradykinin: A major contributor to the innate inflammatory response

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 11; BLOOD CLOTTING FACTOR 12; BLOOD CLOTTING FACTOR 12A; BRADYKININ; CELL SURFACE PROTEIN; CYTOKERATIN 1; HEAT SHOCK PROTEIN 90; HIGH MOLECULAR WEIGHT KININOGEN; KALLIKREIN; KININ; KININOGEN; PLASMA PROTEIN; PREKALLIKREIN; UROKINASE RECEPTOR;

EID: 13444267658     PISSN: 00652776     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0065-2776(04)86005-X     Document Type: Article
Times cited : (122)

References (246)
  • 2
    • 0018935149 scopus 로고
    • Contact-activated factors: Contaminants of immunoglobulins preparations with coagulant and vasoactive properties
    • Alving B.M., Tankersley D.L., Mason B.L., Rossi F., Aronson D.L., Finlayson J.S. Contact-activated factors: Contaminants of immunoglobulins preparations with coagulant and vasoactive properties. J. Lab. Clin. Med. 96:1980;334-346
    • (1980) J. Lab. Clin. Med. , vol.96 , pp. 334-346
    • Alving, B.M.1    Tankersley, D.L.2    Mason, B.L.3    Rossi, F.4    Aronson, D.L.5    Finlayson, J.S.6
  • 3
    • 0023270172 scopus 로고
    • Activation of plasma Hageman factor and kallikrein in ongoing allergic reactions in the skin
    • Atkins P.C., Miragliotta G., Talbot S.F., Zweiman B., Kaplan A.P. Activation of plasma Hageman factor and kallikrein in ongoing allergic reactions in the skin. J. Immunol. 139:1987;2744-2748
    • (1987) J. Immunol. , vol.139 , pp. 2744-2748
    • Atkins, P.C.1    Miragliotta, G.2    Talbot, S.F.3    Zweiman, B.4    Kaplan, A.P.5
  • 5
    • 0034617092 scopus 로고    scopus 로고
    • Thrombin-mediated feedback activation of factor XI on the activated platelet surface is preferred over contact activation by factor XIIa or factor XIa
    • Baglia F.A., Walsh P.N. Thrombin-mediated feedback activation of factor XI on the activated platelet surface is preferred over contact activation by factor XIIa or factor XIa. J. Biol. Chem. 275:2000;20514-20519
    • (2000) J. Biol. Chem. , vol.275 , pp. 20514-20519
    • Baglia, F.A.1    Walsh, P.N.2
  • 6
    • 0037127251 scopus 로고    scopus 로고
    • Factor XI binding to the platelet glycoprotein Ib-IX-V complex promotes factor XI activation by thrombin
    • Baglia F.A., Badellino K.O., Li C.Q., Lopez J.A., Walsh P.N. Factor XI binding to the platelet glycoprotein Ib-IX-V complex promotes factor XI activation by thrombin. J. Biol. Chem. 277:2002;1662-1668
    • (2002) J. Biol. Chem. , vol.277 , pp. 1662-1668
    • Baglia, F.A.1    Badellino, K.O.2    Li, C.Q.3    Lopez, J.A.4    Walsh, P.N.5
  • 7
    • 0037047344 scopus 로고    scopus 로고
    • Activated platelets but not endothelial cells participate in the initiation of the consolidation phase of blood coagulation
    • Baird T.R., Walsh P.N. Activated platelets but not endothelial cells participate in the initiation of the consolidation phase of blood coagulation. J. Biol. Chem. 277:2002;28498-28503
    • (2002) J. Biol. Chem. , vol.277 , pp. 28498-28503
    • Baird, T.R.1    Walsh, P.N.2
  • 8
    • 0038419658 scopus 로고    scopus 로고
    • Factor XI, but not prekallikrein, blocks high molecular weight kininogen binding to human umbilical vein endothelial cells
    • Baird T.R., Walsh P.N. Factor XI, but not prekallikrein, blocks high molecular weight kininogen binding to human umbilical vein endothelial cells. J. Biol. Chem. 278:2003;20618-20623
    • (2003) J. Biol. Chem. , vol.278 , pp. 20618-20623
    • Baird, T.R.1    Walsh, P.N.2
  • 9
    • 0029044322 scopus 로고
    • Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor
    • Bajzar L., Manuel R., Nesheim M.E. Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor. J. Biol. Chem. 270:1995;14477-14484
    • (1995) J. Biol. Chem. , vol.270 , pp. 14477-14484
    • Bajzar, L.1    Manuel, R.2    Nesheim, M.E.3
  • 10
    • 0029895009 scopus 로고    scopus 로고
    • TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex
    • Bajzar L., Morser J., Nesheim M. TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex. J. Biol. Chem. 271:1996;16603-16608
    • (1996) J. Biol. Chem. , vol.271 , pp. 16603-16608
    • Bajzar, L.1    Morser, J.2    Nesheim, M.3
  • 11
    • 0015896128 scopus 로고
    • 2-macroglobulin with proteinases: Characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanism
    • 2- macroglobulin with proteinases: Characteristics and specificity of the reaction, and a hypothesis concerning its molecular mechanism. Biochem. J. 133:1973;709-724
    • (1973) Biochem. J. , vol.133 , pp. 709-724
    • Barrett, A.J.1    Starkey, P.M.2
  • 13
    • 0022472021 scopus 로고
    • Plasma kallikrein during experimentally induced allergic rhinitis: Role in kinin formation and contribution to TAME-esterase activity in nasal secretions
    • Baumgarten C.R., Nichols R.C., Naclerio R.M., Lichtenstein L.M., Norman P.S., Proud D. Plasma kallikrein during experimentally induced allergic rhinitis: Role in kinin formation and contribution to TAME-esterase activity in nasal secretions. J. Immunol. 137:1986a;977-982
    • (1986) J. Immunol. , vol.137 , pp. 977-982
    • Baumgarten, C.R.1    Nichols, R.C.2    Naclerio, R.M.3    Lichtenstein, L.M.4    Norman, P.S.5    Proud, D.6
  • 14
    • 0022516952 scopus 로고
    • Concentrations of glandular kallikrein in human nasal secretions increase during experimentally induced allergic rhinitis
    • Baumgarten C.R., Nichols R.C., Naclerio R.M., Proud D. Concentrations of glandular kallikrein in human nasal secretions increase during experimentally induced allergic rhinitis. J. Immunol. 137:1986b;1323-1328
    • (1986) J. Immunol. , vol.137 , pp. 1323-1328
    • Baumgarten, C.R.1    Nichols, R.C.2    Naclerio, R.M.3    Proud, D.4
  • 15
    • 0022544926 scopus 로고
    • Interaction of factor XIa and antithrombin in the presence and absence of heparin
    • Beeler D.L., Marcum J.A., Schiffman S., Rosenberg R.D. Interaction of factor XIa and antithrombin in the presence and absence of heparin. Blood. 67:1986;1488-1492
    • (1986) Blood , vol.67 , pp. 1488-1492
    • Beeler, D.L.1    Marcum, J.A.2    Schiffman, S.3    Rosenberg, R.D.4
  • 17
    • 0033875539 scopus 로고    scopus 로고
    • Role of blood coagulation factor XI in downregulation of fibrinolysis
    • Bouma B.N., Meijers J.C. Role of blood coagulation factor XI in downregulation of fibrinolysis. Curr. Opin. Hematol. 7:2000;266-272
    • (2000) Curr. Opin. Hematol. , vol.7 , pp. 266-272
    • Bouma, B.N.1    Meijers, J.C.2
  • 18
    • 0030749223 scopus 로고    scopus 로고
    • Human kininogens regulate thrombin binding to platelets through the glycoprotein Ib-IX-V complex
    • Bradford H.N., Dela Cadena R.A., Kunapuli S.P., Dong J.F., Lopez J.A., Colman R.W. Human kininogens regulate thrombin binding to platelets through the glycoprotein Ib-IX-V complex. Blood. 90:1997;1508-1515
    • (1997) Blood , vol.90 , pp. 1508-1515
    • Bradford, H.N.1    Dela Cadena, R.A.2    Kunapuli, S.P.3    Dong, J.F.4    Lopez, J.A.5    Colman, R.W.6
  • 19
    • 0021339934 scopus 로고
    • Factor XII and prekallikrein-kallikrein-kinin in the cryoactivation of human plasma prorenin
    • Brown C.F., Osmond D.H. Factor XII and prekallikrein-kallikrein-kinin in the cryoactivation of human plasma prorenin. Clin. Sci. 66:1984;533-539
    • (1984) Clin. Sci. , vol.66 , pp. 533-539
    • Brown, C.F.1    Osmond, D.H.2
  • 21
    • 0030851598 scopus 로고    scopus 로고
    • Mast cell derived heparin activates the contact system: A link to kinin generation in allergic reactions
    • Brunnee T., Reddigari S.R., Shibayama Y., Kaplan A.P., Silverberg M. Mast cell derived heparin activates the contact system: A link to kinin generation in allergic reactions. Clin. Exp. Allergy. 27:1997;653-663
    • (1997) Clin. Exp. Allergy , vol.27 , pp. 653-663
    • Brunnee, T.1    Reddigari, S.R.2    Shibayama, Y.3    Kaplan, A.P.4    Silverberg, M.5
  • 23
    • 0017287389 scopus 로고
    • Angiotensin-converting enzyme: Vascular endothelial localization
    • Caldwell P.R., Seegal B.C., Hsu K.C., Das M., Soffer R.L. Angiotensin-converting enzyme: Vascular endothelial localization. Science. 191:1976;1050-1051
    • (1976) Science , vol.191 , pp. 1050-1051
    • Caldwell, P.R.1    Seegal, B.C.2    Hsu, K.C.3    Das, M.4    Soffer, R.L.5
  • 25
    • 0014560271 scopus 로고
    • Complement metabolism in man: Hypercatabolism of the fourth (C4) and third (C3) components in patients with renal allograft rejection and hereditary, angioedema (HAE)
    • Carpenter C.B., Ruddy S., Shehadeh I.H., Muller-Eberhard H.J., Merrill J.P., Austen K.F. Complement metabolism in man: Hypercatabolism of the fourth (C4) and third (C3) components in patients with renal allograft rejection and hereditary, angioedema (HAE). J. Clin. Invest. 48:1969;1495-1505
    • (1969) J. Clin. Invest. , vol.48 , pp. 1495-1505
    • Carpenter, C.B.1    Ruddy, S.2    Shehadeh, I.H.3    Muller-Eberhard, H.J.4    Merrill, J.P.5    Austen, K.F.6
  • 26
    • 0019198374 scopus 로고
    • Dissemination of contact activation in plasma by plasma kallikrein
    • Cochrane C.G., Revak S.D. Dissemination of contact activation in plasma by plasma kallikrein. J. Exp. Med. 152:1980;608-619
    • (1980) J. Exp. Med. , vol.152 , pp. 608-619
    • Cochrane, C.G.1    Revak, S.D.2
  • 27
    • 0015754565 scopus 로고
    • Activation of Hageman factor in solid and fluid phases: A critical role of kallikrein
    • Cochrane C.G., Revak S.D., Wuepper K.D. Activation of Hageman factor in solid and fluid phases: A critical role of kallikrein. J. Exp. Med. 138:1973;1564-1583
    • (1973) J. Exp. Med. , vol.138 , pp. 1564-1583
    • Cochrane, C.G.1    Revak, S.D.2    Wuepper, K.D.3
  • 28
    • 0014694698 scopus 로고
    • Activation of plasminogen by human plasma kallikrein
    • Colman R.W. Activation of plasminogen by human plasma kallikrein. Biochem. Biophys. Res. Commun. 35:1969;273-279
    • (1969) Biochem. Biophys. Res. Commun. , vol.35 , pp. 273-279
    • Colman, R.W.1
  • 29
    • 0030830360 scopus 로고    scopus 로고
    • Contact system: A vascular biology modulator with anticoagulant, profibrinolytic, antiadhesive, and proinflammatory attributes
    • Colman R.W., Schmaier A.H. Contact system: A vascular biology modulator with anticoagulant, profibrinolytic, antiadhesive, and proinflammatory attributes. Blood. 90:1997;3819-3843
    • (1997) Blood , vol.90 , pp. 3819-3843
    • Colman, R.W.1    Schmaier, A.H.2
  • 30
    • 0016774847 scopus 로고
    • Williams trait: Human kininogen deficiency with diminished levels of plasminogen proactivator and prekallikrein associated with abnormalities of the Hageman factor-dependent pathways
    • Colman R.W., Bagdasarian A., Talamo R.C., Scott C.F., Seavey M., Guimaraes J.A., Pierce J.V., Kaplan A.P. Williams trait: Human kininogen deficiency with diminished levels of plasminogen proactivator and prekallikrein associated with abnormalities of the Hageman factor-dependent pathways. J. Clin. Invest. 56:1975;1650-1662
    • (1975) J. Clin. Invest. , vol.56 , pp. 1650-1662
    • Colman, R.W.1    Bagdasarian, A.2    Talamo, R.C.3    Scott, C.F.4    Seavey, M.5    Guimaraes, J.A.6    Pierce, J.V.7    Kaplan, A.P.8
  • 32
    • 0030823246 scopus 로고    scopus 로고
    • Binding of high molecular weight kininogen to human endothelial cells is mediated via a site within domains 2 and 3 of the urokinase receptor
    • Colman R.W., Pixley R.A., Najamunnisa S., Yan W., Wang J., Mazar A., McCrae K.R. Binding of high molecular weight kininogen to human endothelial cells is mediated via a site within domains 2 and 3 of the urokinase receptor. J. Clin. Invest. 100:1997;1481-1487
    • (1997) J. Clin. Invest. , vol.100 , pp. 1481-1487
    • Colman, R.W.1    Pixley, R.A.2    Najamunnisa, S.3    Yan, W.4    Wang, J.5    Mazar, A.6    McCrae, K.R.7
  • 34
    • 0020587337 scopus 로고
    • Bradykinin-induced release of prostacyclin and thromboxanes from bovine pulmonary artery endothelial cells: Studies with lower homologs and calcium antagonists
    • Crutchley D.J., Ryan J.W., Ryan U.S., Fisher G.H. Bradykinin-induced release of prostacyclin and thromboxanes from bovine pulmonary artery endothelial cells: Studies with lower homologs and calcium antagonists. Biochim. Biophys. Acta. 751:1983;99-107
    • (1983) Biochim. Biophys. Acta , vol.751 , pp. 99-107
    • Crutchley, D.J.1    Ryan, J.W.2    Ryan, U.S.3    Fisher, G.H.4
  • 36
    • 0030175373 scopus 로고    scopus 로고
    • Activation of factor XII and cleavage of high molecular weight kininogen during acute attacks in hereditary and acquired C1-inhibitor deficiencies
    • Cugno M., Cicardi M., Coppola R., Agostoni A. Activation of factor XII and cleavage of high molecular weight kininogen during acute attacks in hereditary and acquired C1-inhibitor deficiencies. Immunopharmacology. 33:1996;361-364
    • (1996) Immunopharmacology , vol.33 , pp. 361-364
    • Cugno, M.1    Cicardi, M.2    Coppola, R.3    Agostoni, A.4
  • 37
    • 0018821108 scopus 로고
    • Detection of active kallikrein in induced blister fluids of hereditary angioedema patients
    • Curd J.G., Prograis L.J. Jr., Cochrane C.G. Detection of active kallikrein in induced blister fluids of hereditary angioedema patients. J. Exp. Med. 152:1980;742-747
    • (1980) J. Exp. Med. , vol.152 , pp. 742-747
    • Curd, J.G.1    Prograis Jr., L.J.2    Cochrane, C.G.3
  • 38
    • 0021241859 scopus 로고
    • Inactivation of factor XII active fragment in normal plasma. Predominant role of C-1-inhibitor
    • de Agostini A., Lijnen H.R., Pixley R.A., Colman R.W., Schapira M. Inactivation of factor XII active fragment in normal plasma. Predominant role of C-1-inhibitor. J. Clin. Invest. 73:1984;1542-1549
    • (1984) J. Clin. Invest. , vol.73 , pp. 1542-1549
    • De Agostini, A.1    Lijnen, H.R.2    Pixley, R.A.3    Colman, R.W.4    Schapira, M.5
  • 39
    • 0030590847 scopus 로고    scopus 로고
    • Kininogen binding protein p33/gC1qR is localized in the vesicular fraction of endothelial cells
    • Dedio J., Muller-Esterl W. Kininogen binding protein p33/gC1qR is localized in the vesicular fraction of endothelial cells. FEBS Lett. 399:1996;255-258
    • (1996) FEBS Lett. , vol.399 , pp. 255-258
    • Dedio, J.1    Muller-Esterl, W.2
  • 40
    • 0032055226 scopus 로고    scopus 로고
    • The multiligand-binding protein gC1qR, putative C1q receptor, is a mitochondrial protein
    • Dedio J., Jahnen-Dechent W., Bachmann M., Muller-Esterl W. The multiligand-binding protein gC1qR, putative C1q receptor, is a mitochondrial protein. J. Immunol. 160:1998;3534-3542
    • (1998) J. Immunol. , vol.160 , pp. 3534-3542
    • Dedio, J.1    Jahnen-Dechent, W.2    Bachmann, M.3    Muller-Esterl, W.4
  • 41
    • 0018637220 scopus 로고
    • An intrinsic factor XII-prekallikrein-dependent pathway activates the human plasma renin-angiotensin system
    • Derkx F.H., Bouma B.N., Schalekamp M.P., Schalekamp M.A. An intrinsic factor XII-prekallikrein-dependent pathway activates the human plasma renin-angiotensin system. Nature. 280:1979;315-316
    • (1979) Nature , vol.280 , pp. 315-316
    • Derkx, F.H.1    Bouma, B.N.2    Schalekamp, M.P.3    Schalekamp, M.A.4
  • 42
    • 0020047810 scopus 로고
    • The activation of the alternative pathway C3 convertase by human plasma kallikrein
    • DiScipio R.G. The activation of the alternative pathway C3 convertase by human plasma kallikrein. Immunology. 45:1982;587-595
    • (1982) Immunology , vol.45 , pp. 587-595
    • Discipio, R.G.1
  • 43
    • 0014262474 scopus 로고
    • Mechanisms of activation of C′1 esterase in hereditary angioneurotic edema plasma in vitro
    • Donaldson V.H. Mechanisms of activation of C′1 esterase in hereditary angioneurotic edema plasma in vitro. J. Exp. Med. 127:1968;411-429
    • (1968) J. Exp. Med. , vol.127 , pp. 411-429
    • Donaldson, V.H.1
  • 44
    • 0015498852 scopus 로고
    • Brief recordings: Rheumatoid arthritis in a patient with Hageman trait
    • Donaldson V.H., Glueck H.I., Fleming T. Brief recordings: Rheumatoid arthritis in a patient with Hageman trait. N. Engl. J. Med. 286:1972;528-530
    • (1972) N. Engl. J. Med. , vol.286 , pp. 528-530
    • Donaldson, V.H.1    Glueck, H.I.2    Fleming, T.3
  • 45
    • 0017252470 scopus 로고
    • Kininogen deficiency in Fitzgerald trait: Role of high molecular weight kininogen in clotting and fibrinolysis
    • Donaldson V.H., Glueck H.I., Miller M.A., Movat H.Z., Habal F. Kininogen deficiency in Fitzgerald trait: Role of high molecular weight kininogen in clotting and fibrinolysis. J. Lab. Clin. Med. 87:1976;327-337
    • (1976) J. Lab. Clin. Med. , vol.87 , pp. 327-337
    • Donaldson, V.H.1    Glueck, H.I.2    Miller, M.A.3    Movat, H.Z.4    Habal, F.5
  • 46
    • 0017636892 scopus 로고
    • Role of the second component of complement (C2) and plasmin in kinin release in hereditary angioneurotic edema (H.A.N.E.) plasma
    • Donaldson V.H., Rosen F.S., Bing D.H. Role of the second component of complement (C2) and plasmin in kinin release in hereditary angioneurotic edema (H.A.N.E.) plasma. Trans. Assoc. Am. Physicians. 90:1977;174-183
    • (1977) Trans. Assoc. Am. Physicians , vol.90 , pp. 174-183
    • Donaldson, V.H.1    Rosen, F.S.2    Bing, D.H.3
  • 47
    • 0019996918 scopus 로고
    • Formation and structure of human Hageman factor fragments
    • Dunn J.T., Kaplan A.P. Formation and structure of human Hageman factor fragments. J. Clin. Invest. 70:1982;627-631
    • (1982) J. Clin. Invest. , vol.70 , pp. 627-631
    • Dunn, J.T.1    Kaplan, A.P.2
  • 48
    • 0020076571 scopus 로고
    • The cleavage and formation of activated human Hageman factor by autodigestion and by kallikrein
    • Dunn J.T., Silverberg M., Kaplan A.P. The cleavage and formation of activated human Hageman factor by autodigestion and by kallikrein. J. Biol. Chem. 257:1982;1779-1784
    • (1982) J. Biol. Chem. , vol.257 , pp. 1779-1784
    • Dunn, J.T.1    Silverberg, M.2    Kaplan, A.P.3
  • 49
    • 0000077897 scopus 로고
    • An enzyme in human plasma that inactivates bradykinin and kallidins
    • Erdos E.G., Sloane G.M. An enzyme in human plasma that inactivates bradykinin and kallidins. Biochem. Pharmacol. 11:1962;585
    • (1962) Biochem. Pharmacol. , vol.11 , pp. 585
    • Erdos, E.G.1    Sloane, G.M.2
  • 50
    • 4444273183 scopus 로고    scopus 로고
    • Assessment of the role of heparan sulfate in high molecular weight kininogen binding to human umbilical vein endothelial cells
    • Fernando L.P., Fernando A.N., Joseph K., Kaplan A.P. Assessment of the role of heparan sulfate in high molecular weight kininogen binding to human umbilical vein endothelial cells. J. Thromb. Haemost. 1:2003a;2444-2449
    • (2003) J. Thromb. Haemost. , vol.1 , pp. 2444-2449
    • Fernando, L.P.1    Fernando, A.N.2    Joseph, K.3    Kaplan, A.P.4
  • 51
    • 0242521719 scopus 로고    scopus 로고
    • High molecular weight kininogen and factor XII binding to endothelial cells and astrocytes
    • Fernando L.P., Natesan S., Joseph K., Kaplan A.P. High molecular weight kininogen and factor XII binding to endothelial cells and astrocytes. Thromb. Haemost. 90:2003b;787-795
    • (2003) Thromb. Haemost. , vol.90 , pp. 787-795
    • Fernando, L.P.1    Natesan, S.2    Joseph, K.3    Kaplan, A.P.4
  • 52
    • 0020520854 scopus 로고
    • Kinin formation in hereditary angioedema plasma: Evidence against kinin derivation from C2 and in support of "spontaneous" formation of bradykinin
    • Fields T., Ghebrehiwet B., Kaplan A.P. Kinin formation in hereditary angioedema plasma: Evidence against kinin derivation from C2 and in support of "spontaneous" formation of bradykinin. J. Allergy Clin. Immunol. 72:1983;54-60
    • (1983) J. Allergy Clin. Immunol. , vol.72 , pp. 54-60
    • Fields, T.1    Ghebrehiwet, B.2    Kaplan, A.P.3
  • 53
    • 0014883077 scopus 로고
    • Inhibition of activated Hageman factor and activated plasma thromboplastin antecedent by purified serum C1 inactivator
    • Forbes C.D., Pensky J., Ratnoff O.D. Inhibition of activated Hageman factor and activated plasma thromboplastin antecedent by purified serum C1 inactivator. J. Lab. Clin. Med. 76:1970;809-815
    • (1970) J. Lab. Clin. Med. , vol.76 , pp. 809-815
    • Forbes, C.D.1    Pensky, J.2    Ratnoff, O.D.3
  • 54
    • 0015504576 scopus 로고
    • ε-Aminocaproic acid therapy of hereditary angioneurotic edema: A double-blind study
    • Frank M.M., Sergent J.S., Kane M.A., Alling D.W. ε-Aminocaproic acid therapy of hereditary angioneurotic edema: A double-blind study. N. Engl. J. Med. 286:1972;808-812
    • (1972) N. Engl. J. Med. , vol.286 , pp. 808-812
    • Frank, M.M.1    Sergent, J.S.2    Kane, M.A.3    Alling, D.W.4
  • 55
    • 0025874052 scopus 로고
    • Factor XI activation in a revised model of blood coagulation
    • Gailani D., Broze G.J. Jr. Factor XI activation in a revised model of blood coagulation. Science. 253:1991;909-912
    • (1991) Science , vol.253 , pp. 909-912
    • Gailani, D.1    Broze Jr., G.J.2
  • 57
    • 0019471542 scopus 로고
    • Activation of the classical pathway of complement by Hageman factor fragment
    • Ghebrehiwet B., Silverberg M., Kaplan A.P. Activation of the classical pathway of complement by Hageman factor fragment. J. Exp. Med. 153:1981;665-676
    • (1981) J. Exp. Med. , vol.153 , pp. 665-676
    • Ghebrehiwet, B.1    Silverberg, M.2    Kaplan, A.P.3
  • 58
    • 0020529790 scopus 로고
    • Mechanisms of activation of the classical pathway of complement by Hageman factor fragment
    • Ghebrehiwet B., Randazzo B.P., Dunn J.T., Silverberg M., Kaplan A.P. Mechanisms of activation of the classical pathway of complement by Hageman factor fragment. J. Clin. Invest. 71:1983;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
  • 59
    • 0028290256 scopus 로고
    • Isolation, cDNA cloning, and overexpression of a 33-kD cell surface glycoprotein that binds to the globular "heads" of C1q
    • Ghebrehiwet B., Lim B.L., Peerschke E.I., Willis A.C., Reid K.B. Isolation, cDNA cloning, and overexpression of a 33-kD cell surface glycoprotein that binds to the globular "heads" of C1q. J. Exp. Med. 179:1994;1809-1821
    • (1994) J. Exp. Med. , vol.179 , pp. 1809-1821
    • Ghebrehiwet, B.1    Lim, B.L.2    Peerschke, E.I.3    Willis, A.C.4    Reid, K.B.5
  • 60
    • 0014750141 scopus 로고
    • Interaction of plasma kallikrein with the C1 inhibitor
    • Gigli I., Mason J.W., Colman R.W., Austen K.F. Interaction of plasma kallikrein with the C1 inhibitor. J. Immunol. 104:1970;574-581
    • (1970) J. Immunol. , vol.104 , pp. 574-581
    • Gigli, I.1    Mason, J.W.2    Colman, R.W.3    Austen, K.F.4
  • 61
    • 0018828299 scopus 로고
    • Urate crystal-dependent cleavage of Hageman factor in human plasma and synovial fluid
    • Ginsberg M.H., Jaques B., Cochrane C.G., Griffin J.H. Urate crystal-dependent cleavage of Hageman factor in human plasma and synovial fluid. J. Lab. Clin. Med. 95:1980;497-506
    • (1980) J. Lab. Clin. Med. , vol.95 , pp. 497-506
    • Ginsberg, M.H.1    Jaques, B.2    Cochrane, C.G.3    Griffin, J.H.4
  • 62
    • 0015531092 scopus 로고
    • Cold promoted activation of factor VII. 3. Relation to the kallikrein system
    • Gjonnaess H. Cold promoted activation of factor VII. 3. Relation to the kallikrein system. Thromb. Diathesis Haemorrhagica. 28:1972;182-193
    • (1972) Thromb. Diathesis Haemorrhagica , vol.28 , pp. 182-193
    • Gjonnaess, H.1
  • 63
    • 0018103306 scopus 로고
    • The activation of plasminogen by Hageman factor (factor XII) and Hageman factor fragments
    • Goldsmith G., Saito H., Ratnoff O.D. The activation of plasminogen by Hageman factor (factor XII) and Hageman factor fragments. J. Clin. Invest. 12:1978;54
    • (1978) J. Clin. Invest. , vol.12 , pp. 54
    • Goldsmith, G.1    Saito, H.2    Ratnoff, O.D.3
  • 64
    • 0019129748 scopus 로고
    • Rapid fibrinolysis, augmented Hageman factor (factor XII) titers, and decreased C1 esterase inhibitor titers in women taking oral contraceptives
    • Gordon E.M., Ratnoff O.D., Saito H., Donaldson V.H., Pensky J., Jones P.K. Rapid fibrinolysis, augmented Hageman factor (factor XII) titers, and decreased C1 esterase inhibitor titers in women taking oral contraceptives. J. Lab. Clin. Med. 96:1980;762-769
    • (1980) J. Lab. Clin. Med. , vol.96 , pp. 762-769
    • Gordon, E.M.1    Ratnoff, O.D.2    Saito, H.3    Donaldson, V.H.4    Pensky, J.5    Jones, P.K.6
  • 65
    • 0021032717 scopus 로고
    • Influence of augmented Hageman factor (factor XII) titers on the cryoactivation of plasma prorenin in women using oral contraceptive agents
    • Gordon E.M., Douglas J., Ratnoff O.D. Influence of augmented Hageman factor (factor XII) titers on the cryoactivation of plasma prorenin in women using oral contraceptive agents. J. Clin. Invest. 72:1983;1833-1838
    • (1983) J. Clin. Invest. , vol.72 , pp. 1833-1838
    • Gordon, E.M.1    Douglas, J.2    Ratnoff, O.D.3
  • 66
    • 0021134026 scopus 로고
    • Human plasma α-cysteine proteinase inhibitor: Purification by affinity chromatography, characterization and isolation of an active fragment
    • Gounaris A.D., Brown M.A., Barrett A.J. Human plasma α-cysteine proteinase inhibitor: Purification by affinity chromatography, characterization and isolation of an active fragment. Biochem. J. 221:1984;445-452
    • (1984) Biochem. J. , vol.221 , pp. 445-452
    • Gounaris, A.D.1    Brown, M.A.2    Barrett, A.J.3
  • 67
    • 0021739735 scopus 로고
    • Receptors for high molecular weight kininogen on stimulated washed human platelets
    • Greengard J.S., Griffin J.H. Receptors for high molecular weight kininogen on stimulated washed human platelets. Biochemistry. 23:1984;6863-6869
    • (1984) Biochemistry , vol.23 , pp. 6863-6869
    • Greengard, J.S.1    Griffin, J.H.2
  • 68
    • 0001525663 scopus 로고
    • Role of surface in surface-dependent activation of Hageman factor (blood coagulation factor XII)
    • Griffin J.H. Role of surface in surface-dependent activation of Hageman factor (blood coagulation factor XII). Proc. Natl. Acad. Sci. USA. 75:1978;1998-2002
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 1998-2002
    • Griffin, J.H.1
  • 69
    • 0001535419 scopus 로고
    • Mechanisms for the involvement of high molecular weight kininogen in surface-dependent reactions of Hageman factor
    • Griffin J.H., Cochrane C.G. Mechanisms for the involvement of high molecular weight kininogen in surface-dependent reactions of Hageman factor. Proc. Natl. Acad. Sci. USA. 73:1976;2554-2558
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 2554-2558
    • Griffin, J.H.1    Cochrane, C.G.2
  • 71
    • 0015784975 scopus 로고
    • Studies on human plasma alpha 2-macroglobulin-enzyme interactions. Evidence for proteolytic modification of the subunit chain structure
    • Harpel P.C. Studies on human plasma alpha 2-macroglobulin-enzyme interactions. Evidence for proteolytic modification of the subunit chain structure. J. Exp. Med. 138:1973;508-521
    • (1973) J. Exp. Med. , vol.138 , pp. 508-521
    • Harpel, P.C.1
  • 73
    • 0028879618 scopus 로고
    • Conformational changes in low molecular weight kininogen alters its ability to bind to endothelial cells
    • Hasan A.A., Zhang J., Samuel M., Schmaier A.H. Conformational changes in low molecular weight kininogen alters its ability to bind to endothelial cells. Thromb. Haemost. 74:1995;1088-1095
    • (1995) Thromb. Haemost. , vol.74 , pp. 1088-1095
    • Hasan, A.A.1    Zhang, J.2    Samuel, M.3    Schmaier, A.H.4
  • 74
    • 0032584066 scopus 로고    scopus 로고
    • Identification of cytokeratin 1 as a binding protein and presentation receptor for kininogens on endothelial cells
    • Hasan A.A., Zisman T., Schmaier A.H. Identification of cytokeratin 1 as a binding protein and presentation receptor for kininogens on endothelial cells. Proc. Natl. Acad. Sci. USA. 95:1998;3615-3620
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3615-3620
    • Hasan, A.A.1    Zisman, T.2    Schmaier, A.H.3
  • 75
    • 0024508761 scopus 로고
    • Plasminogen activators in dextran sulfate-activated euglobulin fractions: A molecular analysis of factor XII- and prekallikrein-dependent fibrinolysis
    • Hauert J., Nicoloso G., Schleuning W.D., Bachmann F., Schapira M. Plasminogen activators in dextran sulfate-activated euglobulin fractions: A molecular analysis of factor XII- and prekallikrein-dependent fibrinolysis. Blood. 73:1989;994-999
    • (1989) Blood , vol.73 , pp. 994-999
    • Hauert, J.1    Nicoloso, G.2    Schleuning, W.D.3    Bachmann, F.4    Schapira, M.5
  • 78
    • 0029931383 scopus 로고    scopus 로고
    • Isolation and characterization of the kininogen-binding protein p33 from endothelial cells: Identity with the gC1q receptor
    • Herwald H., Dedio J., Kellner R., Loos M., Muller-Esterl W. Isolation and characterization of the kininogen-binding protein p33 from endothelial cells: Identity with the gC1q receptor. J. Biol. Chem. 271:1996;13040-13047
    • (1996) J. Biol. Chem. , vol.271 , pp. 13040-13047
    • Herwald, H.1    Dedio, J.2    Kellner, R.3    Loos, M.4    Muller-Esterl, W.5
  • 79
    • 0022477117 scopus 로고
    • Human high molecular weight kininogen as a thiol proteinase inhibitor: Presence of the entire inhibition capacity in the native form of heavy chain
    • Higashiyama S., Ohkubo I., Ishiguro H., Kunimatsu M., Sawaki K., Sasaki M. Human high molecular weight kininogen as a thiol proteinase inhibitor: Presence of the entire inhibition capacity in the native form of heavy chain. Biochemistry. 25:1986;1669-1675
    • (1986) Biochemistry , vol.25 , pp. 1669-1675
    • Higashiyama, S.1    Ohkubo, I.2    Ishiguro, H.3    Kunimatsu, M.4    Sawaki, K.5    Sasaki, M.6
  • 81
    • 0021235057 scopus 로고
    • In vitro activation of the contact (Hageman factor) system of plasma by heparin and chondroitin sulfate e
    • Hojima Y., Cochrane C.G., Wiggins R.C., Austen K.F., Stevens R.L. In vitro activation of the contact (Hageman factor) system of plasma by heparin and chondroitin sulfate E. Blood. 63:1984;1453-1459
    • (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
  • 82
    • 0018940298 scopus 로고
    • Effect of bradykinin and thrombin on prostacyclin synthesis in endothelial cells from calf and pig aorta and human umbilical cord vein
    • Hong S.L. Effect of bradykinin and thrombin on prostacyclin synthesis in endothelial cells from calf and pig aorta and human umbilical cord vein. Thromb. Res. 18:1980;787-795
    • (1980) Thromb. Res. , vol.18 , pp. 787-795
    • Hong, S.L.1
  • 83
    • 0032577676 scopus 로고    scopus 로고
    • Molecular cloning of platelet factor XI, an alternative splicing product of the plasma factor XI gene
    • Hsu T.C., Shore S.K., Seshsmma T., Bagasra O., Walsh P.N. Molecular cloning of platelet factor XI, an alternative splicing product of the plasma factor XI gene. J. Biol. Chem. 273:1998;13787-13793
    • (1998) J. Biol. Chem. , vol.273 , pp. 13787-13793
    • Hsu, T.C.1    Shore, S.K.2    Seshsmma, T.3    Bagasra, O.4    Walsh, P.N.5
  • 85
    • 8544274821 scopus 로고
    • Active Hageman factor: A plasma lysokinase of the human fibrinolytic system
    • Iatridis P.G., Ferguson J.H. Active Hageman factor: A plasma lysokinase of the human fibrinolytic system. J. Clin. Invest. 41:1962;1277
    • (1962) J. Clin. Invest. , vol.41 , pp. 1277
    • Iatridis, P.G.1    Ferguson, J.H.2
  • 86
    • 0023022473 scopus 로고
    • The activation of pro-urokinase by plasma kallikrein and its inactivation by thrombin
    • Ichinose A., Fujikawa K., Suyama T. The activation of pro-urokinase by plasma kallikrein and its inactivation by thrombin. J. Biol. Chem. 261:1986;3486-3489
    • (1986) J. Biol. Chem. , vol.261 , pp. 3486-3489
    • Ichinose, A.1    Fujikawa, K.2    Suyama, T.3
  • 87
    • 0023520955 scopus 로고
    • Mapping of functional domains of human high molecular weight and low molecular weight kininogens using murine monoclonal antibodies
    • Ishiguro H., Higashiyama S., Ohkubo I., Sasaki M. Mapping of functional domains of human high molecular weight and low molecular weight kininogens using murine monoclonal antibodies. Biochemistry. 26:1987;7021-7029
    • (1987) Biochemistry , vol.26 , pp. 7021-7029
    • Ishiguro, H.1    Higashiyama, S.2    Ohkubo, I.3    Sasaki, M.4
  • 88
    • 0014003932 scopus 로고
    • Separation of two separate substrates for plasma kinin forming enzymes
    • Jacobsen S. Separation of two separate substrates for plasma kinin forming enzymes. Nature. 210:1966;98-99
    • (1966) Nature , vol.210 , pp. 98-99
    • Jacobsen, S.1
  • 90
    • 0022226546 scopus 로고
    • Increased euglobulin fibrinolytic potential in women on oral contraceptives low in oestrogen: Levels of extrinsic and intrinsic plasminogen activators, prekallikrein, factor XII, and C1-inactivator
    • Jespersen J., Kluft C. Increased euglobulin fibrinolytic potential in women on oral contraceptives low in oestrogen: Levels of extrinsic and intrinsic plasminogen activators, prekallikrein, factor XII, and C1-inactivator. Thromb. Haemost. 54:1985;454-459
    • (1985) Thromb. Haemost. , vol.54 , pp. 454-459
    • Jespersen, J.1    Kluft, C.2
  • 91
    • 0026667325 scopus 로고
    • Insights on monoclonal antibodies to kininogens' heavy chain which influence kininogens' binding to platelets
    • Jiang Y., Nawarawong W., Meloni F.J., Schmaier A.H. Insights on monoclonal antibodies to kininogens' heavy chain which influence kininogens' binding to platelets. Thromb. Haemost. 68:1992a;143-148
    • (1992) Thromb. Haemost. , vol.68 , pp. 143-148
    • Jiang, Y.1    Nawarawong, W.2    Meloni, F.J.3    Schmaier, A.H.4
  • 92
    • 0026784525 scopus 로고
    • Domain 3 of kininogens contains a cell-binding site and a site that modifies thrombin activation of platelets
    • Jiang Y.P., Muller-Esterl W., Schmaier A.H. Domain 3 of kininogens contains a cell-binding site and a site that modifies thrombin activation of platelets. J. Biol. Chem. 267:1992b;3712-3717
    • (1992) J. Biol. Chem. , vol.267 , pp. 3712-3717
    • Jiang, Y.P.1    Muller-Esterl, W.2    Schmaier, A.H.3
  • 93
    • 0036892460 scopus 로고    scopus 로고
    • Bradykinin receptor modulation in cellular models of aging and Alzheimer's disease
    • Jong Y.J., Dalemar L.R., Seehra K., Baenziger N.L. Bradykinin receptor modulation in cellular models of aging and Alzheimer's disease. Int. Immunopharmacol. 2:2002;1833-1840
    • (2002) Int. Immunopharmacol. , vol.2 , pp. 1833-1840
    • Jong, Y.J.1    Dalemar, L.R.2    Seehra, K.3    Baenziger, N.L.4
  • 94
    • 0022363879 scopus 로고
    • Kinetic analysis of plasminogen activation by purified plasma kallikrein
    • Jorg M., Binder B.R. Kinetic analysis of plasminogen activation by purified plasma kallikrein. Thromb. Res. 39:1985;323-331
    • (1985) Thromb. Res. , vol.39 , pp. 323-331
    • Jorg, M.1    Binder, B.R.2
  • 95
    • 0029763086 scopus 로고    scopus 로고
    • Identification of the zinc-dependent endothelial cell binding protein for high molecular weight kininogen and factor XII: Identity with the receptor that binds to the globular "heads" of C1q (gC1q-R)
    • Joseph K., Ghebrehiwet B., Peerschke E.I., Reid K.B., Kaplan A.P. Identification of the zinc-dependent endothelial cell binding protein for high molecular weight kininogen and factor XII: Identity with the receptor that binds to the globular "heads" of C1q (gC1q-R). Proc. Natl. Acad. Sci. USA. 93:1996;8552-8557
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8552-8557
    • Joseph, K.1    Ghebrehiwet, B.2    Peerschke, E.I.3    Reid, K.B.4    Kaplan, A.P.5
  • 96
    • 0032823546 scopus 로고    scopus 로고
    • Platelet glycoprotein Ib: A zinc-dependent binding protein for the heavy chain of high-molecular-weight kininogen
    • Joseph K., Nakazawa Y., Bahou W.F., Ghebrehiwet B., Kaplan A.P. Platelet glycoprotein Ib: A zinc-dependent binding protein for the heavy chain of high-molecular-weight kininogen. Mol. Med. 5:1999a;555-563
    • (1999) Mol. Med. , vol.5 , pp. 555-563
    • Joseph, K.1    Nakazawa, Y.2    Bahou, W.F.3    Ghebrehiwet, B.4    Kaplan, A.P.5
  • 97
    • 0032755652 scopus 로고    scopus 로고
    • Interaction of factor XII and high molecular weight kininogen with cytokeratin 1 and gC1qR of vascular endothelial cells and with aggregated Aβ protein of Alzheimer's disease
    • Joseph K., Shibayama Y., Nakazawa Y., Peerschke E.I., Ghebrehiwet B., Kaplan A.P. Interaction of factor XII and high molecular weight kininogen with cytokeratin 1 and gC1qR of vascular endothelial cells and with aggregated Aβ protein of Alzheimer's disease. Immunopharmacology. 43:1999b;203-210
    • (1999) Immunopharmacology , vol.43 , pp. 203-210
    • Joseph, K.1    Shibayama, Y.2    Nakazawa, Y.3    Peerschke, E.I.4    Ghebrehiwet, B.5    Kaplan, A.P.6
  • 98
    • 0032823979 scopus 로고    scopus 로고
    • Cytokeratin 1 and gC1qR mediate high molecular weight kininogen binding to endothelial cells
    • Joseph K., Ghebrehiwet B., Kaplan A.P. Cytokeratin 1 and gC1qR mediate high molecular weight kininogen binding to endothelial cells. Clin. Immunol. 92:1999c;246-255
    • (1999) Clin. Immunol. , vol.92 , pp. 246-255
    • Joseph, K.1    Ghebrehiwet, B.2    Kaplan, A.P.3
  • 99
    • 0035115246 scopus 로고    scopus 로고
    • Activation of the kinin-forming cascade on the surface of endothelial cells
    • Joseph K., Ghebrehiwet B., Kaplan A.P. Activation of the kinin-forming cascade on the surface of endothelial cells. Biol. Chem. 382:2001a;71-75
    • (2001) Biol. Chem. , vol.382 , pp. 71-75
    • Joseph, K.1    Ghebrehiwet, B.2    Kaplan, A.P.3
  • 100
    • 0035173017 scopus 로고    scopus 로고
    • Factor XII-dependent contact activation on endothelial cells and binding proteins gC1qR and cytokeratin 1
    • Joseph K., Shibayama Y., Ghebrehiwet B., Kaplan A.P. Factor XII-dependent contact activation on endothelial cells and binding proteins gC1qR and cytokeratin 1. Thromb. Haemost. 85:2001b;119-124
    • (2001) Thromb. Haemost. , vol.85 , pp. 119-124
    • Joseph, K.1    Shibayama, Y.2    Ghebrehiwet, B.3    Kaplan, A.P.4
  • 101
    • 0036892390 scopus 로고    scopus 로고
    • Activation of the bradykinin-forming cascade on endothelial cells: A role for heat shock protein 90
    • Joseph K., Tholanikunnel B.G., Kaplan A.P. Activation of the bradykinin-forming cascade on endothelial cells: A role for heat shock protein 90. Int. Immunopharmacol. 2:2002a;1851-1859
    • (2002) Int. Immunopharmacol. , vol.2 , pp. 1851-1859
    • Joseph, K.1    Tholanikunnel, B.G.2    Kaplan, A.P.3
  • 102
    • 0037154220 scopus 로고    scopus 로고
    • Heat shock protein 90 catalyzes activation of the prekallikrein-kininogen complex in the absence of factor XII
    • Joseph K., Tholanikunnel B.G., Kaplan A.P. Heat shock protein 90 catalyzes activation of the prekallikrein-kininogen complex in the absence of factor XII. Proc. Natl. Acad. Sci. USA. 99:2002b;896-900
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 896-900
    • Joseph, K.1    Tholanikunnel, B.G.2    Kaplan, A.P.3
  • 103
    • 0014455650 scopus 로고
    • Vascular reactions in hereditary angioneurotic edema
    • Juhlin L., Michaelsson G. Vascular reactions in hereditary angioneurotic edema. Acta Derm. Venereol. 49:1969;20-25
    • (1969) Acta Derm. Venereol. , vol.49 , pp. 20-25
    • Juhlin, L.1    Michaelsson, G.2
  • 104
    • 0014868785 scopus 로고
    • A pre-albumin activator of prekallikrein
    • Kaplan A.P., Austen K.F. A pre-albumin activator of prekallikrein. J. Immunol. 105:1970;802-811
    • (1970) J. Immunol. , vol.105 , pp. 802-811
    • Kaplan, A.P.1    Austen, K.F.2
  • 105
    • 0015044927 scopus 로고
    • A prealbumin activator of prekallikrein. II. Derivation of activators of prekallikrein from active Hageman factor by digestion with plasmin
    • Kaplan A.P., Austen K.F. A prealbumin activator of prekallikrein. II. Derivation of activators of prekallikrein from active Hageman factor by digestion with plasmin. J. Exp. Med. 133:1971;696-712
    • (1971) J. Exp. Med. , vol.133 , pp. 696-712
    • Kaplan, A.P.1    Austen, K.F.2
  • 106
    • 0023201944 scopus 로고
    • The coagulation-kinin pathway of human plasma
    • Kaplan A.P., Silverberg M. The coagulation-kinin pathway of human plasma. Blood. 70:1987;1-15
    • (1987) Blood , vol.70 , pp. 1-15
    • Kaplan, A.P.1    Silverberg, M.2
  • 107
    • 0015256028 scopus 로고
    • A prealbumin activator of prekallikrein. 3. Appearance of chemotactic activity for human neutrophils by the conversion of human prekallikrein to kallikrein
    • Kaplan A.P., Kay A.B., Austen K.F. A prealbumin activator of prekallikrein. 3. Appearance of chemotactic activity for human neutrophils by the conversion of human prekallikrein to kallikrein. J. Exp. Med. 135:1972;81-97
    • (1972) J. Exp. Med. , vol.135 , pp. 81-97
    • Kaplan, A.P.1    Kay, A.B.2    Austen, K.F.3
  • 108
    • 0030885721 scopus 로고    scopus 로고
    • The intrinsic coagulation/kinin-forming cascade: Assembly in plasma and cell surfaces in inflammation
    • Kaplan A.P., Joseph K., Shibayama Y., Reddigari S., Ghebrehiwet B., Silverberg M. The intrinsic coagulation/kinin-forming cascade: Assembly in plasma and cell surfaces in inflammation. Adv. Immunol. 66:1997;225-272
    • (1997) Adv. Immunol. , vol.66 , pp. 225-272
    • Kaplan, A.P.1    Joseph, K.2    Shibayama, Y.3    Reddigari, S.4    Ghebrehiwet, B.5    Silverberg, M.6
  • 109
  • 111
    • 0022445020 scopus 로고
    • Completion of the primary structure of human high-molecular-mass kininogen: The amino acid sequence of the entire heavy chain and evidence for its evolution by gene triplication
    • Kellermann J., Lottspeich F., Henschen A., Muller-Esterl W. Completion of the primary structure of human high-molecular-mass kininogen: The amino acid sequence of the entire heavy chain and evidence for its evolution by gene triplication. Eur. J. Biochem. 154:1986b;471-478
    • (1986) Eur. J. Biochem. , vol.154 , pp. 471-478
    • Kellermann, J.1    Lottspeich, F.2    Henschen, A.3    Muller-Esterl, W.4
  • 112
    • 37949013959 scopus 로고
    • The inflammatory process in acute gouty arthritis. 1. Activation of Hageman factor by urate crystals
    • Kellermeyer R.W., Breckenridge R.T. The inflammatory process in acute gouty arthritis. 1. Activation of Hageman factor by urate crystals. J. Lab. Clin. Med. 63:1965;307
    • (1965) J. Lab. Clin. Med. , vol.63 , pp. 307
    • Kellermeyer, R.W.1    Breckenridge, R.T.2
  • 114
    • 0014261894 scopus 로고
    • Effect of C′1 esterase on vascular permeability in man: Studies in normal and complement-deficient individuals and in patients with hereditary angioneurotic edema
    • Klemperer M.R., Donaldson V.H., Rosen F.S. Effect of C′1 esterase on vascular permeability in man: Studies in normal and complement-deficient individuals and in patients with hereditary angioneurotic edema. J. Clin. Invest. 47:1968;604-611
    • (1968) J. Clin. Invest. , vol.47 , pp. 604-611
    • Klemperer, M.R.1    Donaldson, V.H.2    Rosen, F.S.3
  • 115
    • 0017095326 scopus 로고
    • Occurrence of C1 inactivator and other proteinase inhibitors in euglobulin fractions and their influence on fibrinolytic activity
    • Kluft C. Occurrence of C1 inactivator and other proteinase inhibitors in euglobulin fractions and their influence on fibrinolytic activity. Haemostasis. 5:1976;136-146
    • (1976) Haemostasis , vol.5 , pp. 136-146
    • Kluft, C.1
  • 116
    • 0017588157 scopus 로고
    • Elimination of inhibition in euglobulin fibrinolysis by use of flufenamate: Involvement of C1-inactivator
    • Kluft C. Elimination of inhibition in euglobulin fibrinolysis by use of flufenamate: Involvement of C1-inactivator. Haemostasis. 6:1977;351-369
    • (1977) Haemostasis , vol.6 , pp. 351-369
    • Kluft, C.1
  • 117
    • 0021351386 scopus 로고
    • Intrinsic plasma fibrinolysis: Involvement of urokinase-related activity in the factor XII-independent plasminogen proactivator pathway
    • Kluft C., Wijngaards G., Jie A.F. Intrinsic plasma fibrinolysis: Involvement of urokinase-related activity in the factor XII-independent plasminogen proactivator pathway. J. Lab. Clin. Med. 103:1984;408-419
    • (1984) J. Lab. Clin. Med. , vol.103 , pp. 408-419
    • Kluft, C.1    Wijngaards, G.2    Jie, A.F.3
  • 118
    • 0016192479 scopus 로고
    • Cold-promoted activation of factor VII in human plasma: Studies on the associated acyl-arginine esterase activity
    • Laake K., Vennerod A.M., Haugen G., Gjonnaess H. Cold-promoted activation of factor VII in human plasma: Studies on the associated acyl-arginine esterase activity. Thromb. Res. 4:1974;769-785
    • (1974) Thromb. Res. , vol.4 , pp. 769-785
    • Laake, K.1    Vennerod, A.M.2    Haugen, G.3    Gjonnaess, H.4
  • 119
    • 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. 74:1995;698-703
    • (1995) Thromb. Haemost. , vol.74 , pp. 698-703
    • Lenich, C.1    Pannell, R.2    Gurewich, V.3
  • 120
    • 0030803026 scopus 로고    scopus 로고
    • High molecular weight kininogen peptides inhibit the formation of kallikrein on endothelial cell surfaces and subsequent urokinase-dependent plasmin formation
    • Lin Y., Harris R.B., Yan W., McCrae K.R., Zhang H., Colman R.W. High molecular weight kininogen peptides inhibit the formation of kallikrein on endothelial cell surfaces and subsequent urokinase-dependent plasmin formation. Blood. 90:1997;690-697
    • (1997) Blood , vol.90 , pp. 690-697
    • Lin, Y.1    Harris, R.B.2    Yan, W.3    McCrae, K.R.4    Zhang, H.5    Colman, R.W.6
  • 121
    • 0018406731 scopus 로고
    • Human platelets and factor XI. Localization in platelet membranes of factor XI-like activity and its functional distinction from plasma factor XI
    • Lipscomb M.S., Walsh P.N. Human platelets and factor XI. Localization in platelet membranes of factor XI-like activity and its functional distinction from plasma factor XI. J. Clin. Invest. 63:1979;1006-1014
    • (1979) J. Clin. Invest. , vol.63 , pp. 1006-1014
    • Lipscomb, M.S.1    Walsh, P.N.2
  • 122
    • 0021288233 scopus 로고
    • Factor XII deficiency in a man with gout and angioimmunoblastic lymphadenopathy
    • Londino A.V. Jr., Luparello F.J. Factor XII deficiency in a man with gout and angioimmunoblastic lymphadenopathy. Arch. Internal Med. 144:1984;1497-1498
    • (1984) Arch. Internal Med. , vol.144 , pp. 1497-1498
    • Londino Jr., A.V.1    Luparello, F.J.2
  • 123
    • 0021255416 scopus 로고
    • Human low-molecular-mass kininogen: Amino-acid sequence of the light chain; Homology with other protein sequences
    • Lottspeich F., Kellermann J., Henschen A., Rauth G., Muller-Esterl W. Human low-molecular-mass kininogen: Amino-acid sequence of the light chain; homology with other protein sequences. Eur. J. Biochem. 142:1984;227-232
    • (1984) Eur. J. Biochem. , vol.142 , pp. 227-232
    • Lottspeich, F.1    Kellermann, J.2    Henschen, A.3    Rauth, G.4    Muller-Esterl, W.5
  • 124
    • 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. 71:1994;347-352
    • (1994) Thromb. Haemost. , vol.71 , pp. 347-352
    • Loza, J.P.1    Gurewich, V.2    Johnstone, M.3    Pannell, R.4
  • 125
    • 0031923705 scopus 로고    scopus 로고
    • Oleic acid and angiotensin II induce a synergistic mitogenic response in vascular smooth muscle cells
    • Lu G., Meier K.E., Jaffa A.A., Rosenzweig S.A., Egan B.M. Oleic acid and angiotensin II induce a synergistic mitogenic response in vascular smooth muscle cells. Hypertension. 31:1998;978-985
    • (1998) Hypertension , vol.31 , pp. 978-985
    • Lu, G.1    Meier, K.E.2    Jaffa, A.A.3    Rosenzweig, S.A.4    Egan, B.M.5
  • 126
    • 0014326759 scopus 로고
    • A case of hereditary angioneurotic oedema, successfully treated with epsilon-aminocaproic acid: Studies on C′1 esterase inhibitor, C′1 activation, plasminogen level and histamine metabolism
    • Lundh B., Laurell A.B., Wetterqvist H., White T., Granerus G. A case of hereditary angioneurotic oedema, successfully treated with epsilon-aminocaproic acid: Studies on C′1 esterase inhibitor, C′1 activation, plasminogen level and histamine metabolism. Clin. Exp. Immunol. 3:1968;733-745
    • (1968) Clin. Exp. Immunol. , vol.3 , pp. 733-745
    • Lundh, B.1    Laurell, A.B.2    Wetterqvist, H.3    White, T.4    Granerus, G.5
  • 127
    • 0035871850 scopus 로고    scopus 로고
    • Expression and colocalization of cytokeratin 1 and urokinase plasminogen activator receptor on endothelial cells
    • Mahdi F., Shariat-Madar Z., Todd R.F. III, Figueroa C.D., Schmaier A.H. Expression and colocalization of cytokeratin 1 and urokinase plasminogen activator receptor on endothelial cells. Blood. 97:2001;2342-2350
    • (2001) Blood , vol.97 , pp. 2342-2350
    • Mahdi, F.1    Shariat-Madar, Z.2    Todd III, R.F.3    Figueroa, C.D.4    Schmaier, A.H.5
  • 128
    • 0037093204 scopus 로고    scopus 로고
    • Factor XII interacts with the multiprotein assembly of urokinase plasminogen activator receptor, gC1qR, and cytokeratin 1 on endothelial cell membranes
    • Mahdi F., Madar Z.S., Figueroa C.D., Schmaier A.H. Factor XII interacts with the multiprotein assembly of urokinase plasminogen activator receptor, gC1qR, and cytokeratin 1 on endothelial cell membranes. Blood. 99:2002;3585-3596
    • (2002) Blood , vol.99 , pp. 3585-3596
    • Mahdi, F.1    Madar, Z.S.2    Figueroa, C.D.3    Schmaier, A.H.4
  • 129
    • 0242415187 scopus 로고    scopus 로고
    • The relative priority of prekallikrein and factors XI/XIa assembly on cultured endothelial cells
    • Mahdi F., Shariat-Madar Z., Schmaier A.H. The relative priority of prekallikrein and factors XI/XIa assembly on cultured endothelial cells. J. Biol. Chem. 278:2003;43983-43990
    • (2003) J. Biol. Chem. , vol.278 , pp. 43983-43990
    • Mahdi, F.1    Shariat-Madar, Z.2    Schmaier, A.H.3
  • 130
    • 0017149563 scopus 로고
    • Identification of prekallikrein and high-molecular-weight kininogen as a complex in human plasma
    • Mandle R.J., Colman R.W., Kaplan A.P. Identification of prekallikrein and high-molecular-weight kininogen as a complex in human plasma. Proc. Natl. Acad. Sci. USA. 73:1976;4179-4183
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 4179-4183
    • Mandle, R.J.1    Colman, R.W.2    Kaplan, A.P.3
  • 131
    • 0018716550 scopus 로고
    • Hageman-factor-dependent fibrinolysis: Generation of fibrinolytic activity by the interaction of human activated factor XI and plasminogen
    • Mandle R.J. Jr., Kaplan A.P. Hageman-factor-dependent fibrinolysis: Generation of fibrinolytic activity by the interaction of human activated factor XI and plasminogen. Blood. 54:1979;850-862
    • (1979) Blood , vol.54 , pp. 850-862
    • Mandle Jr., R.J.1    Kaplan, A.P.2
  • 133
    • 0014869080 scopus 로고
    • Plasma kallikrein and Hageman factor in gram-negative bacteremia
    • Mason J.W., Kleeberg U., Dolan P., Colman R.W. Plasma kallikrein and Hageman factor in gram-negative bacteremia. Ann. Internal Med. 73:1970;545-551
    • (1970) Ann. Internal Med. , vol.73 , pp. 545-551
    • Mason, J.W.1    Kleeberg, U.2    Dolan, P.3    Colman, R.W.4
  • 134
    • 0015364724 scopus 로고
    • Inhibitors of kallikrein in human plasma
    • McConnell D.J. Inhibitors of kallikrein in human plasma. J. Clin. Invest. 51:1972;1611-1623
    • (1972) J. Clin. Invest. , vol.51 , pp. 1611-1623
    • McConnell, D.J.1
  • 136
    • 0017734538 scopus 로고
    • Activation and function of human Hageman factor: The role of high molecular weight kininogen and prekallikrein
    • Meier H.L., Pierce J.V., Colman R.W., Kaplan A.P. Activation and function of human Hageman factor: The role of high molecular weight kininogen and prekallikrein. J. Clin. Invest. 60:1977;18-31
    • (1977) J. Clin. Invest. , vol.60 , pp. 18-31
    • Meier, H.L.1    Pierce, J.V.2    Colman, R.W.3    Kaplan, A.P.4
  • 137
    • 0019774267 scopus 로고
    • Dextran sulphate stimulated fibrinolytic activity in whole human plasma: Dependence on the contact activation system and on a urokinase-related antigen [abstract]
    • Miles L.A., Rothschild Z., Griffin J.H. Dextran sulphate stimulated fibrinolytic activity in whole human plasma: Dependence on the contact activation system and on a urokinase-related antigen [abstract]. Thromb. Haemost. 46:1981;211
    • (1981) Thromb. Haemost. , vol.46 , pp. 211
    • Miles, L.A.1    Rothschild, Z.2    Griffin, J.H.3
  • 138
    • 0020673587 scopus 로고
    • A comparison of the abilities of plasma kallikrein, β-factor XIIa, factor XIa and urokinase to activate plasminogen
    • Miles L.A., Greengard J.S., Griffin J.H. A comparison of the abilities of plasma kallikrein, β-factor XIIa, factor XIa and urokinase to activate plasminogen. Thromb. Res. 29:1983a;407-417
    • (1983) Thromb. Res. , vol.29 , pp. 407-417
    • Miles, L.A.1    Greengard, J.S.2    Griffin, J.H.3
  • 139
    • 0020672163 scopus 로고
    • Dextran sulfate-dependent fibrinolysis in whole human plasma
    • Miles L.A., Rothschild Z., Griffin J.H. Dextran sulfate-dependent fibrinolysis in whole human plasma. J. Lab. Clin. Med. 101:1983b;214-225
    • (1983) J. Lab. Clin. Med. , vol.101 , pp. 214-225
    • Miles, L.A.1    Rothschild, Z.2    Griffin, J.H.3
  • 140
    • 0019827081 scopus 로고
    • Studies on human high molecular weight (HMW) kininogen. II. Structural change of HMW kininogen by the action of human plasma kallikrein
    • Mori K., Nagasawa S. Studies on human high molecular weight (HMW) kininogen. II. Structural change of HMW kininogen by the action of human plasma kallikrein. J. Biochem. 89:1981;1465-1473
    • (1981) J. Biochem. , vol.89 , pp. 1465-1473
    • Mori, K.1    Nagasawa, S.2
  • 141
    • 0019410067 scopus 로고
    • Studies on human high molecular weight (HMW) kininogen. III. Cleavage of HMW kininogen by the action of human salivary kallikrein
    • Mori K., Sakamoto W., Nagasawa S. Studies on human high molecular weight (HMW) kininogen. III. Cleavage of HMW kininogen by the action of human salivary kallikrein. J. Biochem. 90:1981;503-509
    • (1981) J. Biochem. , vol.90 , pp. 503-509
    • Mori, K.1    Sakamoto, W.2    Nagasawa, S.3
  • 142
    • 0031973492 scopus 로고    scopus 로고
    • High molecular weight kininogen regulates prekallikrein assembly and activation on endothelial cells: A novel mechanism for contact activation
    • Motta G., Rojkjaer R., Hasan A.A., Cines D.B., Schmaier A.H. High molecular weight kininogen regulates prekallikrein assembly and activation on endothelial cells: A novel mechanism for contact activation. Blood. 91:1998;516-528
    • (1998) Blood , vol.91 , pp. 516-528
    • Motta, G.1    Rojkjaer, R.2    Hasan, A.A.3    Cines, D.B.4    Schmaier, A.H.5
  • 143
    • 0034839624 scopus 로고    scopus 로고
    • Assembly of high molecular weight kininogen and activation of prekallikrein on cell matrix
    • Motta G., Shariat-Madar Z., Mahdi F., Sampaio C.A., Schmaier A.H. Assembly of high molecular weight kininogen and activation of prekallikrein on cell matrix. Thromb. Haemost. 86:2001;840-847
    • (2001) Thromb. Haemost. , vol.86 , pp. 840-847
    • Motta, G.1    Shariat-Madar, Z.2    Mahdi, F.3    Sampaio, C.A.4    Schmaier, A.H.5
  • 144
    • 0021876151 scopus 로고
    • Human plasma kininogens are identical with α-cysteine proteinase inhibitors: Evidence from immunological, enzymological and sequence data
    • Muller-Esterl W., Fritz H., Machleidt W., Ritonja A., Brzin J., Kotnik M., Turk V., Kellermann J., Lottspeich F. Human plasma kininogens are identical with α-cysteine proteinase inhibitors: Evidence from immunological, enzymological and sequence data. FEBS Lett. 182:1985a;310-314
    • (1985) FEBS Lett. , vol.182 , pp. 310-314
    • Muller-Esterl, W.1    Fritz, H.2    MacHleidt, W.3    Ritonja, A.4    Brzin, J.5    Kotnik, M.6    Turk, V.7    Kellermann, J.8    Lottspeich, F.9
  • 145
    • 0021874739 scopus 로고
    • Limited proteolysis of human low-molecular-mass kininogen by tissue kallikrein: Isolation and characterization of the heavy and the light chains
    • Muller-Esterl W., Rauth G., Lottspeich F., Kellermann J., Henschen A. Limited proteolysis of human low-molecular-mass kininogen by tissue kallikrein: Isolation and characterization of the heavy and the light chains. Eur. J. Biochem. 149:1985b;15-22
    • (1985) Eur. J. Biochem. , vol.149 , pp. 15-22
    • Muller-Esterl, W.1    Rauth, G.2    Lottspeich, F.3    Kellermann, J.4    Henschen, A.5
  • 146
    • 0019955184 scopus 로고
    • Identification of plasma kallikrein as an activator of latent collagenase in rheumatoid synovial fluid
    • Nagase H., Cawston T.E., De Silva M., Barrett A.J. Identification of plasma kallikrein as an activator of latent collagenase in rheumatoid synovial fluid. Biochim. Biophys. Acta. 702:1982;133-142
    • (1982) Biochim. Biophys. Acta , vol.702 , pp. 133-142
    • Nagase, H.1    Cawston, T.E.2    De Silva, M.3    Barrett, A.J.4
  • 147
    • 0025788582 scopus 로고
    • Activation of human blood coagulation factor XI independent of factor XII: Factor XI is activated by thrombin and factor XIa in the presence of negatively charged surfaces
    • Naito K., Fujikawa K. Activation of human blood coagulation factor XI independent of factor XII: Factor XI is activated by thrombin and factor XIa in the presence of negatively charged surfaces. J. Biol. Chem. 266:1991;7353-7358
    • (1991) J. Biol. Chem. , vol.266 , pp. 7353-7358
    • Naito, K.1    Fujikawa, K.2
  • 148
    • 0036891758 scopus 로고    scopus 로고
    • Inhibition of contact activation by a kininogen peptide (HKH20) derived from domain 5
    • Nakazawa Y., Joseph K., Kaplan A.P. Inhibition of contact activation by a kininogen peptide (HKH20) derived from domain 5. Int. Immunopharmacol. 2:2002;1875-1885
    • (2002) Int. Immunopharmacol. , vol.2 , pp. 1875-1885
    • Nakazawa, Y.1    Joseph, K.2    Kaplan, A.P.3
  • 149
    • 0026788306 scopus 로고
    • Generation of vasoactive peptide bradykinin from human umbilical vein endothelium-bound high molecular weight kininogen by plasma kallikrein
    • Nishikawa K., Shibayama Y., Kuna P., Calcaterra E., Kaplan A.P., Reddigari S.R. Generation of vasoactive peptide bradykinin from human umbilical vein endothelium-bound high molecular weight kininogen by plasma kallikrein. Blood. 80:1992;1980-1988
    • (1992) Blood , vol.80 , pp. 1980-1988
    • Nishikawa, K.1    Shibayama, Y.2    Kuna, P.3    Calcaterra, E.4    Kaplan, A.P.5    Reddigari, S.R.6
  • 153
    • 0014594053 scopus 로고
    • Studies on a complex mechanism for the activation of plasminogen by kaolin and by chloroform: The participation of Hageman factor and additional cofactors
    • Ogston D., Ogston C.M., Ratnoff O.D., Forbes C.D. Studies on a complex mechanism for the activation of plasminogen by kaolin and by chloroform: The participation of Hageman factor and additional cofactors. J. Clin. Invest. 48:1969;1786-1801
    • (1969) J. Clin. Invest. , vol.48 , pp. 1786-1801
    • Ogston, D.1    Ogston, C.M.2    Ratnoff, O.D.3    Forbes, C.D.4
  • 154
    • 0015009161 scopus 로고
    • The assay of a plasma component necessary for the generation of a plasminogen activator in the presence of Hageman factor (Hageman factor co-factor)
    • Ogston D., Bennett N.B., Ogston C.M., Ratnoff O.D. The assay of a plasma component necessary for the generation of a plasminogen activator in the presence of Hageman factor (Hageman factor co-factor). Br. J. Haematol. 20:1971;209-216
    • (1971) Br. J. Haematol. , vol.20 , pp. 209-216
    • Ogston, D.1    Bennett, N.B.2    Ogston, C.M.3    Ratnoff, O.D.4
  • 155
    • 0021943946 scopus 로고
    • The regulation of human factor XIIa by plasma proteinase inhibitors
    • Pixley R.A., Schapira M., Colman R.W. The regulation of human factor XIIa by plasma proteinase inhibitors. J. Biol. Chem. 260:1985;1723-1729
    • (1985) J. Biol. Chem. , vol.260 , pp. 1723-1729
    • Pixley, R.A.1    Schapira, M.2    Colman, R.W.3
  • 156
    • 0026050747 scopus 로고
    • Effect of heparin on the activation of factor XII and the contact system in plasma [see comment]
    • Pixley R.A., Cassello A., De La Cadena R.A., Kaufman N., Colman R.W. Effect of heparin on the activation of factor XII and the contact system in plasma [see comment]. Thromb. Haemost. 66:1991;540-547
    • (1991) Thromb. Haemost. , vol.66 , pp. 540-547
    • Pixley, R.A.1    Cassello, A.2    De La Cadena, R.A.3    Kaufman, N.4    Colman, R.W.5
  • 158
    • 0027469403 scopus 로고
    • The contact system contributes to hypotension but not disseminated intravascular coagulation in lethal bacteremia: In vivo use of a monoclonal anti-factor XII antibody to block contact activation in baboons
    • Pixley R.A., De La Cadena R., Page J.D., Kaufman N., Wyshock E.G., Chang A., Taylor F.B. Jr., Colman R.W. The contact system contributes to hypotension but not disseminated intravascular coagulation in lethal bacteremia: In vivo use of a monoclonal anti-factor XII antibody to block contact activation in baboons. J. Clin. Invest. 91:1993;61-68
    • (1993) J. Clin. Invest. , vol.91 , pp. 61-68
    • Pixley, R.A.1    De La Cadena, R.2    Page, J.D.3    Kaufman, N.4    Wyshock, E.G.5    Chang, A.6    Taylor Jr., F.B.7    Colman, R.W.8
  • 159
    • 0021030001 scopus 로고
    • Kinins are generated in vivo following nasal airway challenge of allergic individuals with allergen
    • Proud D., Togias A., Naclerio R.M., Crush S.A., Norman P.S., Lichtenstein L.M. Kinins are generated in vivo following nasal airway challenge of allergic individuals with allergen. J. Clin. Invest. 72:1983;1678-1685
    • (1983) J. Clin. Invest. , vol.72 , pp. 1678-1685
    • Proud, D.1    Togias, A.2    Naclerio, R.M.3    Crush, S.A.4    Norman, P.S.5    Lichtenstein, L.M.6
  • 160
  • 161
    • 0017653036 scopus 로고
    • Activation of bovine factor VII by hageman factor fragments
    • Radcliffe R., Bagdasarian A., Colman R., Nemerson Y. Activation of bovine factor VII by hageman factor fragments. Blood. 50:1977;611-617
    • (1977) Blood , vol.50 , pp. 611-617
    • Radcliffe, R.1    Bagdasarian, A.2    Colman, R.3    Nemerson, Y.4
  • 163
    • 0014055995 scopus 로고
    • The conversion of C′IS to C′1 esterase by plasmin and trypsin
    • Ratnoff O.D., Naff G.B. The conversion of C′IS to C′1 esterase by plasmin and trypsin. J. Exp. Med. 125:1967;337-358
    • (1967) J. Exp. Med. , vol.125 , pp. 337-358
    • Ratnoff, O.D.1    Naff, G.B.2
  • 164
    • 0023949040 scopus 로고
    • Cleavage of human high-molecular weight kininogen by purified kallikreins
    • Reddigari S., Kaplan A.P. Cleavage of human high-molecular weight kininogen by purified kallikreins and upon contact activation of plasma. Blood. 71:1988;1334-1340
    • (1988) Blood , vol.71 , pp. 1334-1340
    • Reddigari, S.1    Kaplan, A.P.2
  • 165
    • 0024807696 scopus 로고
    • Studies of the cleavage of human high molecular weight kininogen by purified plasma and tissue kallikreins, and upon contact activation of plasma
    • Reddigari S., Kaplan A.P. Studies of the cleavage of human high molecular weight kininogen by purified plasma and tissue kallikreins, and upon contact activation of plasma. Adv. Exp. Med. Biol. 247B:1989;317-324
    • (1989) Adv. Exp. Med. Biol. , vol.247 , pp. 317-324
    • Reddigari, S.1    Kaplan, A.P.2
  • 166
    • 0027410345 scopus 로고
    • Human high molecular weight kininogen binds to human umbilical vein endothelial cells via its heavy and light chains
    • Reddigari S.R., Kuna P., Miragliotta G., Shibayama Y., Nishikawa K., Kaplan A.P. Human high molecular weight kininogen binds to human umbilical vein endothelial cells via its heavy and light chains. Blood. 81:1993a;1306-1311
    • (1993) Blood , vol.81 , pp. 1306-1311
    • Reddigari, S.R.1    Kuna, P.2    Miragliotta, G.3    Shibayama, Y.4    Nishikawa, K.5    Kaplan, A.P.6
  • 167
    • 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 S.R., Shibayama Y., Brunnee T., Kaplan A.P. 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. 268:1993b;11982-11987
    • (1993) J. Biol. Chem. , vol.268 , pp. 11982-11987
    • Reddigari, S.R.1    Shibayama, Y.2    Brunnee, T.3    Kaplan, A.P.4
  • 168
    • 0018995127 scopus 로고
    • Pharmacology of bradykinin and related kinins
    • Regoli D., Barabe J. Pharmacology of bradykinin and related kinins. Pharmacol. Rev. 32:1980;1-46
    • (1980) Pharmacol. Rev. , vol.32 , pp. 1-46
    • Regoli, D.1    Barabe, J.2
  • 169
    • 0034721787 scopus 로고    scopus 로고
    • High molecular weight kininogen utilizes heparan sulfate proteoglycans for accumulation on endothelial cells
    • Renne T., Dedio J., David G., Muller-Esterl W. High molecular weight kininogen utilizes heparan sulfate proteoglycans for accumulation on endothelial cells. J. Biol. Chem. 275:2000;33688-33696
    • (2000) J. Biol. Chem. , vol.275 , pp. 33688-33696
    • Renne, T.1    Dedio, J.2    David, G.3    Muller-Esterl, W.4
  • 171
    • 0016782498 scopus 로고
    • Endotoxin, prekallikrein, complement and systemic vascular resistance: Sequential measurements in man
    • Robinson J.A., Klondnycky M.L., Loeb H.S., Racic M.R., Gunnar R.M. Endotoxin, prekallikrein, complement and systemic vascular resistance: Sequential measurements in man. Am. J. Med. 59:1975;61-67
    • (1975) Am. J. Med. , vol.59 , pp. 61-67
    • Robinson, J.A.1    Klondnycky, M.L.2    Loeb, H.S.3    Racic, M.R.4    Gunnar, R.M.5
  • 172
    • 0032748421 scopus 로고    scopus 로고
    • Activation of the plasma kallikrein/kinin system on endothelial cell membranes
    • Rojkjaer R., Schmaier A.H. Activation of the plasma kallikrein/kinin system on endothelial cell membranes. Immunopharmacology. 43:1999a;109-114
    • (1999) Immunopharmacology , vol.43 , pp. 109-114
    • Rojkjaer, R.1    Schmaier, A.H.2
  • 173
    • 0033012370 scopus 로고    scopus 로고
    • Activation of the plasma kallikrein/kinin system on endothelial cells
    • Rojkjaer R., Schmaier A.H. Activation of the plasma kallikrein/kinin system on endothelial cells. Proc. Assoc. Am. Physicians. 111:1999b;220-227
    • (1999) Proc. Assoc. Am. Physicians , vol.111 , pp. 220-227
    • Rojkjaer, R.1    Schmaier, A.H.2
  • 175
    • 0022410598 scopus 로고
    • Surface-dependent activation of human factor XII (Hageman factor) by kallikrein and its light chain
    • Rosing J., Tans G., Griffin J.H. Surface-dependent activation of human factor XII (Hageman factor) by kallikrein and its light chain. Eur. J. Biochem. 151:1985;531-538
    • (1985) Eur. J. Biochem. , vol.151 , pp. 531-538
    • Rosing, J.1    Tans, G.2    Griffin, J.H.3
  • 176
    • 0019180947 scopus 로고
    • The participation of plasma thromboplastin antecedent (factor XI) in contact-activated fibrinolysis
    • Saito H. The participation of plasma thromboplastin antecedent (factor XI) in contact-activated fibrinolysis. Proc. Soc. Exp. Biol. Med. 164:1980;153-157
    • (1980) Proc. Soc. Exp. Biol. Med. , vol.164 , pp. 153-157
    • Saito, H.1
  • 177
    • 0016064395 scopus 로고
    • Defective activation of clotting, fibrinolytic, and permeability- enhancing systems in human Fletcher trait plasma
    • Saito H., Ratnoff O.D., Donaldson V.H. Defective activation of clotting, fibrinolytic, and permeability-enhancing systems in human Fletcher trait plasma. Circ. Res. 34:1974;641-651
    • (1974) Circ. Res. , vol.34 , pp. 641-651
    • Saito, H.1    Ratnoff, O.D.2    Donaldson, V.H.3
  • 178
    • 0031020877 scopus 로고    scopus 로고
    • Progress curve analysis of the kinetics with which blood coagulation factor XIa is inhibited by protease nexin-2
    • Scandura J.M., Zhang Y., Van Nostrand W.E., Walsh P.N. Progress curve analysis of the kinetics with which blood coagulation factor XIa is inhibited by protease nexin-2. Biochemistry. 36:1997;412-420
    • (1997) Biochemistry , vol.36 , pp. 412-420
    • Scandura, J.M.1    Zhang, Y.2    Van Nostrand, W.E.3    Walsh, P.N.4
  • 179
    • 0019407070 scopus 로고
    • Protection of human plasma kallikrein from inactivation by C1 inhibitor and other protease inhibitors: The role of high molecular weight kininogen
    • Schapira M., Scott C.F., Colman R.W. Protection of human plasma kallikrein from inactivation by C1 inhibitor and other protease inhibitors: The role of high molecular weight kininogen. Biochemistry. 20:1981;2738-2743
    • (1981) Biochemistry , vol.20 , pp. 2738-2743
    • Schapira, M.1    Scott, C.F.2    Colman, R.W.3
  • 181
    • 0020082693 scopus 로고
    • High molecular weight kininogen or its light chain protects human plasma kallikrein from inactivation by plasma protease inhibitors
    • Schapira M., Scott C.F., James A., Silver L.D., Kueppers F., James H.L., Colman R.W. High molecular weight kininogen or its light chain protects human plasma kallikrein from inactivation by plasma protease inhibitors. Biochemistry. 21:1982b;567-572
    • (1982) Biochemistry , vol.21 , pp. 567-572
    • Schapira, M.1    Scott, C.F.2    James, A.3    Silver, L.D.4    Kueppers, F.5    James, H.L.6    Colman, R.W.7
  • 182
    • 0020059596 scopus 로고
    • Contribution of plasma protease inhibitors to the inactivation of kallikrein in plasma
    • Schapira M., Scott C.F., Colman R.W. Contribution of plasma protease inhibitors to the inactivation of kallikrein in plasma. J. Clin. Invest. 69:1982c;462-468
    • (1982) J. Clin. Invest. , vol.69 , pp. 462-468
    • Schapira, M.1    Scott, C.F.2    Colman, R.W.3
  • 184
    • 0030758681 scopus 로고    scopus 로고
    • Contact activation: A revision
    • Schmaier A.H. Contact activation: A revision. Thromb. Haemost. 78:1997;101-107
    • (1997) Thromb. Haemost. , vol.78 , pp. 101-107
    • Schmaier, A.H.1
  • 185
    • 0031718765 scopus 로고    scopus 로고
    • Plasma contact activation: A revised hypothesis
    • Schmaier A.H. Plasma contact activation: A revised hypothesis. Biol. Res. 31:1998;251-262
    • (1998) Biol. Res. , vol.31 , pp. 251-262
    • Schmaier, A.H.1
  • 186
    • 0023797442 scopus 로고
    • The expression of high molecular weight kininogen on human umbilical vein endothelial cells
    • Schmaier A.H., Kuo A., Lundberg D., Murray S., Cines D.B. The expression of high molecular weight kininogen on human umbilical vein endothelial cells. J. Biol. Chem. 263:1988;16327-16333
    • (1988) J. Biol. Chem. , vol.263 , pp. 16327-16333
    • Schmaier, A.H.1    Kuo, A.2    Lundberg, D.3    Murray, S.4    Cines, D.B.5
  • 187
    • 0032695008 scopus 로고    scopus 로고
    • Activation of the plasma kallikrein/kinin system on cells: A revised hypothesis
    • Schmaier A.H., Rojkjaer R., Shariat-Madar Z. Activation of the plasma kallikrein/kinin system on cells: A revised hypothesis. Thromb. Haemost. 82:1999;226-233
    • (1999) Thromb. Haemost. , vol.82 , pp. 226-233
    • Schmaier, A.H.1    Rojkjaer, R.2    Shariat-Madar, Z.3
  • 188
    • 0015634027 scopus 로고
    • Inhibition by C1INH of Hagemann factor fragment activation of coagulation, fibrinolysis, and kinin generation
    • Schreiber A.D., Kaplan A.P., Austen K.F. Inhibition by C1INH of Hagemann factor fragment activation of coagulation, fibrinolysis, and kinin generation. J. Clin. Invest. 52:1973;1402-1409
    • (1973) J. Clin. Invest. , vol.52 , pp. 1402-1409
    • Schreiber, A.D.1    Kaplan, A.P.2    Austen, K.F.3
  • 189
    • 0018842614 scopus 로고
    • Function and immunochemistry of prekallikrein-high molecular weight kininogen complex in plasma
    • Scott C.F., Colman R.W. Function and immunochemistry of prekallikrein-high molecular weight kininogen complex in plasma. J. Clin. Invest. 65:1980;413-421
    • (1980) J. Clin. Invest. , vol.65 , pp. 413-421
    • Scott, C.F.1    Colman, R.W.2
  • 190
    • 0019929180 scopus 로고
    • Effect of heparin on the inactivation rate of human factor XIa by antithrombin-III
    • Scott C.F., Schapira M., Colman R.W. Effect of heparin on the inactivation rate of human factor XIa by antithrombin-III. Blood. 60:1982a;940-947
    • (1982) Blood , vol.60 , pp. 940-947
    • Scott, C.F.1    Schapira, M.2    Colman, R.W.3
  • 192
    • 0022244862 scopus 로고
    • Cleavage of human high molecular weight kininogen by factor XIa in vitro: Effect on structure and function
    • Scott C.F., Silver L.D., Purdon A.D., Colman R.W. Cleavage of human high molecular weight kininogen by factor XIa in vitro: Effect on structure and function. J. Biol. Chem. 260:1985;10856-10863
    • (1985) J. Biol. Chem. , vol.260 , pp. 10856-10863
    • Scott, C.F.1    Silver, L.D.2    Purdon, A.D.3    Colman, R.W.4
  • 193
    • 1142280091 scopus 로고
    • Initiation of plasma prorenin activation by Hageman factor-dependent conversion of plasma prekallikrein to kallikrein
    • Sealey J.E., Atlas S.A., Laragh J.H., Silverberg M., Kaplan A.P. Initiation of plasma prorenin activation by Hageman factor-dependent conversion of plasma prekallikrein to kallikrein. Proc. Natl. Acad. Sci. USA. 76:1979;5914-5918
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 5914-5918
    • Sealey, J.E.1    Atlas, S.A.2    Laragh, J.H.3    Silverberg, M.4    Kaplan, A.P.5
  • 194
    • 0018731365 scopus 로고
    • Activation of human factor VII in plasma and in purified systems: Roles of activated factor IX, kallikrein, and activated factor XII
    • Seligsohn U., Osterud B., Brown S.F., Griffin J.H., Rapaport S.I. Activation of human factor VII in plasma and in purified systems: Roles of activated factor IX, kallikrein, and activated factor XII. J. Clin. Invest. 64:1979;1056-1065
    • (1979) J. Clin. Invest. , vol.64 , pp. 1056-1065
    • Seligsohn, U.1    Osterud, B.2    Brown, S.F.3    Griffin, J.H.4    Rapaport, S.I.5
  • 195
    • 0033548677 scopus 로고    scopus 로고
    • Mapping binding domains of kininogens on endothelial cell cytokeratin 1
    • Shariat-Madar Z., Mahdi F., Schmaier A.H. Mapping binding domains of kininogens on endothelial cell cytokeratin 1. J. Biol. Chem. 274:1999;7137-7145
    • (1999) J. Biol. Chem. , vol.274 , pp. 7137-7145
    • Shariat-Madar, Z.1    Mahdi, F.2    Schmaier, A.H.3
  • 196
    • 0035085180 scopus 로고    scopus 로고
    • Factor XI assembly and activation on human umbilical vein endothelial cells in culture
    • Shariat-Madar Z., Mahdi F., Schmaier A.H. Factor XI assembly and activation on human umbilical vein endothelial cells in culture. Thromb. Haemost. 85:2001;544-551
    • (2001) Thromb. Haemost. , vol.85 , pp. 544-551
    • Shariat-Madar, Z.1    Mahdi, F.2    Schmaier, A.H.3
  • 197
    • 0037124049 scopus 로고    scopus 로고
    • Identification and characterization of prolylcarboxypeptidase as an endothelial cell prekallikrein activator
    • Shariat-Madar Z., Mahdi F., Schmaier A.H. Identification and characterization of prolylcarboxypeptidase as an endothelial cell prekallikrein activator. J. Biol. Chem. 277:2002;17962-17969
    • (2002) J. Biol. Chem. , vol.277 , pp. 17962-17969
    • Shariat-Madar, Z.1    Mahdi, F.2    Schmaier, A.H.3
  • 198
    • 0015531064 scopus 로고
    • Tranexamic acid therapy in hereditary angioneurotic edema
    • Sheffer A.L., Austen K.F., Rosen F.S. Tranexamic acid therapy in hereditary angioneurotic edema. N. Engl. J. Med. 287:1972;452-454
    • (1972) N. Engl. J. Med. , vol.287 , pp. 452-454
    • Sheffer, A.L.1    Austen, K.F.2    Rosen, F.S.3
  • 199
  • 200
    • 0022493752 scopus 로고
    • Studies of the digestion of bradykinin, lysyl bradykinin, and kinin-degradation products by carboxypeptidases A, B, and N
    • Sheikh I.A., Kaplan A.P. Studies of the digestion of bradykinin, lysyl bradykinin, and kinin-degradation products by carboxypeptidases A, B, and N. Biochem. Pharmacol. 35:1986b;1957-1963
    • (1986) Biochem. Pharmacol. , vol.35 , pp. 1957-1963
    • Sheikh, I.A.1    Kaplan, A.P.2
  • 201
    • 0024808492 scopus 로고
    • The mechanism of degradation of bradykinin (lysyl-bradykinin) in human serum
    • Sheikh I.A., Kaplan A.P. The mechanism of degradation of bradykinin (lysyl-bradykinin) in human serum. Adv. Exp. Med. Biol. 247A:1989a;331-336
    • (1989) Adv. Exp. Med. Biol. , vol.247 , pp. 331-336
    • Sheikh, I.A.1    Kaplan, A.P.2
  • 202
    • 0024581756 scopus 로고
    • Mechanism of digestion of bradykinin and lysylbradykinin (kallidin) in human serum: Role of carboxypeptidase, angiotensin-converting enzyme and determination of final degradation products
    • Sheikh I.A., Kaplan A.P. Mechanism of digestion of bradykinin and lysylbradykinin (kallidin) in human serum: Role of carboxypeptidase, angiotensin-converting enzyme and determination of final degradation products. Biochem. Pharmacol. 38:1989b;993-1000
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 993-1000
    • Sheikh, I.A.1    Kaplan, A.P.2
  • 204
    • 0028364334 scopus 로고
    • Hereditary angioneurotic oedema: Characterization of plasma kinin and vascular permeability-enhancing activities
    • Shoemaker L.R., Schurman S.J., Donaldson V.H., Davis A.E. III. Hereditary angioneurotic oedema: Characterization of plasma kinin and vascular permeability-enhancing activities. Clin. Exp. Immunol. 95:1994;22-28
    • (1994) Clin. Exp. Immunol. , vol.95 , pp. 22-28
    • Shoemaker, L.R.1    Schurman, S.J.2    Donaldson, V.H.3    Davis III, A.E.4
  • 206
    • 0019952023 scopus 로고
    • Enzymatic activities of activated and zymogen forms of human Hageman factor (factor XII)
    • Silverberg M., Kaplan A.P. Enzymatic activities of activated and zymogen forms of human Hageman factor (factor XII). Blood. 60:1982;64-70
    • (1982) Blood , vol.60 , pp. 64-70
    • Silverberg, M.1    Kaplan, A.P.2
  • 207
    • 0019197848 scopus 로고
    • Autoactivation of human Hageman factor: Demonstration utilizing a synthetic substrate
    • Silverberg M., Dunn J.T., Garen L., Kaplan A.P. Autoactivation of human Hageman factor: Demonstration utilizing a synthetic substrate. J. Biol. Chem. 255:1980a;7281-7286
    • (1980) J. Biol. Chem. , vol.255 , pp. 7281-7286
    • Silverberg, M.1    Dunn, J.T.2    Garen, L.3    Kaplan, A.P.4
  • 208
    • 0019165199 scopus 로고
    • The mechanism by which the light chain of cleaved HMW-kininogen augments the activation of prekallikrein, factor XI and Hageman factor
    • Silverberg M., Nicoll J.E., Kaplan A.P. The mechanism by which the light chain of cleaved HMW-kininogen augments the activation of prekallikrein, factor XI and Hageman factor. Thromb. Res. 20:1980b;173-189
    • (1980) Thromb. Res. , vol.20 , pp. 173-189
    • Silverberg, M.1    Nicoll, J.E.2    Kaplan, A.P.3
  • 209
    • 0022978944 scopus 로고
    • Study of the effect of high molecular weight kininogen upon the fluid-phase inactivation of kallikrein by C1 inhibitor
    • Silverberg M., Longo J., Kaplan A.P. Study of the effect of high molecular weight kininogen upon the fluid-phase inactivation of kallikrein by C1 inhibitor. J. Biol. Chem. 261:1986;14965-14968
    • (1986) J. Biol. Chem. , vol.261 , pp. 14965-14968
    • Silverberg, M.1    Longo, J.2    Kaplan, A.P.3
  • 210
    • 0021241860 scopus 로고
    • Blood coagulation factor XIa binds specifically to a site on activated human platelets distinct from that for factor XI
    • Sinha D., Seaman F.S., Koshy A., Knight L.C., Walsh P.N. Blood coagulation factor XIa binds specifically to a site on activated human platelets distinct from that for factor XI. J. Clin. Invest. 73:1984;1550-1556
    • (1984) J. Clin. Invest. , vol.73 , pp. 1550-1556
    • Sinha, D.1    Seaman, F.S.2    Koshy, A.3    Knight, L.C.4    Walsh, P.N.5
  • 211
    • 0021930258 scopus 로고
    • Tissue plasminogen activator release in vivo in response to vasoactive agents
    • Smith D., Gilbert M., Owen W.G. Tissue plasminogen activator release in vivo in response to vasoactive agents. Blood. 66:1985;835-839
    • (1985) Blood , vol.66 , pp. 835-839
    • Smith, D.1    Gilbert, M.2    Owen, W.G.3
  • 212
    • 0017167631 scopus 로고
    • Inhibition of activated factor XII by antithrombin-heparin cofactor
    • Stead N., Kaplan A.P., Rosenberg R.D. Inhibition of activated factor XII by antithrombin-heparin cofactor. J. Biol. Chem. 251:1976;6481-6488
    • (1976) J. Biol. Chem. , vol.251 , pp. 6481-6488
    • Stead, N.1    Kaplan, A.P.2    Rosenberg, R.D.3
  • 215
    • 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 J.F., 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. 261:1986;15396-15401
    • (1986) J. Biol. Chem. , vol.261 , pp. 15396-15401
    • Tait, J.F.1    Fujikawa, K.2
  • 216
    • 0023257512 scopus 로고
    • Primary structure requirements for the binding of human high molecular weight kininogen to plasma prekallikrein and factor XI
    • Tait J.F., Fujikawa K. Primary structure requirements for the binding of human high molecular weight kininogen to plasma prekallikrein and factor XI. J. Biol. Chem. 262:1987;11651-11656
    • (1987) J. Biol. Chem. , vol.262 , pp. 11651-11656
    • Tait, J.F.1    Fujikawa, K.2
  • 217
    • 0014607319 scopus 로고
    • A radioimmunoassay for bradykinin in plasma and synovial fluid
    • Talamo R.C., Haber E., Austen K.F. A radioimmunoassay for bradykinin in plasma and synovial fluid. J. Lab. Clin. Med. 74:1969;816-827
    • (1969) J. Lab. Clin. Med. , vol.74 , pp. 816-827
    • Talamo, R.C.1    Haber, E.2    Austen, K.F.3
  • 219
    • 0021352747 scopus 로고
    • Kinetics of activation and autoactivation of human factor XII
    • Tankersley D.L., Finlayson J.S. Kinetics of activation and autoactivation of human factor XII. Biochemistry. 23:1984;273-279
    • (1984) Biochemistry , vol.23 , pp. 273-279
    • Tankersley, D.L.1    Finlayson, J.S.2
  • 220
    • 0019134970 scopus 로고
    • Kinetics of activation of prekallikrein by prekallikrein activator
    • Tankersley D.L., Fournel M.A., Schroeder D.D. Kinetics of activation of prekallikrein by prekallikrein activator. Biochemistry. 19:1980;3121-3127
    • (1980) Biochemistry , vol.19 , pp. 3121-3127
    • Tankersley, D.L.1    Fournel, M.A.2    Schroeder, D.D.3
  • 221
    • 0017700478 scopus 로고
    • Association of factor XI and high molecular weight kininogen in human plasma
    • Thompson R.E., Mandle R. Jr., Kaplan A.P. Association of factor XI and high molecular weight kininogen in human plasma. J. Clin. Invest. 60:1977;1376-1380
    • (1977) J. Clin. Invest. , vol.60 , pp. 1376-1380
    • Thompson, R.E.1    Mandle Jr., R.2    Kaplan, A.P.3
  • 222
    • 0000260093 scopus 로고
    • Studies of binding of prekallikrein and factor XI to high molecular weight kininogen and its light chain
    • Thompson R.E., Mandle R. Jr., Kaplan A.P. Studies of binding of prekallikrein and factor XI to high molecular weight kininogen and its light chain. Proc. Natl. Acad. Sci. USA. 76:1979;4862-4866
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4862-4866
    • Thompson, R.E.1    Mandle Jr., R.2    Kaplan, A.P.3
  • 223
  • 226
    • 0020629994 scopus 로고
    • Interaction of human plasma kallikrein and its light chain with C1 inhibitor
    • van der Graaf F., Koedam J.A., Griffin J.H., Bouma B.N. Interaction of human plasma kallikrein and its light chain with C1 inhibitor. Biochemistry. 22:1983b;4860-4866
    • (1983) Biochemistry , vol.22 , pp. 4860-4866
    • Van Der Graaf, F.1    Koedam, J.A.2    Griffin, J.H.3    Bouma, B.N.4
  • 227
    • 0023926495 scopus 로고
    • The binding of high molecular weight kininogen to cultured human endothelial cells
    • van Iwaarden F., de Groot P.G., Bouma B.N. The binding of high molecular weight kininogen to cultured human endothelial cells. J. Biol. Chem. 263:1988;4698-4703
    • (1988) J. Biol. Chem. , vol.263 , pp. 4698-4703
    • Van Iwaarden, F.1    De Groot, P.G.2    Bouma, B.N.3
  • 228
    • 0021877149 scopus 로고
    • Competitive antagonists of bradykinin
    • Vavrek R.J., Stewart J.M. Competitive antagonists of bradykinin. Peptides. 6:1985;161-164
    • (1985) Peptides , vol.6 , pp. 161-164
    • Vavrek, R.J.1    Stewart, J.M.2
  • 229
    • 0017180657 scopus 로고
    • Inactivation and binding of human plasma kallikrein by antithrombin III and heparin
    • Vennerod A.M., Laake K., Solberg A.K., Stromland S. Inactivation and binding of human plasma kallikrein by antithrombin III and heparin. Thromb. Res. 9:1976;457-466
    • (1976) Thromb. Res. , vol.9 , pp. 457-466
    • Vennerod, A.M.1    Laake, K.2    Solberg, A.K.3    Stromland, S.4
  • 230
    • 0028050572 scopus 로고
    • Surface independent factor XI activation by thrombin in the presence of high molecular weight kininogen
    • von dem Borne P.A., Koppelman S.J., Bouma B.N., Meijers J.C. Surface independent factor XI activation by thrombin in the presence of high molecular weight kininogen. Thromb. Haemost. 72:1994;397-402
    • (1994) Thromb. Haemost. , vol.72 , pp. 397-402
    • Von Dem Borne, P.A.1    Koppelman, S.J.2    Bouma, B.N.3    Meijers, J.C.4
  • 233
    • 0030757454 scopus 로고    scopus 로고
    • Degradation of C1-inhibitor by plasmin: Implications for the control of inflammatory processes
    • Wallace E.M., Perkins S.J., Sim R.B., Willis A.C., Feighery C., Jackson J. Degradation of C1-inhibitor by plasmin: Implications for the control of inflammatory processes. Mol. Med. 3:1997;385-396
    • (1997) Mol. Med. , vol.3 , pp. 385-396
    • Wallace, E.M.1    Perkins, S.J.2    Sim, R.B.3    Willis, A.C.4    Feighery, C.5    Jackson, J.6
  • 234
    • 0019370191 scopus 로고
    • Contributions of human platelets to the proteolytic activation of blood coagulation factors XII and XI
    • Walsh P.N., Griffin J.H. Contributions of human platelets to the proteolytic activation of blood coagulation factors XII and XI. Blood. 57:1981;106-118
    • (1981) Blood , vol.57 , pp. 106-118
    • Walsh, P.N.1    Griffin, J.H.2
  • 235
    • 0015949294 scopus 로고
    • Fletcher factor deficiency: A diminished rate of Hageman factor activation caused by absence of prekallikrein with abnormalities of coagulation, fibrinolysis, chemotactic activity, and kinin generation
    • Weiss A.S., Gallin J.I., Kaplan A.P. Fletcher factor deficiency: A diminished rate of Hageman factor activation caused by absence of prekallikrein with abnormalities of coagulation, fibrinolysis, chemotactic activity, and kinin generation. J. Clin. Invest. 53:1974;622-633
    • (1974) J. Clin. Invest. , vol.53 , pp. 622-633
    • Weiss, A.S.1    Gallin, J.I.2    Kaplan, A.P.3
  • 236
    • 0000476042 scopus 로고
    • Role of high-molecular-weight kininogen in surface-binding and activation of coagulation factor XI and prekallikrein
    • Wiggins R.C., Bouma B.N., Cochrane C.G., Griffin J.H. Role of high-molecular-weight kininogen in surface-binding and activation of coagulation factor XI and prekallikrein. Proc. Natl. Acad. Sci. USA. 74:1977;4636-4640
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 4636-4640
    • Wiggins, R.C.1    Bouma, B.N.2    Cochrane, C.G.3    Griffin, J.H.4
  • 237
    • 0015762999 scopus 로고
    • Prekallikrein deficiency in man
    • Wuepper K.D. Prekallikrein deficiency in man. J. Exp. Med. 138:1973;1345-1355
    • (1973) J. Exp. Med. , vol.138 , pp. 1345-1355
    • Wuepper, K.D.1
  • 238
    • 0016787047 scopus 로고
    • Flaujeac trait: Deficiency of human plasma kininogen
    • Wuepper K.D., Miller D.R., Lacombe M.J. Flaujeac trait: Deficiency of human plasma kininogen. J. Clin. Invest. 56:1975;1663-1672
    • (1975) J. Clin. Invest. , vol.56 , pp. 1663-1672
    • Wuepper, K.D.1    Miller, D.R.2    Lacombe, M.J.3
  • 239
    • 0028965130 scopus 로고
    • Inactivation of factor XIa in human plasma assessed by measuring factor XIa-protease inhibitor complexes: Major role for C1-inhibitor
    • Wuillemin W.A., Minnema M., Meijers J.C., Roem D., Eerenberg A.J., Nuijens J.H., ten Cate H., Hack C.E. Inactivation of factor XIa in human plasma assessed by measuring factor XIa-protease inhibitor complexes: Major role for C1-inhibitor. Blood. 85:1995;1517-1526
    • (1995) Blood , vol.85 , pp. 1517-1526
    • Wuillemin, W.A.1    Minnema, M.2    Meijers, J.C.3    Roem, D.4    Eerenberg, A.J.5    Nuijens, J.H.6    Ten Cate, H.7    Hack, C.E.8
  • 240
    • 15844367087 scopus 로고    scopus 로고
    • Modulation of contact system proteases by glycosaminoglycans: Selective enhancement of the inhibition of factor XIa
    • Wuillemin W.A., Eldering E., Citarella F., de Ruig C.P., ten Cate H., Hack C.E. Modulation of contact system proteases by glycosaminoglycans: Selective enhancement of the inhibition of factor XIa. J. Biol. Chem. 271:1996;12913-12918
    • (1996) J. Biol. Chem. , vol.271 , pp. 12913-12918
    • Wuillemin, W.A.1    Eldering, E.2    Citarella, F.3    De Ruig, C.P.4    Ten Cate, H.5    Hack, C.E.6
  • 241
    • 0014214810 scopus 로고
    • Second kininase in human blood plasma
    • Yang H.Y., Erdos E.G. Second kininase in human blood plasma. Nature. 215:1967;1402-1403
    • (1967) Nature , vol.215 , pp. 1402-1403
    • Yang, H.Y.1    Erdos, E.G.2
  • 242
    • 0018762660 scopus 로고
    • Isolation of completely inactive plasma prorenin and its activation by kallikreins: A possible new link between renin and kallikrein
    • Yokosawa N., Takahashi N., Inagami T., Page D.L. Isolation of completely inactive plasma prorenin and its activation by kallikreins: A possible new link between renin and kallikrein. Biochim. Biophys. Acta. 569:1979;211-219
    • (1979) Biochim. Biophys. Acta. , vol.569 , pp. 211-219
    • Yokosawa, N.1    Takahashi, N.2    Inagami, T.3    Page, D.L.4
  • 243
    • 0028909546 scopus 로고
    • Unique C1 inhibitor dysfunction in a kindred without angioedema. II. Identification of an Ala443 → Val substitution and functional analysis of the recombinant mutant protein
    • Zahedi R., Bissler J.J., Davis A.E. III, Andreadis C., Wisnieski J.J. Unique C1 inhibitor dysfunction in a kindred without angioedema. II. Identification of an Ala443 → Val substitution and functional analysis of the recombinant mutant protein. J. Clin. Invest. 95:1995;1299-1305
    • (1995) J. Clin. Invest. , vol.95 , pp. 1299-1305
    • Zahedi, R.1    Bissler, J.J.2    Davis III, A.E.3    Andreadis, C.4    Wisnieski, J.J.5
  • 244
    • 0031570956 scopus 로고    scopus 로고
    • Role of the P2 residue of complement 1 inhibitor (Ala443) in determination of target protease specificity: Inhibition of complement and contact system proteases
    • Zahedi R., Wisnieski J., Davis A.E. III. Role of the P2 residue of complement 1 inhibitor (Ala443) in determination of target protease specificity: Inhibition of complement and contact system proteases. J. Immunol. 159:1997;983-988
    • (1997) J. Immunol. , vol.159 , pp. 983-988
    • Zahedi, R.1    Wisnieski, J.2    Davis III, A.E.3
  • 245
    • 0030671397 scopus 로고    scopus 로고
    • The mechanism by which heparin promotes the inhibition of coagulation factor XIa by protease nexin-2
    • Zhang Y., Scandura J.M., Van Nostrand W.E., Walsh P.N. The mechanism by which heparin promotes the inhibition of coagulation factor XIa by protease nexin-2. J. Biol. Chem. 272:1997;26139-26144
    • (1997) J. Biol. Chem. , vol.272 , pp. 26139-26144
    • Zhang, Y.1    Scandura, J.M.2    Van Nostrand, W.E.3    Walsh, P.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.