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Volumn 90, Issue 10, 1997, Pages 3819-3843

Contact system: A vascular biology modulator with anticoagulant, profibrinolytic, antiadhesive, and proinflammatory attributes

Author keywords

[No Author keywords available]

Indexed keywords

KININOGEN; PREKALLIKREIN;

EID: 0030830360     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v90.10.3819     Document Type: Review
Times cited : (544)

References (296)
  • 1
    • 84931128415 scopus 로고
    • Bradykinin, a hypotensive and smooth muscle stimulating factor released from plasma globulin by snake venoms and by trypsin
    • Roche e Silva M, Beraldo WT, Rosenfeld G: Bradykinin, a hypotensive and smooth muscle stimulating factor released from plasma globulin by snake venoms and by trypsin. Am J Physiol 150:261, 1949
    • (1949) Am J Physiol , vol.150 , pp. 261
    • Roche E Silva, M.1    Beraldo, W.T.2    Rosenfeld, G.3
  • 2
    • 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 RW, Bagdasarian A, Talamo RC, Scott CF, Seavey M, Guimaraes JA, Pierce JV, Kaplan AP: 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 56:1650, 1975
    • (1975) J Clin Invest , vol.56 , pp. 1650
    • 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
  • 3
    • 0016787047 scopus 로고
    • Flaujeac trait. Deficiency of human plasma kininogen
    • Wuepper KD, Miller DR, Lacombe MJ: Flaujeac trait. Deficiency of human plasma kininogen. J Clin Invest 56:1663, 1975
    • (1975) J Clin Invest , vol.56 , pp. 1663
    • Wuepper, K.D.1    Miller, D.R.2    Lacombe, M.J.3
  • 4
    • 0016736847 scopus 로고
    • Fitzgerald trait: Deficiency of a hitherto unrecognized agent, Fitzgerald factor, participating in surface mediated reactions of clotting, fibrinolysis, generation of kinins, and the property of diluted plasma enhancing vascular permeability (PF/DIL)
    • Saito H, Ratnoff OD, Waldmann R, Abraham JP: Fitzgerald trait: Deficiency of a hitherto unrecognized agent, Fitzgerald factor, participating in surface mediated reactions of clotting, fibrinolysis, generation of kinins, and the property of diluted plasma enhancing vascular permeability (PF/DIL). J Clin Invest 55:1082, 1975
    • (1975) J Clin Invest , vol.55 , pp. 1082
    • Saito, H.1    Ratnoff, O.D.2    Waldmann, R.3    Abraham, J.P.4
  • 5
    • 0021800408 scopus 로고
    • Cloning and sequence analysis of cDNAs for human high molecular weight and low molecular weight prekininogens. Primary structures of two human prekininogens
    • Takagaki Y, Kitamura N, Nakanishi S: Cloning and sequence analysis of cDNAs for human high molecular weight and low molecular weight prekininogens. Primary structures of two human prekininogens. J Biol Chem 260:8601, 1985
    • (1985) J Biol Chem , vol.260 , pp. 8601
    • Takagaki, Y.1    Kitamura, N.2    Nakanishi, S.3
  • 7
    • 0025772329 scopus 로고
    • The human kininogen gene (KNG) mapped to chromosome 3q26-qter by analysis of somatic cell hybrids using the polymerase chain reaction
    • Fong D, Smith DI, Hsieh WT: The human kininogen gene (KNG) mapped to chromosome 3q26-qter by analysis of somatic cell hybrids using the polymerase chain reaction. Hum Genet 87:189, 1991
    • (1991) Hum Genet , vol.87 , pp. 189
    • Fong, D.1    Smith, D.I.2    Hsieh, W.T.3
  • 9
    • 0028938024 scopus 로고
    • Three members of the human cystatin gene superfamily, AHSG, HRG, and KNG, map within one megabase of genomic DNA at 3q27
    • Rizzu P, Baldini A: Three members of the human cystatin gene superfamily, AHSG, HRG, and KNG, map within one megabase of genomic DNA at 3q27. Cytogenet Cell Genet 70:26, 1995
    • (1995) Cytogenet Cell Genet , vol.70 , pp. 26
    • Rizzu, P.1    Baldini, A.2
  • 10
    • 0025281441 scopus 로고
    • A set of U1 snRNA-complementary sequences involved in governing alternative RNA splicing of the kininogen genes
    • Kakizuka A, Ingi T, Murai T, Nakanishi S: A set of U1 snRNA-complementary sequences involved in governing alternative RNA splicing of the kininogen genes. J Biol Chem 265:10102, 1990
    • (1990) J Biol Chem , vol.265 , pp. 10102
    • Kakizuka, A.1    Ingi, T.2    Murai, T.3    Nakanishi, S.4
  • 12
    • 0027182033 scopus 로고
    • A point mutation of alanine 163 to threonine is responsible for the defective secretion of high molecular weight kininogen by the liver of brown Norway Katholiek rats
    • Hayashi I, Hoshiko S, Makabe O, Oh-ishi S: A point mutation of alanine 163 to threonine is responsible for the defective secretion of high molecular weight kininogen by the liver of brown Norway Katholiek rats. J Biol Chem 268:17219, 1993
    • (1993) J Biol Chem , vol.268 , pp. 17219
    • Hayashi, I.1    Hoshiko, S.2    Makabe, O.3    Oh-ishi, S.4
  • 13
    • 0026623460 scopus 로고
    • Differential regulation of kininogen gene expression by estrogen and progesterone in vivo
    • Chen LM, Chung P, Chao S, Chao L, Chao J: Differential regulation of kininogen gene expression by estrogen and progesterone in vivo. Biochim Biophys Acta 1131:145, 1992
    • (1992) Biochim Biophys Acta , vol.1131 , pp. 145
    • Chen, L.M.1    Chung, P.2    Chao, S.3    Chao, L.4    Chao, J.5
  • 15
    • 0028941346 scopus 로고
    • Murine fibroblasts synthesize and secrete kininogen in response to eyclic-AMP, prostaglandin E2 and tumor necrosis factor
    • Takano M, Yokoyama K, Yayama K, Okamoto H: Murine fibroblasts synthesize and secrete kininogen in response to eyclic-AMP, prostaglandin E2 and tumor necrosis factor. Biochim Biophys Acta 1265:189, 1995
    • (1995) Biochim Biophys Acta , vol.1265 , pp. 189
    • Takano, M.1    Yokoyama, K.2    Yayama, K.3    Okamoto, H.4
  • 16
    • 0026584593 scopus 로고
    • Sensitive antigenic determinations of high molecular weight kininogen performed by covalent coupling of capture antibody
    • Scott CF, Colman RW: Sensitive antigenic determinations of high molecular weight kininogen performed by covalent coupling of capture antibody. J Lab Clin Med 119:77, 1992
    • (1992) J Lab Clin Med , vol.119 , pp. 77
    • Scott, C.F.1    Colman, R.W.2
  • 17
    • 84981837744 scopus 로고
    • Some data on two purified kininogens from human plasma
    • Jacobsen S, Kriz M: Some data on two purified kininogens from human plasma. Br J Pharmacol 29:25, 1967
    • (1967) Br J Pharmacol , vol.29 , pp. 25
    • Jacobsen, S.1    Kriz, M.2
  • 20
    • 0023797442 scopus 로고
    • The expression of high molecular weight kininogen on human umbilical vein endothelial cells
    • Schmaier AH, Kuo A, Lundberg D, Murray S, Cines DB: The expression of high molecular weight kininogen on human umbilical vein endothelial cells. J Biol Chem 263:16327, 1988
    • (1988) J Biol Chem , vol.263 , pp. 16327
    • Schmaier, A.H.1    Kuo, A.2    Lundberg, D.3    Murray, S.4    Cines, D.B.5
  • 24
    • 0023659241 scopus 로고
    • Interstitial-tissue localization of high-molecular-weight kininogen in guinea-pig skin
    • Yamamoto T, Tsuruta J, Kambara T: Interstitial-tissue localization of high-molecular-weight kininogen in guinea-pig skin. Biochim Biophys Acta 916:332, 1987
    • (1987) Biochim Biophys Acta , vol.916 , pp. 332
    • Yamamoto, T.1    Tsuruta, J.2    Kambara, T.3
  • 25
    • 0021676017 scopus 로고
    • Isolation of a human cDNa for alpha 2-thiol proteinase inhibitor and its identity with low molecular weight kininogen
    • Ohkubo I, Kurachi K, Takasawa T, Shiokawa H, Sasaki M: Isolation of a human cDNA for alpha 2-thiol proteinase inhibitor and its identity with low molecular weight kininogen. Biochemistry 23:5691, 1984
    • (1984) Biochemistry , vol.23 , pp. 5691
    • Ohkubo, I.1    Kurachi, K.2    Takasawa, T.3    Shiokawa, H.4    Sasaki, M.5
  • 26
    • 0028200808 scopus 로고
    • The shape of high molecular weight kininogen: Organization into structural domains, changes with activation, and interactions with prekallikrein, as determined by electron microscopy
    • Weisel JW, Nagaswami C, Woodhead JL, DeLa Cadena RA, Page JD, Colman RW: The shape of high molecular weight kininogen: Organization into structural domains, changes with activation, and interactions with prekallikrein, as determined by electron microscopy. J Biol Chem 269:10100, 1994
    • (1994) J Biol Chem , vol.269 , pp. 10100
    • Weisel, J.W.1    Nagaswami, C.2    Woodhead, J.L.3    DeLa Cadena, R.A.4    Page, J.D.5    Colman, R.W.6
  • 27
    • 0022555509 scopus 로고
    • Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases
    • Salvesen G, Parkes C, Abrahamson M, Grubb A, Barrett AJ: Human low-Mr kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases. Biochem J 234:429, 1986
    • (1986) Biochem J , vol.234 , pp. 429
    • Salvesen, G.1    Parkes, C.2    Abrahamson, M.3    Grubb, A.4    Barrett, A.J.5
  • 28
    • 0023100566 scopus 로고
    • Determination of the bifunctional properties of high molecular weight kininogen by studies with monoclonal antibodies directed to each of its chains
    • Schmaier AH, Schutsky D, Farber A, Silver LD, Bradford HN, Colman RW: Determination of the bifunctional properties of high molecular weight kininogen by studies with monoclonal antibodies directed to each of its chains. J Biol Chem 262:1405, 1987
    • (1987) J Biol Chem , vol.262 , pp. 1405
    • Schmaier, A.H.1    Schutsky, D.2    Farber, A.3    Silver, L.D.4    Bradford, H.N.5    Colman, R.W.6
  • 29
    • 0024208268 scopus 로고
    • Proteinase-sensitive regions in the heavy chain of low molecular weight kininogen map to the inter-domain junctions
    • Vogel R, Assfalg-Machleidt I, Esterl A, Machleidt W, Muller-Esterl W: Proteinase-sensitive regions in the heavy chain of low molecular weight kininogen map to the inter-domain junctions. J Biol Chem 263:12661, 1988
    • (1988) J Biol Chem , vol.263 , pp. 12661
    • Vogel, R.1    Assfalg-Machleidt, I.2    Esterl, A.3    Machleidt, W.4    Muller-Esterl, W.5
  • 30
    • 0027370885 scopus 로고
    • Contiguous binding and inhibitory sites on kininogens required for the inhibition of platelet calpain
    • Bradford HN, Jameson BA, Adam AA, Wassell RP, Colman RW: Contiguous binding and inhibitory sites on kininogens required for the inhibition of platelet calpain. J Biol Chem 268:26546, 1993
    • (1993) J Biol Chem , vol.268 , pp. 26546
    • Bradford, H.N.1    Jameson, B.A.2    Adam, A.A.3    Wassell, R.P.4    Colman, R.W.5
  • 31
    • 0029076637 scopus 로고
    • High-molecular-weight kininogen is exclusively membrane bound on endothelial cells to influence activation of vascular endothelium
    • Hasan AA, Cines DB, Ngaiza JR, Jaffe EA, Schmaier AH: High-molecular-weight kininogen is exclusively membrane bound on endothelial cells to influence activation of vascular endothelium. Blood 85:3134, 1995
    • (1995) Blood , vol.85 , pp. 3134
    • Hasan, A.A.1    Cines, D.B.2    Ngaiza, J.R.3    Jaffe, E.A.4    Schmaier, A.H.5
  • 32
    • 0028879618 scopus 로고
    • Conformational changes in low molecular weight kininogen alters its ability to bind to endothelial cells
    • Hasan AA, Zhang J, Samuel M, Schmaier AH: Conformational changes in low molecular weight kininogen alters its ability to bind to endothelial cells. Thromb Haemost 74:1088, 1995
    • (1995) Thromb Haemost , vol.74 , pp. 1088
    • Hasan, A.A.1    Zhang, J.2    Samuel, M.3    Schmaier, A.H.4
  • 34
    • 0023521478 scopus 로고
    • Heavy chain of human high molecular weight and low molecular weight kininogen binds calcium ion
    • Ishiguro H, Higashiyama S, Ohkubo I, Sasaki M: Heavy chain of human high molecular weight and low molecular weight kininogen binds calcium ion. Biochemistry 26:7021, 1987
    • (1987) Biochemistry , vol.26 , pp. 7021
    • Ishiguro, H.1    Higashiyama, S.2    Ohkubo, I.3    Sasaki, M.4
  • 35
    • 0027281344 scopus 로고
    • Bradykinin regulates the expression of kininogen binding sites on endothelial cells
    • Zini JM, Schmaier AH, Cines DB: Bradykinin regulates the expression of kininogen binding sites on endothelial cells. Blood 81:2936, 1993
    • (1993) Blood , vol.81 , pp. 2936
    • Zini, J.M.1    Schmaier, A.H.2    Cines, D.B.3
  • 38
    • 0023926495 scopus 로고
    • The binding of high molecular weight kininogen to cultured human endothelial cells
    • van Iwaarden F, deGroot PG, Bouma BN: The binding of high molecular weight kininogen to cultured human endothelial cells. J Biol Chem 263:4698, 1988
    • (1988) J Biol Chem , vol.263 , pp. 4698
    • Van Iwaarden, F.1    DeGroot, P.G.2    Bouma, B.N.3
  • 39
    • 0343600912 scopus 로고
    • Digestive process and regulation of renal excretory function. Pepsanurin and prokinins inhibitors of diuresis mediated by atrial natriuretic peptide
    • Croxatto HR, Boric MP, Roblero J, Albertini R, Silva R: Digestive process and regulation of renal excretory function. Pepsanurin and prokinins inhibitors of diuresis mediated by atrial natriuretic peptide. Rev Med Chile 122:1162, 1995
    • (1995) Rev Med Chile , vol.122 , pp. 1162
    • Croxatto, H.R.1    Boric, M.P.2    Roblero, J.3    Albertini, R.4    Silva, R.5
  • 40
    • 0025122795 scopus 로고
    • Kinetics of inhibition of platelet calpain II by human kininogens
    • Bradford HN, Schmaier AH, Colman RW: Kinetics of inhibition of platelet calpain II by human kininogens. Biochem J 270:83, 1990
    • (1990) Biochem J , vol.270 , pp. 83
    • Bradford, H.N.1    Schmaier, A.H.2    Colman, R.W.3
  • 42
    • 0028795423 scopus 로고
    • Interaction of cysteine proteinases with recombinant kininogen domain 2, expressed in Escherichia coli
    • Ylinenjarvi K, Prasthofer TW, Martin NC, Bjork I: Interaction of cysteine proteinases with recombinant kininogen domain 2, expressed in Escherichia coli. FEBS Lett 357:309, 1995
    • (1995) FEBS Lett , vol.357 , pp. 309
    • Ylinenjarvi, K.1    Prasthofer, T.W.2    Martin, N.C.3    Bjork, I.4
  • 43
    • 0029740267 scopus 로고    scopus 로고
    • Structural requirements for cathepsin B and cathepsin H inhibition by kininogens
    • Bano B, Kunapuli SP, Bradford HN, Colman RW: Structural requirements for cathepsin B and cathepsin H inhibition by kininogens. J Protein Chem 15:519, 1996
    • (1996) J Protein Chem , vol.15 , pp. 519
    • Bano, B.1    Kunapuli, S.P.2    Bradford, H.N.3    Colman, R.W.4
  • 44
    • 0027413558 scopus 로고
    • Purification and characterization of a potent 70-kDa thiol lysyl-proteinase (Lys-gingivain) from Porphyromonas gingivalis that cleaves kininogens and fibrinogen
    • Scott CF, Whitaker EJ, Hammond BF, Colman RW: Purification and characterization of a potent 70-kDa thiol lysyl-proteinase (Lys-gingivain) from Porphyromonas gingivalis that cleaves kininogens and fibrinogen. J Biol Chem 268:7935, 1993
    • (1993) J Biol Chem , vol.268 , pp. 7935
    • Scott, C.F.1    Whitaker, E.J.2    Hammond, B.F.3    Colman, R.W.4
  • 45
    • 0022624818 scopus 로고
    • High molecular weight kininogen: Localization in the unstimulated and activated platelet and activation by a platelet calpain(s)
    • Schmaier AH, Smith PM, Purdon AD, White JG, Colman RW: High molecular weight kininogen: Localization in the unstimulated and activated platelet and activation by a platelet calpain(s). Blood 67:119, 1986
    • (1986) Blood , vol.67 , pp. 119
    • Schmaier, A.H.1    Smith, P.M.2    Purdon, A.D.3    White, J.G.4    Colman, R.W.5
  • 48
    • 0025834590 scopus 로고
    • Low molecular weight kininogen binds to platelets to modulate thrombin-induced platelet activation
    • Meloni FJ, Schmaier AH: Low molecular weight kininogen binds to platelets to modulate thrombin-induced platelet activation. J Biol Chem 266:6786, 1991
    • (1991) J Biol Chem , vol.266 , pp. 6786
    • Meloni, F.J.1    Schmaier, A.H.2
  • 49
    • 0027410345 scopus 로고
    • Human high molecular weight kininogen binds to human umbilical vein endothelial cells via its heavy and light chains
    • Reddigari SR, Kuna P, Miragliotta G, Shibayama Y, Nishikawa K, Kaplan AP: Human high molecular weight kininogen binds to human umbilical vein endothelial cells via its heavy and light chains. Blood 81:1306, 1993
    • (1993) Blood , vol.81 , pp. 1306
    • Reddigari, S.R.1    Kuna, P.2    Miragliotta, G.3    Shibayama, Y.4    Nishikawa, K.5    Kaplan, A.P.6
  • 50
    • 0026784525 scopus 로고
    • Domain 3 of kininogens contains a cell-binding site and a site that modifies thrombin activation of platelets
    • Jiang YP, Muller Esterl W, Schmaier AH: Domain 3 of kininogens contains a cell-binding site and a site that modifies thrombin activation of platelets. J Biol Chem 267:3712, 1992
    • (1992) J Biol Chem , vol.267 , pp. 3712
    • Jiang, Y.P.1    Muller Esterl, W.2    Schmaier, A.H.3
  • 52
    • 0024066065 scopus 로고
    • The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases
    • Bode W, Engh R, Musil D, Thiele U, Huber R, Karshikov A, Brzin J, Kos J, Turk V: The 2.0 A X-ray crystal structure of chicken egg white cystatin and its possible mode of interaction with cysteine proteinases. EMBO J 7:2593, 1988
    • (1988) EMBO J , vol.7 , pp. 2593
    • Bode, W.1    Engh, R.2    Musil, D.3    Thiele, U.4    Huber, R.5    Karshikov, A.6    Brzin, J.7    Kos, J.8    Turk, V.9
  • 55
    • 0026090569 scopus 로고
    • High molecular weight kininogen inhibits thrombin-induced platelet aggregation and cleavage of aggregin by inhibiting binding of thrombin to platelets
    • Puri RN, Zhou F, Hu CJ, Colman RF, Colman RW: High molecular weight kininogen inhibits thrombin-induced platelet aggregation and cleavage of aggregin by inhibiting binding of thrombin to platelets. Blood 77:500, 1991
    • (1991) Blood , vol.77 , pp. 500
    • Puri, R.N.1    Zhou, F.2    Hu, C.J.3    Colman, R.F.4    Colman, R.W.5
  • 56
    • 0029814343 scopus 로고    scopus 로고
    • Bradykinin and its metabolite, Arg-Pro-Pro-Gly-Phe, are selective inhibitors of α-thrombin-induced platelet activation
    • Hasan AAK, Amenta S, Schmaier AH: Bradykinin and its metabolite, Arg-Pro-Pro-Gly-Phe, are selective inhibitors of α-thrombin-induced platelet activation. Circulation 94:517, 1996
    • (1996) Circulation , vol.94 , pp. 517
    • Hasan, A.A.K.1    Amenta, S.2    Schmaier, A.H.3
  • 57
    • 0029884794 scopus 로고    scopus 로고
    • Thrombin-induced platelet aggregation is inhibited by the heptapeptide Leu271-Ala277 domain 3 in the heavy chain of high molecular weight kininogen
    • Kunapuli SP, Bradford HN, Jameson BA, DeLa Cadena RA, Rick L, Wassell RP, Colman RW: Thrombin-induced platelet aggregation is inhibited by the heptapeptide Leu271-Ala277 domain 3 in the heavy chain of high molecular weight kininogen. J Biol Chem 271:11228, 1996
    • (1996) J Biol Chem , vol.271 , pp. 11228
    • Kunapuli, S.P.1    Bradford, H.N.2    Jameson, B.A.3    DeLa Cadena, R.A.4    Rick, L.5    Wassell, R.P.6    Colman, R.W.7
  • 58
    • 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 89:1465, 1981
    • (1981) J Biochem , vol.89 , pp. 1465
    • Mori, K.1    Nagasawa, S.2
  • 59
    • 0023684099 scopus 로고
    • Structural changes of plasma high molecular weight kininogen after in vitro activation and in sepsis
    • Schmaier AH, Farber A, Schein R, Sprung C: Structural changes of plasma high molecular weight kininogen after in vitro activation and in sepsis. J Lab Clin Med 112:182, 1988
    • (1988) J Lab Clin Med , vol.112 , pp. 182
    • Schmaier, A.H.1    Farber, A.2    Schein, R.3    Sprung, C.4
  • 60
    • 0028245056 scopus 로고
    • Surface-induced alterations in the kinetic pathway for cleavage of human high molecular weight kininogen by plasma kallikrein
    • Tayeh MA, Olson ST, Shore JD: Surface-induced alterations in the kinetic pathway for cleavage of human high molecular weight kininogen by plasma kallikrein. J Biol Chem 269:16318, 1994
    • (1994) J Biol Chem , vol.269 , pp. 16318
    • Tayeh, M.A.1    Olson, S.T.2    Shore, J.D.3
  • 61
    • 0020964984 scopus 로고
    • Kinin release from high molecular weight kininogen by the action of Hageman factor in the absence of kallikrein
    • Wiggins RC: Kinin release from high molecular weight kininogen by the action of Hageman factor in the absence of kallikrein. J Biol Chem 258:8963, 1983
    • (1983) J Biol Chem , vol.258 , pp. 8963
    • Wiggins, R.C.1
  • 62
    • 0022244862 scopus 로고
    • Cleavage of human high molecular weight kininogen by factor XIa in vitro. Effect on structure and function
    • Scott CF, Silver LD, Purdon AD, Colman RW: Cleavage of human high molecular weight kininogen by factor XIa in vitro. Effect on structure and function. J Biol Chem 260:10856, 1985
    • (1985) J Biol Chem , vol.260 , pp. 10856
    • Scott, C.F.1    Silver, L.D.2    Purdon, A.D.3    Colman, R.W.4
  • 63
    • 0023812659 scopus 로고
    • Mechanism of kinin release from human low-molecular-mass-kininogen by the synergistic action of human plasma kallikrein and leukocyte elastase
    • Sato F, Nagasawa S: Mechanism of kinin release from human low-molecular-mass-kininogen by the synergistic action of human plasma kallikrein and leukocyte elastase. Biol Chem Hoppe Seyler 369:1009, 1988
    • (1988) Biol Chem Hoppe Seyler , vol.369 , pp. 1009
    • Sato, F.1    Nagasawa, S.2
  • 64
    • 0023678602 scopus 로고
    • Granulocyte elastase cleaves human high molecular weight kininogen and destroys its clot-promoting activity
    • Kleniewski J, Donaldson VH: Granulocyte elastase cleaves human high molecular weight kininogen and destroys its clot-promoting activity. J Exp Med 167:1895, 1988
    • (1988) J Exp Med , vol.167 , pp. 1895
    • Kleniewski, J.1    Donaldson, V.H.2
  • 65
    • 0028034957 scopus 로고
    • The carboxyl terminus of bradykinin and amino terminus of the light chain of kininogens comprise an endothelial cell binding domain
    • Hasan AAK, Cines DB, Zhang J, Schmaier AH: The carboxyl terminus of bradykinin and amino terminus of the light chain of kininogens comprise an endothelial cell binding domain. J Biol Chem 269:31822, 1994
    • (1994) J Biol Chem , vol.269 , pp. 31822
    • Hasan, A.A.K.1    Cines, D.B.2    Zhang, J.3    Schmaier, A.H.4
  • 66
    • 0026516038 scopus 로고
    • High molecular weight kininogen binds to platelets by its heavy and light chains and when bound has altered susceptibility to kallikrein cleavage
    • Meloni FJ, Gustafson EJ, Schmaier AH: High molecular weight kininogen binds to platelets by its heavy and light chains and when bound has altered susceptibility to kallikrein cleavage. Blood 79:1233, 1992
    • (1992) Blood , vol.79 , pp. 1233
    • Meloni, F.J.1    Gustafson, E.J.2    Schmaier, A.H.3
  • 68
    • 24844450225 scopus 로고
    • The binding sites on high molecular weight kininogen (HK) to activated human neutrophils are localized to K263-Q292, Q329-M357, and H493-K520
    • abstr
    • Khan M, Punia N, Majluf-Cruz A, Kunapuli SP, Cooper SL, DeLa Cadena RA, Colman RW: The binding sites on high molecular weight kininogen (HK) to activated human neutrophils are localized to K263-Q292, Q329-M357, and H493-K520. Blood 86:33a, 1995 (abstr, suppl 1)
    • (1995) Blood , vol.86 , Issue.1 SUPPL.
    • Khan, M.1    Punia, N.2    Majluf-Cruz, A.3    Kunapuli, S.P.4    Cooper, S.L.5    DeLa Cadena, R.A.6    Colman, R.W.7
  • 69
    • 0023190486 scopus 로고
    • Effects of chemical modifications on the surface- And protein-binding properties of the light chain of human high molecular weight kininogen
    • Retzios AD, Rosenfeld R, Schiffman S: Effects of chemical modifications on the surface-and protein-binding properties of the light chain of human high molecular weight kininogen. J Biol Chem 262:3074, 1987
    • (1987) J Biol Chem , vol.262 , pp. 3074
    • Retzios, A.D.1    Rosenfeld, R.2    Schiffman, S.3
  • 70
    • 0027452929 scopus 로고
    • Deletion mutagenesis of high molecular weight kininogen light chain: Identification of two anionic surface binding subdomains
    • Kunapuli SP, DeLa Cadena RA, Colman RW: Deletion mutagenesis of high molecular weight kininogen light chain: Identification of two anionic surface binding subdomains. J Biol Chem 268:2486, 1993
    • (1993) J Biol Chem , vol.268 , pp. 2486
    • Kunapuli, S.P.1    DeLa Cadena, R.A.2    Colman, R.W.3
  • 71
    • 0024511155 scopus 로고
    • Binding of heparin to human high molecular weight kininogen
    • Bjork I, Olson ST, Sheffer RG, Shore JD: Binding of heparin to human high molecular weight kininogen. Biochemistry 28:1213, 1989
    • (1989) Biochemistry , vol.28 , pp. 1213
    • Bjork, I.1    Olson, S.T.2    Sheffer, R.G.3    Shore, J.D.4
  • 72
    • 0027070905 scopus 로고
    • The sequence HGLGHGHEQQHGLGHGH in the light chain of high molecular weight kininogen serves as a primary structural feature for zinc-dependet binding to an anionic surface
    • DeLa Cadena RA, Colman RW: The sequence HGLGHGHEQQHGLGHGH in the light chain of high molecular weight kininogen serves as a primary structural feature for zinc-dependet binding to an anionic surface. Protein Sci 1:151, 1992
    • (1992) Protein Sci , vol.1 , pp. 151
    • DeLa Cadena, R.A.1    Colman, R.W.2
  • 73
    • 0028831866 scopus 로고
    • Human kininogens interact with M protein, a bacterial surface protein and virulence determinant
    • Ben Nasr AB, Herwald H, Muller-Esterl W, Bjorck L: Human kininogens interact with M protein, a bacterial surface protein and virulence determinant. Biochem J 305:173, 1995
    • (1995) Biochem J , vol.305 , pp. 173
    • Ben Nasr, A.B.1    Herwald, H.2    Muller-Esterl, W.3    Bjorck, L.4
  • 74
    • 0021244031 scopus 로고
    • Cleavage of human high molecular weight kininogen markedly enhances its coagulant activity. Evidence that this molecule exists as a procofactor
    • Scott CF, Silver LD, Schapira M, Colman RW: Cleavage of human high molecular weight kininogen markedly enhances its coagulant activity. Evidence that this molecule exists as a procofactor. J Clin Invest 73:954, 1984
    • (1984) J Clin Invest , vol.73 , pp. 954
    • Scott, C.F.1    Silver, L.D.2    Schapira, M.3    Colman, R.W.4
  • 75
    • 0023003707 scopus 로고
    • Identification of the binding site for plasma prekallikrein in human high molecular weight kininogen. A region from residues 185 to 224 of the kininogen light chain retains full binding activity
    • Tait JF, Fujikawa K: Identification of the binding site for plasma prekallikrein in human high molecular weight kininogen. A region from residues 185 to 224 of the kininogen light chain retains full binding activity. J Biol Chem 261:15396, 1986
    • (1986) J Biol Chem , vol.261 , pp. 15396
    • Tait, J.F.1    Fujikawa, K.2
  • 76
    • 0023257512 scopus 로고
    • Primary structure requirements for the binding of human high molecular weight kininogen to plasma prekallikrein and factor XI
    • Tait JF, Fujikawa K: Primary structure requirements for the binding of human high molecular weight kininogen to plasma prekallikrein and factor XI. J Biol Chem 262:11651, 1987
    • (1987) J Biol Chem , vol.262 , pp. 11651
    • Tait, J.F.1    Fujikawa, K.2
  • 77
    • 0025345587 scopus 로고
    • Mapping of the prekallikrein binding site of human H-kininogen by ligand screening of lambda gt11 expression libraries: Mimicking of the predicted binding site by anti-idiotypic antibodies
    • Vogel R, Kaufmann J, Chung DW, Kellermann J, Muller-Esterl W: Mapping of the prekallikrein binding site of human H-kininogen by ligand screening of lambda gt11 expression libraries: Mimicking of the predicted binding site by anti-idiotypic antibodies. J Biol Chem 265:12494, 1990
    • (1990) J Biol Chem , vol.265 , pp. 12494
    • Vogel, R.1    Kaufmann, J.2    Chung, D.W.3    Kellermann, J.4    Muller-Esterl, W.5
  • 78
    • 0021090449 scopus 로고
    • Protein-protein interactions in contact activation of blood coagulation. Characterization of fluorescein-labeled human high molecular weight kininogen-light chain as a probe
    • Bock PE, Shore JD: Protein-protein interactions in contact activation of blood coagulation. Characterization of fluorescein-labeled human high molecular weight kininogen-light chain as a probe. J Biol Chem 258:15079, 1983
    • (1983) J Biol Chem , vol.258 , pp. 15079
    • Bock, P.E.1    Shore, J.D.2
  • 79
    • 0022407110 scopus 로고
    • Protein-protein interactions in contact activation of blood coagulation. Binding of high molecular weight kininogen and the 5-(iodoacetamido) fluorescein-labeled kininogen light chain to prekallikrein, kallikrein, and the separated kallikrein heavy and light chains
    • Bock PE, Shore JD, Tans G, Griffin JH: Protein-protein interactions in contact activation of blood coagulation. Binding of high molecular weight kininogen and the 5-(iodoacetamido) fluorescein-labeled kininogen light chain to prekallikrein, kallikrein, and the separated kallikrein heavy and light chains. J Biol Chem 260:12434, 1985
    • (1985) J Biol Chem , vol.260 , pp. 12434
    • Bock, P.E.1    Shore, J.D.2    Tans, G.3    Griffin, J.H.4
  • 80
    • 0025605373 scopus 로고
    • Solution phase conformation studies of the prekallikrein binding domain of high molecular weight kininogen
    • Scarsdale JN, Harris RB: Solution phase conformation studies of the prekallikrein binding domain of high molecular weight kininogen. J Protein Chem 9:647, 1990
    • (1990) J Protein Chem , vol.9 , pp. 647
    • Scarsdale, J.N.1    Harris, R.B.2
  • 81
    • 0025858894 scopus 로고
    • Calorimetric and spectroscopic examination of the solution phase structures of prekallikrein binding domain peptides of high molecular weight kininogen
    • You JL, Scarsdale JN, Harris RB: Calorimetric and spectroscopic examination of the solution phase structures of prekallikrein binding domain peptides of high molecular weight kininogen. J Protein Chem 10:301, 1991
    • (1991) J Protein Chem , vol.10 , pp. 301
    • You, J.L.1    Scarsdale, J.N.2    Harris, R.B.3
  • 82
    • 0027500736 scopus 로고
    • Conformational analysis of synthetic peptides encompassing the factor XI and prekallikrein overlapping binding domains of high molecular weight kininogen
    • You JL, Page JD, Scarsdale JN, Colman RW, Harris RB: Conformational analysis of synthetic peptides encompassing the factor XI and prekallikrein overlapping binding domains of high molecular weight kininogen. Peptides 14:867, 1993
    • (1993) Peptides , vol.14 , pp. 867
    • You, J.L.1    Page, J.D.2    Scarsdale, J.N.3    Colman, R.W.4    Harris, R.B.5
  • 83
    • 0024319089 scopus 로고
    • Monoclonal antibody to human high molecular weight kininogen recognizes its prekallikrein binding site and inhibits coagulant activity
    • Reddigari S, Kaplan AP: Monoclonal antibody to human high molecular weight kininogen recognizes its prekallikrein binding site and inhibits coagulant activity. Blood 74:695, 1989
    • (1989) Blood , vol.74 , pp. 695
    • Reddigari, S.1    Kaplan, A.P.2
  • 84
    • 0027418773 scopus 로고
    • Structural dissection of the multidomain kininogens. Fine mapping of the target epitopes of antibodies interfering with their functional properties
    • Kaufmann J, Haasemann M, Modrow S, Muller-Esterl W: Structural dissection of the multidomain kininogens. Fine mapping of the target epitopes of antibodies interfering with their functional properties. J Biol Chem 268:9079, 1993
    • (1993) J Biol Chem , vol.268 , pp. 9079
    • Kaufmann, J.1    Haasemann, M.2    Modrow, S.3    Muller-Esterl, W.4
  • 85
    • 0029028074 scopus 로고
    • Assembly and activation of the intrinsic fibrinolytic pathway on the surface of human endothelial cells in culture
    • Lenich C, Pannell R, Gurewich V: Assembly and activation of the intrinsic fibrinolytic pathway on the surface of human endothelial cells in culture. Thromb Haemost 74:698, 1995
    • (1995) Thromb Haemost , vol.74 , pp. 698
    • Lenich, C.1    Pannell, R.2    Gurewich, V.3
  • 86
    • 85084725120 scopus 로고    scopus 로고
    • High molecular weight kininogen regulates prekallikrein assembly and activation on endothelial cells: A novel mechanism for contact activation
    • in press
    • Motta G, Rojkjaer R, Hasan AAK, Cines DB, Schmaier AH: High molecular weight kininogen regulates prekallikrein assembly and activation on endothelial cells: A novel mechanism for contact activation. Blood (in press)
    • Blood
    • Motta, G.1    Rojkjaer, R.2    Hasan, A.A.K.3    Cines, D.B.4    Schmaier, A.H.5
  • 88
    • 0023515093 scopus 로고
    • Organization of the gene for human factor XI
    • Asakai R, Davie EW, Chung DW: Organization of the gene for human factor XI. Biochemistry 26:7221, 1987
    • (1987) Biochemistry , vol.26 , pp. 7221
    • Asakai, R.1    Davie, E.W.2    Chung, D.W.3
  • 89
    • 0023043187 scopus 로고
    • Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats
    • Chung DW, Fujikawa K, McMullen BA, DAvie EW: Human plasma prekallikrein, a zymogen to a serine protease that contains four tandem repeats. Biochemistry 25:2410, 1986
    • (1986) Biochemistry , vol.25 , pp. 2410
    • Chung, D.W.1    Fujikawa, K.2    McMullen, B.A.3    DAvie, E.W.4
  • 90
    • 0026082814 scopus 로고
    • Location of the disulfide bonds in human plasma prekallikrein: The presence of four novel apple domains in the amino-terminal portion of the molecule
    • McMullen BA, Fujikawa K, Davie EW: Location of the disulfide bonds in human plasma prekallikrein: The presence of four novel apple domains in the amino-terminal portion of the molecule. Biochemistry 30:2050, 1991
    • (1991) Biochemistry , vol.30 , pp. 2050
    • McMullen, B.A.1    Fujikawa, K.2    Davie, E.W.3
  • 91
    • 0025975587 scopus 로고
    • Location of the disulfide bonds in human coagulation factor XI: The presence of a Tandem apple domain
    • McMullen BA, Fugikawa K, Davie EW: Location of the disulfide bonds in human coagulation factor XI: The presence of a Tandem apple domain. Biochemistry 30:2056, 1991
    • (1991) Biochemistry , vol.30 , pp. 2056
    • McMullen, B.A.1    Fugikawa, K.2    Davie, E.W.3
  • 92
    • 0017738854 scopus 로고
    • Hageman factor substrates. Human plasma prekallikrein: Mechanism of activation by Hageman factor and participation in Hageman factor-dependent fibrinolysis
    • Mandle RJ Jr, Kaplan AP: Hageman factor substrates. Human plasma prekallikrein: Mechanism of activation by Hageman factor and participation in Hageman factor-dependent fibrinolysis. J Biol Chem 252:6097, 1977
    • (1977) J Biol Chem , vol.252 , pp. 6097
    • Mandle Jr., R.J.1    Kaplan, A.P.2
  • 93
    • 0018714471 scopus 로고
    • Human plasma prekallikrein: A rapid high yield method for purification
    • Scott CF, Liu CY, Colman RW: Human plasma prekallikrein: A rapid high yield method for purification. Eur J Biochem 100:77, 1979
    • (1979) Eur J Biochem , vol.100 , pp. 77
    • Scott, C.F.1    Liu, C.Y.2    Colman, R.W.3
  • 94
    • 0020055028 scopus 로고
    • Assay of prekallikrein in human plasma: Comparison of amidolytic, esterolytic, coagulation, and immunochemical assays
    • Fisher CA, Schmaier AH, Addonizio VP, Colman RW: Assay of prekallikrein in human plasma: Comparison of amidolytic, esterolytic, coagulation, and immunochemical assays. Blood 59:963, 1982
    • (1982) Blood , vol.59 , pp. 963
    • Fisher, C.A.1    Schmaier, A.H.2    Addonizio, V.P.3    Colman, R.W.4
  • 95
    • 0014784309 scopus 로고
    • The isolation of human plasma prekallikrein
    • McConnell DJ, Mason B: The isolation of human plasma prekallikrein. Br J Pharmacol 38:490, 1970
    • (1970) Br J Pharmacol , vol.38 , pp. 490
    • McConnell, D.J.1    Mason, B.2
  • 96
    • 0015251714 scopus 로고
    • Plasma prekallikrein: Isolation, characterization, and mechanism of action
    • Wuepper KD, Cochrane CG: Plasma prekallikrein: Isolation, characterization, and mechanism of action. J Exp Med 135:1, 1972
    • (1972) J Exp Med , vol.135 , pp. 1
    • Wuepper, K.D.1    Cochrane, C.G.2
  • 97
    • 0022633449 scopus 로고
    • Human plasma prekallikrein: Immunoaffinity purification and activation to α- And β-kallikrein
    • Burger D, Schleuning W-D, Schapira M: Human plasma prekallikrein: Immunoaffinity purification and activation to α-and β-kallikrein. J Biol Chem 261:324, 1986
    • (1986) J Biol Chem , vol.261 , pp. 324
    • Burger, D.1    Schleuning, W.-D.2    Schapira, M.3
  • 99
    • 0017149563 scopus 로고
    • Identification of prekallikrein and high molecular weight kininogen as a complex in human plasma
    • Mandle R Jr, Colman RW, Kaplan AP: Identification of prekallikrein and high molecular weight kininogen as a complex in human plasma. Proc Natl Acad Sci USA 73:4179, 1976
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 4179
    • Mandle Jr., R.1    Colman, R.W.2    Kaplan, A.P.3
  • 100
    • 0025824239 scopus 로고
    • Localization of distinct functional domains on prekallikrein for interaction with both high molecular weight kininogen and activated factor XII in a 28-kDa fragment (amino acids 141-371)
    • Page JD, Colman RW: Localization of distinct functional domains on prekallikrein for interaction with both high molecular weight kininogen and activated factor XII in a 28-kDa fragment (amino acids 141-371). J Biol Chem 266:8143, 1991
    • (1991) J Biol Chem , vol.266 , pp. 8143
    • Page, J.D.1    Colman, R.W.2
  • 101
    • 0028127236 scopus 로고
    • Localization of the binding site on plasma kallikrein for high molecular weight kininogen to both apple 1 and apple 4 domains of the heavy chain
    • Page JD, You JL, Harris RB, Colman RW: Localization of the binding site on plasma kallikrein for high molecular weight kininogen to both apple 1 and apple 4 domains of the heavy chain. Arch Biochem Biophys 314:159, 1994
    • (1994) Arch Biochem Biophys , vol.314 , pp. 159
    • Page, J.D.1    You, J.L.2    Harris, R.B.3    Colman, R.W.4
  • 102
    • 0025368839 scopus 로고
    • High molecular weight kininogen-binding site of prekallikrein probed by monoclonal antibodies
    • Hock J, Vogel R, Linke RP, Muller-Esterl W: High molecular weight kininogen-binding site of prekallikrein probed by monoclonal antibodies. J Biol Chem. 265:12005, 1990
    • (1990) J Biol Chem. , vol.265 , pp. 12005
    • Hock, J.1    Vogel, R.2    Linke, R.P.3    Muller-Esterl, W.4
  • 103
    • 0029815025 scopus 로고    scopus 로고
    • Direct evidence for multi-facial contacts between high molecular weight kininogen and plasma prekallikrein
    • Lin Y, Shenoy S, Harris RB, Colman RW: Direct evidence for multi-facial contacts between high molecular weight kininogen and plasma prekallikrein. Biochemistry 35:12945, 1996
    • (1996) Biochemistry , vol.35 , pp. 12945
    • Lin, Y.1    Shenoy, S.2    Harris, R.B.3    Colman, R.W.4
  • 105
    • 0014750141 scopus 로고
    • Interaction of plasma kallikrein with the C1 inhibitor
    • Gigli I, Mason JW, Colman RW, Austen KF: Interaction of plasma kallikrein with the C1 inhibitor. J Immunol 104:574, 1970
    • (1970) J Immunol , vol.104 , pp. 574
    • Gigli, I.1    Mason, J.W.2    Colman, R.W.3    Austen, K.F.4
  • 107
    • 0020059596 scopus 로고
    • Contribution of plasma protease inhibitors to the inactivation of kallikrein in plasma
    • Schapira M, Scott CF, Colman RW: Contribution of plasma protease inhibitors to the inactivation of kallikrein in plasma. J Clin Invest 69:462, 1982
    • (1982) J Clin Invest , vol.69 , pp. 462
    • Schapira, M.1    Scott, C.F.2    Colman, R.W.3
  • 108
    • 0020629994 scopus 로고
    • Interaction of human plasma, kallikrein and its light chain with C1 inhibitor
    • Van der Graff F, Koedam JA, Griffin JH, Bouma BN: Interaction of human plasma, kallikrein and its light chain with C1 inhibitor. Biochemistry 22:4860, 1983
    • (1983) Biochemistry , vol.22 , pp. 4860
    • Van Der Graff, F.1    Koedam, J.A.2    Griffin, J.H.3    Bouma, B.N.4
  • 109
    • 0020082693 scopus 로고
    • High molecular weight kininogen or its light chain protects human plasma kallikrein from inactivation by plasma protease inhibitors
    • Schapira M, Scott CF, James A, Silver LD, Kueppers F, James HL, Colman RW: High molecular weight kininogen or its light chain protects human plasma kallikrein from inactivation by plasma protease inhibitors. Biochemistry 21:567, 1982
    • (1982) Biochemistry , vol.21 , pp. 567
    • 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
  • 110
    • 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 CF, Colman RW: Protection of human plasma kallikrein from inactivation by C1 inhibitor and other protease inhibitors. The role of high molecular weight kininogen. Biochemistry 20:2738, 1981
    • (1981) Biochemistry , vol.20 , pp. 2738
    • Schapira, M.1    Scott, C.F.2    Colman, R.W.3
  • 111
    • 0021671839 scopus 로고
    • Plasma prekallikrein assay: Reversible inhibition of C1 inhibitor by chloroform and its use in measuring prekallikrein in different mammalian species
    • Schmaier AH, Gustafson EG, Idell S, Colman RW: Plasma prekallikrein assay: Reversible inhibition of C1 inhibitor by chloroform and its use in measuring prekallikrein in different mammalian species. J Lab Clin Med 104:882, 1984
    • (1984) J Lab Clin Med , vol.104 , pp. 882
    • Schmaier, A.H.1    Gustafson, E.G.2    Idell, S.3    Colman, R.W.4
  • 114
    • 0026026441 scopus 로고
    • Interaction of plasma kallikrein with protein C inhibitor in purified mixtures and in plasma
    • Espana F, Estelles A, Griffin JH, Aznar J: Interaction of plasma kallikrein with protein C inhibitor in purified mixtures and in plasma. Thromb Haemost 65:46, 1991
    • (1991) Thromb Haemost , vol.65 , pp. 46
    • Espana, F.1    Estelles, A.2    Griffin, J.H.3    Aznar, J.4
  • 115
    • 0024508761 scopus 로고
    • Plasminogen activators in dextran sulfate-activated euglobulin functions: A molecular analysis of factor XII and prekallikrein-dependent fibrinolysis
    • Hauert J, Nicoloso G, Schleuning WD, Bachmann F, Schapira M: Plasminogen activators in dextran sulfate-activated euglobulin functions: A molecular analysis of factor XII and prekallikrein-dependent fibrinolysis. Blood 73:994, 1989
    • (1989) Blood , vol.73 , pp. 994
    • Hauert, J.1    Nicoloso, G.2    Schleuning, W.D.3    Bachmann, F.4    Schapira, M.5
  • 116
    • 0023022473 scopus 로고
    • The activation of prourokinase by plasma kallikrein and its inactivation by thrombin
    • Ichinose A, Fujikawa K, Suyama T: The activation of prourokinase by plasma kallikrein and its inactivation by thrombin. J Biol Chem 261:3486, 1986
    • (1986) J Biol Chem , vol.261 , pp. 3486
    • Ichinose, A.1    Fujikawa, K.2    Suyama, T.3
  • 117
    • 0024215593 scopus 로고
    • Assignment of human coagulation factor XII (fXII) to chromosome 5 by cDNA hybridization to DNA from somatic cell hybrids
    • Citarella F, Tripodi M, Fantoni A, Bernardi F, Romeo G, Rocchi M: Assignment of human coagulation factor XII (fXII) to chromosome 5 by cDNA hybridization to DNA from somatic cell hybrids. Hum Genet 80:397, 1988
    • (1988) Hum Genet , vol.80 , pp. 397
    • Citarella, F.1    Tripodi, M.2    Fantoni, A.3    Bernardi, F.4    Romeo, G.5    Rocchi, M.6
  • 119
    • 0023265140 scopus 로고
    • Characterization of the human blood coagulation factor XII gene
    • Cool DE, MacGillivray RTA: Characterization of the human blood coagulation factor XII gene. J Biol Chem 262:13662, 1987
    • (1987) J Biol Chem , vol.262 , pp. 13662
    • Cool, D.E.1    MacGillivray, R.T.A.2
  • 121
    • 0022481605 scopus 로고
    • Characterization of a cDNa coding for human factor XII (Hageman factor)
    • Que BG, Davie EW: Characterization of a cDNA coding for human factor XII (Hageman factor). Biochemistry 25:1525, 1986
    • (1986) Biochemistry , vol.25 , pp. 1525
    • Que, B.G.1    Davie, E.W.2
  • 123
    • 0016283761 scopus 로고
    • Structural changes accompanying enzymatic activation of Hageman factor
    • Revak SD, Cochrane CC, Johnston A, Hugli T: Structural changes accompanying enzymatic activation of Hageman factor. J Clin Invest 54:619, 1974
    • (1974) J Clin Invest , vol.54 , pp. 619
    • Revak, S.D.1    Cochrane, C.C.2    Johnston, A.3    Hugli, T.4
  • 124
    • 0017163250 scopus 로고
    • Radioimmunoassay of human Hageman factor (factor XII)
    • Saito H, Ratnoff OD, Pensky J: Radioimmunoassay of human Hageman factor (factor XII). J Lab Clin Med 88:506, 1976
    • (1976) J Lab Clin Med , vol.88 , pp. 506
    • Saito, H.1    Ratnoff, O.D.2    Pensky, J.3
  • 126
    • 0023848328 scopus 로고
    • Dose-dependent effects of postmenopausal estrogen and progestin on antithrombin III and factor XII
    • Gordon EM, Williams SR, Frenchek B, Mazur CA, Speroff L: Dose-dependent effects of postmenopausal estrogen and progestin on antithrombin III and factor XII. J Lab Clin Med 111:52, 1988
    • (1988) J Lab Clin Med , vol.111 , pp. 52
    • Gordon, E.M.1    Williams, S.R.2    Frenchek, B.3    Mazur, C.A.4    Speroff, L.5
  • 127
    • 0025357677 scopus 로고
    • The increased rate of activation of factor XII in late pregnancy can contribute to the increased reactivity of factor VII
    • Mitropoulos KA, Martin JC, Burgess Al, Esnouf MP, Stirling Y, Howorth DJ, Reeves BE: The increased rate of activation of factor XII in late pregnancy can contribute to the increased reactivity of factor VII. Thromb Haemost 63:349, 1990
    • (1990) Thromb Haemost , vol.63 , pp. 349
    • Mitropoulos, K.A.1    Martin, J.C.2    Al, B.3    Esnouf, M.P.4    Stirling, Y.5    Howorth, D.J.6    Reeves, B.E.7
  • 128
    • 0025896345 scopus 로고
    • Enhanced expression of factor XII (Hageman factor) in isolated livers of estrogen-and prolactin-treated rats
    • Gordon EM, Johnson TR, Ramos LP, Schmeidler-Sapiro KT: Enhanced expression of factor XII (Hageman factor) in isolated livers of estrogen-and prolactin-treated rats. J Lab Clin Med 117:353, 1991
    • (1991) J Lab Clin Med , vol.117 , pp. 353
    • Gordon, E.M.1    Johnson, T.R.2    Ramos, L.P.3    Schmeidler-Sapiro, K.T.4
  • 132
    • 0023258668 scopus 로고
    • A monoclonal antibody recognizing an icosapeptide sequence in the heavy chain of human factor XII inhibits surface-catalyzed activation
    • Pixley RA, Stumpo LG, Birkmeyer K, Silver L, Colman RW: A monoclonal antibody recognizing an icosapeptide sequence in the heavy chain of human factor XII inhibits surface-catalyzed activation. J Biol Chem 262:10140, 1987
    • (1987) J Biol Chem , vol.262 , pp. 10140
    • Pixley, R.A.1    Stumpo, L.G.2    Birkmeyer, K.3    Silver, L.4    Colman, R.W.5
  • 134
    • 0029967088 scopus 로고    scopus 로고
    • Structure/function analysis of human factor XII using recombinant deletion mutants. Evidence for an additional region involved in the binding to negatively charged surfaces
    • Citrella F, Ravon DM, Pascucci B, Felici A, Fantoni A, Hack CE: Structure/function analysis of human factor XII using recombinant deletion mutants. Evidence for an additional region involved in the binding to negatively charged surfaces, Eur J Biochem 238:240, 1996
    • (1996) Eur J Biochem , vol.238 , pp. 240
    • Citrella, F.1    Ravon, D.M.2    Pascucci, B.3    Felici, A.4    Fantoni, A.5    Hack, C.E.6
  • 135
    • 0015754565 scopus 로고
    • Activation of Hageman factor in solid and fluid phases. a critical role of kallikrein
    • Cochrane CG, Revak SD, Wuepper KD: Activation of Hageman factor in solid and fluid phases. A critical role of kallikrein. J Exp Med 138:1564, 1973
    • (1973) J Exp Med , vol.138 , pp. 1564
    • Cochrane, C.G.1    Revak, S.D.2    Wuepper, K.D.3
  • 136
    • 0026701990 scopus 로고
    • Human factor XII (Hageman factor) autoactivation by dextran sulfate: Circular dichroism, fluorescence, and ultraviolet difference spectroscopic studies
    • Samuel M, Pixley RA, Villanueva MA, Colman RW, Villanueva GB: Human factor XII (Hageman factor) autoactivation by dextran sulfate: Circular dichroism, fluorescence, and ultraviolet difference spectroscopic studies. J Biol Chem 267:19691, 1992
    • (1992) J Biol Chem , vol.267 , pp. 19691
    • Samuel, M.1    Pixley, R.A.2    Villanueva, M.A.3    Colman, R.W.4    Villanueva, G.B.5
  • 137
    • 0021843169 scopus 로고
    • Effect of heparin on the inactivation rate of human activated factor XII by antithrombin III
    • Pixley RA, Schapira M, Colman RW: Effect of heparin on the inactivation rate of human activated factor XII by antithrombin III. Blood 66:198, 1985
    • (1985) Blood , vol.66 , pp. 198
    • Pixley, R.A.1    Schapira, M.2    Colman, R.W.3
  • 139
    • 0026046175 scopus 로고
    • Functional characterization of an abnormal factor XII molecule (F XII Bern)
    • Wuillemin WA, Huber I, Furlan M, Lammle B: Functional characterization of an abnormal factor XII molecule (F XII Bern). Blood 78:997, 1991
    • (1991) Blood , vol.78 , pp. 997
    • Wuillemin, W.A.1    Huber, I.2    Furlan, M.3    Lammle, B.4
  • 140
    • 0015754565 scopus 로고
    • Activation of Hageman factor in solid and fluid phases: A critical role of kallikrein
    • Cochrane CG, Revak SD, Wuepper KD: Activation of Hageman factor in solid and fluid phases: A critical role of kallikrein. J Exp Med 138:1564, 1973
    • (1973) J Exp Med , vol.138 , pp. 1564
    • Cochrane, C.G.1    Revak, S.D.2    Wuepper, K.D.3
  • 141
    • 0017690677 scopus 로고
    • The binding and cleavage characteristics of huma Hageman factor during contact activation: A comparison of normal plasma with plasma deficient in factor XI, prekallikrein or high molecular weight kininogen
    • Revak SD, Cochrane CG, Griffin JH: The binding and cleavage characteristics of huma Hageman factor during contact activation: a comparison of normal plasma with plasma deficient in factor XI, prekallikrein or high molecular weight kininogen. J Clin Invest 59:1167, 1977
    • (1977) J Clin Invest , vol.59 , pp. 1167
    • Revak, S.D.1    Cochrane, C.G.2    Griffin, J.H.3
  • 142
    • 0001525663 scopus 로고
    • The role of surface in the surface-dependent activation of Hageman factor (blood coagulation factor XII)
    • Griffin JH: The role of surface in the surface-dependent activation of Hageman factor (blood coagulation factor XII). Proc Natl Acad Sci USA 75:1998, 1978
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 1998
    • Griffin, J.H.1
  • 143
    • 0020586697 scopus 로고
    • The binding of bovine factor XII to kaolin
    • Kirby E, McDevitt PJ: The binding of bovine factor XII to kaolin. Blood 61:652, 1983
    • (1983) Blood , vol.61 , pp. 652
    • Kirby, E.1    McDevitt, P.J.2
  • 144
    • 0018632212 scopus 로고
    • The autoactivation of rabbit Hageman factor
    • Wiggins RC, Cochrane CG: The autoactivation of rabbit Hageman factor. J Exp Med 150:1122, 1979
    • (1979) J Exp Med , vol.150 , pp. 1122
    • Wiggins, R.C.1    Cochrane, C.G.2
  • 146
    • 0019197848 scopus 로고
    • Autoactivation of human Hageman factor: Demonstration utilizing a synthetic substrate
    • Silverberg M, Dunn JT, Garen L, Kaplan AP: Autoactivation of human Hageman factor: Demonstration utilizing a synthetic substrate. J Biol Chem 255:7281, 1980
    • (1980) J Biol Chem , vol.255 , pp. 7281
    • Silverberg, M.1    Dunn, J.T.2    Garen, L.3    Kaplan, A.P.4
  • 147
    • 0020076571 scopus 로고
    • The cleavage and formation of activated human Hageman factor by autodigestion and by kallikrein
    • Dunn JT, Silverberg M, Kaplan AP: The cleavage and formation of activated human Hageman factor by autodigestion and by kallikrein. J Biol Chem 257:1779, 1982
    • (1982) J Biol Chem , vol.257 , pp. 1779
    • Dunn, J.T.1    Silverberg, M.2    Kaplan, A.P.3
  • 148
    • 0020597530 scopus 로고
    • Activation of Hageman factor (factor XII) by sulfatides and other agents in the absence of plasma proteases
    • Espana F, Ratnoff OD: Activation of Hageman factor (factor XII) by sulfatides and other agents in the absence of plasma proteases. J Lab Clin Med 102:31, 1983
    • (1983) J Lab Clin Med , vol.102 , pp. 31
    • Espana, F.1    Ratnoff, O.D.2
  • 149
    • 0021352747 scopus 로고
    • Kinetics of activation and autoactivation of human factor XII
    • Tankersley DL, Finlayson JS: Kinetics of activation and autoactivation of human factor XII. Biochemistry 23:273, 1984
    • (1984) Biochemistry , vol.23 , pp. 273
    • Tankersley, D.L.1    Finlayson, J.S.2
  • 150
    • 0027496212 scopus 로고
    • Contact activation in human plasma is triggered by zinc ion modulation of factor XII (Hageman factor)
    • Schousboe I: Contact activation in human plasma is triggered by zinc ion modulation of factor XII (Hageman factor). Blood Coagul Fibrinolysis 4:671, 1993
    • (1993) Blood Coagul Fibrinolysis , vol.4 , pp. 671
    • Schousboe, I.1
  • 151
    • 0027233729 scopus 로고
    • Surface-independent acceleration of factor XII activation by zinc ions. I. Kinetic characterization of the metal ion rate enhancement
    • Bernardo MM, Day DE, Olson ST, Shore JD: Surface-independent acceleration of factor XII activation by zinc ions. I. Kinetic characterization of the metal ion rate enhancement. J Biol Chem 268:12468, 1993
    • (1993) J Biol Chem , vol.268 , pp. 12468
    • Bernardo, M.M.1    Day, D.E.2    Olson, S.T.3    Shore, J.D.4
  • 152
    • 0027281416 scopus 로고
    • Surface-independent acceleration of factor XII activation by zinc ions. II. Direct binding and fluorescence studies
    • Bernardo MM, Day DE, Halvorson HR, Olson ST, Shore JD: Surface-independent acceleration of factor XII activation by zinc ions. II. Direct binding and fluorescence studies. J Biol Chem 268:12477, 1993
    • (1993) J Biol Chem , vol.268 , pp. 12477
    • Bernardo, M.M.1    Day, D.E.2    Halvorson, H.R.3    Olson, S.T.4    Shore, J.D.5
  • 153
    • 0030788208 scopus 로고    scopus 로고
    • 2+ binding sites in factor XII and its activation derivatives
    • 2+ binding sites in factor XII and its activation derivatives. Eur J Biochem 247:491, 1997
    • (1997) Eur J Biochem , vol.247 , pp. 491
    • Rojkjaer, R.1    Schousboe, I.2
  • 154
    • 0018913292 scopus 로고
    • Activation of rabbit Hageman factor by homogenates of cultured rabbit endothelial cells
    • Wiggins RC, Loskutoff DJ, Cochrane CG, Griffin JH: Activation of rabbit Hageman factor by homogenates of cultured rabbit endothelial cells. J Clin Invest 65:197, 1980
    • (1980) J Clin Invest , vol.65 , pp. 197
    • Wiggins, R.C.1    Loskutoff, D.J.2    Cochrane, C.G.3    Griffin, J.H.4
  • 155
    • 0015935999 scopus 로고
    • Isolation of the high molecular weight activators of prekallikrein
    • Bagdasarian A, Talamo RC, Colman RW: Isolation of the high molecular weight activators of prekallikrein. J Biol Chem 248:7742, 1973
    • (1973) J Biol Chem , vol.248 , pp. 7742
    • Bagdasarian, A.1    Talamo, R.C.2    Colman, R.W.3
  • 156
    • 0014868785 scopus 로고
    • A prealbumin activator of prekallikrein
    • Kaplan AP, Austen FK: A prealbumin activator of prekallikrein. J Immunol 105:802, 1970
    • (1970) J Immunol , vol.105 , pp. 802
    • Kaplan, A.P.1    Austen, F.K.2
  • 158
    • 0018733141 scopus 로고
    • Molecular assembly in the contact phase of the Hageman factor system
    • Cochrane CG, Griffin JH: Molecular assembly in the contact phase of the Hageman factor system. Am J Med 67:657, 1979
    • (1979) Am J Med , vol.67 , pp. 657
    • Cochrane, C.G.1    Griffin, J.H.2
  • 159
    • 0015044927 scopus 로고
    • A prealbumin activator of prekallikrein. II. Derivation of activators of prekallikrein from active Hageman factor by digestion with plasmin
    • Kaplan AP, Austen FK: A prealbumin activator of prekallikrein. II. Derivation of activators of prekallikrein from active Hageman factor by digestion with plasmin. J Exp Med 133:696, 1971
    • (1971) J Exp Med , vol.133 , pp. 696
    • Kaplan, A.P.1    Austen, F.K.2
  • 160
    • 0017806879 scopus 로고
    • Surface and fluid phase activities of two forms of activated Hageman factor produced during contact activation of plasma
    • Revak SD, Cochrane CG, Bouma BN, Griffin JH: Surface and fluid phase activities of two forms of activated Hageman factor produced during contact activation of plasma. J Exp Med 147:719, 1978
    • (1978) J Exp Med , vol.147 , pp. 719
    • Revak, S.D.1    Cochrane, C.G.2    Bouma, B.N.3    Griffin, J.H.4
  • 161
    • 0017255109 scopus 로고
    • The relationship of structure and function in human Hageman factor. the association of enzymatic binding activities with separate regions of the molecule
    • Revak SD, Cochrane CG: The relationship of structure and function in human Hageman factor. The association of enzymatic binding activities with separate regions of the molecule. J Clin Invest 57:852, 1976
    • (1976) J Clin Invest , vol.57 , pp. 852
    • Revak, S.D.1    Cochrane, C.G.2
  • 162
    • 0014883077 scopus 로고
    • Inhibition of activated Hageman factor and activated plasma thromboplastin antecedent by purified C1-inactivator
    • Forbes CO, Pensky J, Ratnoff OD: Inhibition of activated Hageman factor and activated plasma thromboplastin antecedent by purified C1-inactivator. J Lab Clin Med 76:809, 1970
    • (1970) J Lab Clin Med , vol.76 , pp. 809
    • Forbes, C.O.1    Pensky, J.2    Ratnoff, O.D.3
  • 163
    • 0015634027 scopus 로고
    • Inhibition by C1-INH of Hageman factor fragment activation of coagulation, fibrinolysis and kinin-generation
    • Schreiber AD, Kaplan AD, Austen FK: Inhibition by C1-INH of Hageman factor fragment activation of coagulation, fibrinolysis and kinin-generation. J Clin Invest 52:1402, 1973
    • (1973) J Clin Invest , vol.52 , pp. 1402
    • Schreiber, A.D.1    Kaplan, A.D.2    Austen, F.K.3
  • 164
    • 0021241859 scopus 로고
    • Inactivation of factor XII active fragment in normal plasma: Predominant role of C1-inhibitor
    • de Agostini A, Lijnen HR, Pixley RA, Colman RW, Schapira M: Inactivation of factor XII active fragment in normal plasma: Predominant role of C1-inhibitor. J Clin Invest 73:1542, 1984
    • (1984) J Clin Invest , vol.73 , pp. 1542
    • De Agostini, A.1    Lijnen, H.R.2    Pixley, R.A.3    Colman, R.W.4    Schapira, M.5
  • 165
    • 0021943946 scopus 로고
    • The regulation of human factor XIIa by plasma proteinase inhibitors
    • Pixley RA, Schapira M, Colman RW: The regulation of human factor XIIa by plasma proteinase inhibitors. J Biol Chem 260:1723, 1985
    • (1985) J Biol Chem , vol.260 , pp. 1723
    • Pixley, R.A.1    Schapira, M.2    Colman, R.W.3
  • 166
    • 0023212415 scopus 로고
    • Effect of negatively charged activating compounds on inactivation of factor XIIa by C1 inhibitor
    • Pixley RA, Schmaier AH, Colman RW: Effect of negatively charged activating compounds on inactivation of factor XIIa by C1 inhibitor. Arch Biochem Biophys 256:490, 1987
    • (1987) Arch Biochem Biophys , vol.256 , pp. 490
    • Pixley, R.A.1    Schmaier, A.H.2    Colman, R.W.3
  • 167
    • 0017167631 scopus 로고
    • The inhibition of human activated Hageman factor (HF) by human antithrombin-heparin cofactor (AT)
    • Stead NW, Kaplan AP, Rosenberg RD: The inhibition of human activated Hageman factor (HF) by human antithrombin-heparin cofactor (AT). J Biol Chem 251:6481, 1976
    • (1976) J Biol Chem , vol.251 , pp. 6481
    • Stead, N.W.1    Kaplan, A.P.2    Rosenberg, R.D.3
  • 168
    • 0021843169 scopus 로고
    • Effect of heparin on the inactivation rate of human activated factor XII by antithrombin III
    • Pixley RA, Colman RW: Effect of heparin on the inactivation rate of human activated factor XII by antithrombin III. Blood 66:198, 1985
    • (1985) Blood , vol.66 , pp. 198
    • Pixley, R.A.1    Colman, R.W.2
  • 169
    • 0024327242 scopus 로고
    • Interaction of type 1 plasminogen activator inhibitor with the enzymes of the contact activation system
    • Berrettini M, Schleef RR, Espana F, Loskutoff DJ, Griffin JH: Interaction of type 1 plasminogen activator inhibitor with the enzymes of the contact activation system. J Biol Chem 264:11738, 1989
    • (1989) J Biol Chem , vol.264 , pp. 11738
    • Berrettini, M.1    Schleef, R.R.2    Espana, F.3    Loskutoff, D.J.4    Griffin, J.H.5
  • 170
    • 0027459092 scopus 로고
    • Endothelial cells produce a substance that inhibits contact activation of coagulation by blocking the activation of Hageman factor
    • Kleniewski J, Donaldson VH: Endothelial cells produce a substance that inhibits contact activation of coagulation by blocking the activation of Hageman factor. Proc Natl Acad Sci USA 90:198, 1993
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 198
    • Kleniewski, J.1    Donaldson, V.H.2
  • 171
    • 0021739735 scopus 로고
    • Receptors for high molecular weight kininogen on stimulated washed human platelets
    • Greengard JS, Griffin JH: Receptors for high molecular weight kininogen on stimulated washed human platelets. Biochemistry 23:6863, 1984
    • (1984) Biochemistry , vol.23 , pp. 6863
    • Greengard, J.S.1    Griffin, J.H.2
  • 172
    • 0023895740 scopus 로고
    • High-molecular weight kininogen is present in cultured human endothelial cells: Localization, isolation, and characterization
    • van Iwaarden F, de Groot PG, Sixma JJ, Berrettini M, Bouma BN: High-molecular weight kininogen is present in cultured human endothelial cells: Localization, isolation, and characterization. Blood 71:1268, 1988
    • (1988) Blood , vol.71 , pp. 1268
    • Van Iwaarden, F.1    De Groot, P.G.2    Sixma, J.J.3    Berrettini, M.4    Bouma, B.N.5
  • 173
    • 0021328610 scopus 로고
    • Radioimmunoassays of human high and low molecular weight kininogens in plasmas and platelets
    • Kerbiriou-Nabias DM, Garcia FO, Larrieu MJ: Radioimmunoassays of human high and low molecular weight kininogens in plasmas and platelets. Br J Haematol 56:273, 1984
    • (1984) Br J Haematol , vol.56 , pp. 273
    • Kerbiriou-Nabias, D.M.1    Garcia, F.O.2    Larrieu, M.J.3
  • 176
    • 0026699897 scopus 로고
    • Assembly and expression of an intrinsic factor IX activator complex on the surface of cultured human endothelial cells
    • Berrettini M, Schleef RR, Heeb MJ, Hopmeier P, Griffin JH: Assembly and expression of an intrinsic factor IX activator complex on the surface of cultured human endothelial cells. J Biol Chem 267:19833, 1992
    • (1992) J Biol Chem , vol.267 , pp. 19833
    • Berrettini, M.1    Schleef, R.R.2    Heeb, M.J.3    Hopmeier, P.4    Griffin, J.H.5
  • 177
    • 0019407381 scopus 로고
    • On the attribution and additivity of binding energies
    • Jencks WP: On the attribution and additivity of binding energies. Proc Natl Acad Sci USA 78:4046, 1981
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 4046
    • Jencks, W.P.1
  • 178
    • 0024579549 scopus 로고
    • Conformation of high molecular weight kininogen: Effects of kallikrein and factor XIa cleavage
    • Villanueva GB, Leung L, Bradford H, Colman RW: Conformation of high molecular weight kininogen: Effects of kallikrein and factor XIa cleavage. Biochem Biophys Res Commun 158:72, 1989
    • (1989) Biochem Biophys Res Commun , vol.158 , pp. 72
    • Villanueva, G.B.1    Leung, L.2    Bradford, H.3    Colman, R.W.4
  • 179
    • 0001637870 scopus 로고
    • Permanent cell lines expressing human factor VHI-related antigen established by hybridization
    • Edgell CJS, McDonald CC, Graham JB: Permanent cell lines expressing human factor VHI-related antigen established by hybridization. Proc Natl Acad Sci USA 80:3734, 1983
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 3734
    • Edgell, C.J.S.1    McDonald, C.C.2    Graham, J.B.3
  • 180
    • 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, Mueller-Esterl W: Isolation and characterization of the kininogen-binding protein p33 from endothelial cells: Identity with the gC1q receptor. J Biol Chem 271:13040, 1996
    • (1996) J Biol Chem , vol.271 , pp. 13040
    • Herwald, H.1    Dedio, J.2    Kellner, R.3    Loos, M.4    Mueller-Esterl, W.5
  • 181
    • 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 BL, Peerschke EI, Willis AC, Reid KB: Isolation, cDNA cloning, and overexpression of a 33-kD cell surface glycoprotein that binds to the globular "heads" of C1q. J Exp Med 179:1809, 1994
    • (1994) J Exp Med , vol.179 , pp. 1809
    • Ghebrehiwet, B.1    Lim, B.L.2    Peerschke, E.I.3    Willis, A.C.4    Reid, K.B.5
  • 182
    • 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 (gC1qR)
    • Joseph K, Ghebrehiwet B, Peerschke EIB, Reid KBM, Kaplan AP: 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 (gC1qR). Proc Natl Acad Sci USA 93:8552, 1996
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8552
    • Joseph, K.1    Ghebrehiwet, B.2    Peerschke, E.I.B.3    Reid, K.B.M.4    Kaplan, A.P.5
  • 183
    • 0030590847 scopus 로고    scopus 로고
    • Kininogen binding protein p33/ gC1qR is localized in the vesicular fraction of endothelial cells
    • Dedio J, Mueller-Esterl W. Kininogen binding protein p33/ gC1qR is localized in the vesicular fraction of endothelial cells. FEBS Lett 399:255, 1996
    • (1996) FEBS Lett , vol.399 , pp. 255
    • Dedio, J.1    Mueller-Esterl, W.2
  • 184
    • 0027212538 scopus 로고
    • Human Hageman factor (factor XII) and high molecular weight kininogen compete for the same binding site on human umbilical vein endothelial cells
    • Reddigari SR, Shibayama Y, Brunnee T, Kaplan AP: Human Hageman factor (factor XII) and high molecular weight kininogen compete for the same binding site on human umbilical vein endothelial cells. J Biol Chem 268:11982, 1993
    • (1993) J Biol Chem , vol.268 , pp. 11982
    • Reddigari, S.R.1    Shibayama, Y.2    Brunnee, T.3    Kaplan, A.P.4
  • 185
    • 1842315966 scopus 로고    scopus 로고
    • High molecular weight kininogen binds to the vitronectin binding domain(s) on the endothelial cell receptor
    • abstr
    • Colman RW, Pixley RA, Najamunnisa S, Yan W-Y, Wang J, Mazar A, McCrae KR: High molecular weight kininogen binds to the vitronectin binding domain(s) on the endothelial cell receptor. Circulation 94:I-42, 1996 (abstr)
    • (1996) Circulation , vol.94
    • Colman, R.W.1    Pixley, R.A.2    Najamunnisa, S.3    Yan, W.-Y.4    Wang, J.5    Mazar, A.6    McCrae, K.R.7
  • 187
    • 24844463623 scopus 로고    scopus 로고
    • The integrin, CD11b/CD18 (Mac-1) is a major cell receptor for high molecular weight kininogen (HK)
    • abstr
    • 186a. Sheng N, Fairbanks M, Henrikson R, Canziani G, Chaiken I, Moser D, Colman RW: The integrin, CD11b/CD18 (Mac-1) is a major cell receptor for high molecular weight kininogen (HK). FASEB J 11:19920, 1997 (abstr)
    • (1997) FASEB J , vol.11 , pp. 19920
    • Sheng, N.1    Fairbanks, M.2    Henrikson, R.3    Canziani, G.4    Chaiken, I.5    Moser, D.6    Colman, R.W.7
  • 188
    • 1842284379 scopus 로고    scopus 로고
    • Cytokeratin 1 is the major cell receptor for kininogens
    • abstr
    • Hasan AAK, Zisman T, Schmaier AH: Cytokeratin 1 is the major cell receptor for kininogens. Thromb Haemost 77:141, 1997 (abstr, suppl 1)
    • (1997) Thromb Haemost , vol.77 , Issue.1 SUPPL. , pp. 141
    • Hasan, A.A.K.1    Zisman, T.2    Schmaier, A.H.3
  • 189
    • 0028901093 scopus 로고
    • A cytokeratin 8-like protein with plasminogen-binding activity is present on the external surface of hepatocytes, HepG2 cells, and breast carcinoma cell line
    • Hembrough TA, Vasudevan J, Allietta MM, Glass WF II, Gonias SL: A cytokeratin 8-like protein with plasminogen-binding activity is present on the external surface of hepatocytes, HepG2 cells, and breast carcinoma cell line. J Cell Sci 108:1071, 1995
    • (1995) J Cell Sci , vol.108 , pp. 1071
    • Hembrough, T.A.1    Vasudevan, J.2    Allietta, M.M.3    Glass II, W.F.4    Gonias, S.L.5
  • 190
    • 0029795405 scopus 로고    scopus 로고
    • Cell-surface cytokeratin 8 is the major plasminogen receptor on breast cancer cells and is required for the accelerated activation of cell-associated plasminogen by tissue-type plasminogen activator
    • Hembrough TA, Li L, Gonias SL: Cell-surface cytokeratin 8 is the major plasminogen receptor on breast cancer cells and is required for the accelerated activation of cell-associated plasminogen by tissue-type plasminogen activator. J Biol Chem 271:25684, 1996
    • (1996) J Biol Chem , vol.271 , pp. 25684
    • Hembrough, T.A.1    Li, L.2    Gonias, S.L.3
  • 191
    • 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 AP, Reddigari SR: Generation of vasoactive peptide bradykinin from human umbilical vein endothelium-bound high molecular weight kininogen by plasma kallikrein. Blood 80:1980, 1992
    • (1992) Blood , vol.80 , pp. 1980
    • Nishikawa, K.1    Shibayama, Y.2    Kuna, P.3    Calcaterra, E.4    Kaplan, A.P.5    Reddigari, S.R.6
  • 192
    • 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 FS, Koshy A, Knight LC, Walsh PN: Blood coagulation factor XIa binds specifically to a site on activated human platelets distinct from that for factor XI. J Clin Invest 73:1550, 1984
    • (1984) J Clin Invest , vol.73 , pp. 1550
    • Sinha, D.1    Seaman, F.S.2    Koshy, A.3    Knight, L.C.4    Walsh, P.N.5
  • 193
    • 0022461227 scopus 로고
    • Functional characterization of platelet-bound factor XIa: Retention of factor XIa activity on the platelet surface
    • Walsh PN, Sinha D, Koshy A, Seaman FS, Bradford H: Functional characterization of platelet-bound factor XIa: Retention of factor XIa activity on the platelet surface. Blood 68:225, 1986
    • (1986) Blood , vol.68 , pp. 225
    • Walsh, P.N.1    Sinha, D.2    Koshy, A.3    Seaman, F.S.4    Bradford, H.5
  • 194
    • 0028211344 scopus 로고
    • Plateletbound prekallikrein promotes pro-urokinase-induced clot lysis: A mechanism for targeting the factor XII dependent intrinsic pathway of fibrinolysis
    • Loza JP, Gurewich V, Johnstone M, Pannell R: Plateletbound prekallikrein promotes pro-urokinase-induced clot lysis: A mechanism for targeting the factor XII dependent intrinsic pathway of fibrinolysis. Thromb Haemost 71:347, 1994
    • (1994) Thromb Haemost , vol.71 , pp. 347
    • Loza, J.P.1    Gurewich, V.2    Johnstone, M.3    Pannell, R.4
  • 195
    • 0015256028 scopus 로고
    • A prealbumin activator of prekallikrein II. Appearance of chemotactic activity for human neutrophils by the conversion of prekallikrein to kallikrein
    • Kaplan AP, Kay AR, Austen KF: A prealbumin activator of prekallikrein II. Appearance of chemotactic activity for human neutrophils by the conversion of prekallikrein to kallikrein. J Exp Med 135:81, 1972
    • (1972) J Exp Med , vol.135 , pp. 81
    • Kaplan, A.P.1    Kay, A.R.2    Austen, K.F.3
  • 198
    • 0024792576 scopus 로고
    • Purified human plasma kallikrein does not stimulate but primes neutrophils for Superoxide production
    • Zimmerli W, Huber I, Bouma BN, Lammle B: Purified human plasma kallikrein does not stimulate but primes neutrophils for Superoxide production. Thromb Haemost 62:1121, 1989
    • (1989) Thromb Haemost , vol.62 , pp. 1121
    • Zimmerli, W.1    Huber, I.2    Bouma, B.N.3    Lammle, B.4
  • 199
    • 0020084572 scopus 로고
    • Leukocyte elastase release during blood coagulation: A potential mechanism for activation of the alternative fibrinolytic pathway
    • Plow EF: Leukocyte elastase release during blood coagulation: A potential mechanism for activation of the alternative fibrinolytic pathway. J Clin Invest 69:564, 1982
    • (1982) J Clin Invest , vol.69 , pp. 564
    • Plow, E.F.1
  • 200
    • 0020641054 scopus 로고
    • The skin window as a monitor of leukocytic functions in contact activation factor deficiencies in man
    • Rebuck JW: The skin window as a monitor of leukocytic functions in contact activation factor deficiencies in man. Am J Clin Pathol 79:405, 1983
    • (1983) Am J Clin Pathol , vol.79 , pp. 405
    • Rebuck, J.W.1
  • 203
    • 0024230452 scopus 로고
    • Modulation of the human monocyte binding site for monomeric immunoglobulin G by activated Hageman factor
    • Chien P, Pixley RA, Stumpo LG, Colman RW, Schreiber AD: Modulation of the human monocyte binding site for monomeric immunoglobulin G by activated Hageman factor. J Clin Invest 82:1554, 1988
    • (1988) J Clin Invest , vol.82 , pp. 1554
    • Chien, P.1    Pixley, R.A.2    Stumpo, L.G.3    Colman, R.W.4    Schreiber, A.D.5
  • 204
    • 0008216379 scopus 로고
    • Modulation of the human monocyte FcgR1 by activated Hageman factor: Mapping the functional XIIa site
    • abstr
    • Chien P, Pixley RA, Ruiz P, Colman RW, Schreiber AD: Modulation of the human monocyte FcgR1 by activated Hageman factor: Mapping the functional XIIa site. Blood 76:178a, 1990(abstr, suppl 1)
    • (1990) Blood , vol.76 , Issue.1 SUPPL.
    • Chien, P.1    Pixley, R.A.2    Ruiz, P.3    Colman, R.W.4    Schreiber, A.D.5
  • 206
    • 0020587337 scopus 로고
    • Bradykinin-induced release of prostacyclin and thromboxanes from bovine pulmonary artery endothelial cells. Studies with lower homologs and calcium antagonists
    • Crutchley DJ, Ryan JW, Ryan US, Fisher GH: Bradykinin-induced release of prostacyclin and thromboxanes from bovine pulmonary artery endothelial cells. Studies with lower homologs and calcium antagonists. Biochim Biophys Acta 751:99, 1983
    • (1983) Biochim Biophys Acta , vol.751 , pp. 99
    • Crutchley, D.J.1    Ryan, J.W.2    Ryan, U.S.3    Fisher, G.H.4
  • 207
    • 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 SL: Effect of bradykinin and thrombin on prostacyclin synthesis in endothelial cells from calf and pig aorta and human umbilical cord vein. Thromb Res 18:787, 1980
    • (1980) Thromb Res , vol.18 , pp. 787
    • Hong, S.L.1
  • 209
    • 0021930258 scopus 로고
    • Tissue plasminogen activator release in vivo in response to vasoactive agents
    • Smith D, Gilbert M, Owen WG: Tissue plasminogen activator release in vivo in response to vasoactive agents. Blood 66:835, 1983
    • (1983) Blood , vol.66 , pp. 835
    • Smith, D.1    Gilbert, M.2    Owen, W.G.3
  • 210
    • 0030951836 scopus 로고    scopus 로고
    • Selective stimulation of tissue-type plasminogen activator (t-PA) in vivo by infusion of bradykinin
    • Brown NJ, Nadeau JH, Vaughan DE: Selective stimulation of tissue-type plasminogen activator (t-PA) in vivo by infusion of bradykinin. Thromb Haemost 77:522, 1997
    • (1997) Thromb Haemost , vol.77 , pp. 522
    • Brown, N.J.1    Nadeau, J.H.2    Vaughan, D.E.3
  • 211
    • 0023198721 scopus 로고
    • Nitric oxide release accounts for the biologic activity of endothelium-derived relaxing factor
    • Palmer RMJ, Ferrige AG, Moncada S: Nitric oxide release accounts for the biologic activity of endothelium-derived relaxing factor. Nature 327:524, 1987
    • (1987) Nature , vol.327 , pp. 524
    • Palmer, R.M.J.1    Ferrige, A.G.2    Moncada, S.3
  • 212
    • 0027132065 scopus 로고
    • Endothelium-dependent hyperpolarization caused by bradykinin in human coronary arteries
    • Nakashima M, Mombouli JV, Taylor AA, Vanhoutte PM: Endothelium-dependent hyperpolarization caused by bradykinin in human coronary arteries. J Clin Invest 92:2867, 1993
    • (1993) J Clin Invest , vol.92 , pp. 2867
    • Nakashima, M.1    Mombouli, J.V.2    Taylor, A.A.3    Vanhoutte, P.M.4
  • 213
    • 0024998640 scopus 로고
    • Stimulation of cyclic GMP production in cultured endothelial cells of the pig by bradykinin, adenosine diphosphate, calcium ionophore A23187 and nitric oxide
    • Boulanger C, Schini VB, Moncada S, Vanhoutte PM: Stimulation of cyclic GMP production in cultured endothelial cells of the pig by bradykinin, adenosine diphosphate, calcium ionophore A23187 and nitric oxide. Br J Pharmacol 101:152, 1990
    • (1990) Br J Pharmacol , vol.101 , pp. 152
    • Boulanger, C.1    Schini, V.B.2    Moncada, S.3    Vanhoutte, P.M.4
  • 214
    • 0025320649 scopus 로고
    • Bradykinin stimulates the production of cyclic GMP via activation of B2 kinin receptors in cultured porcine aortic endothelial cells
    • Schini VB, Boulanger C, Regoli D, Vanhoutte PM: Bradykinin stimulates the production of cyclic GMP via activation of B2 kinin receptors in cultured porcine aortic endothelial cells. J Pharmacol Exp Ther 252:581, 1990
    • (1990) J Pharmacol Exp Ther , vol.252 , pp. 581
    • Schini, V.B.1    Boulanger, C.2    Regoli, D.3    Vanhoutte, P.M.4
  • 215
    • 0025008449 scopus 로고
    • Induction of nitric oxide synthase by cytokines in vascular smooth muscle cells
    • Busse R, Mulsch A: Induction of nitric oxide synthase by cytokines in vascular smooth muscle cells. FEBS Lett 275:87, 1990
    • (1990) FEBS Lett , vol.275 , pp. 87
    • Busse, R.1    Mulsch, A.2
  • 216
    • 0028345042 scopus 로고
    • Induction of nitric oxide synthase by cyclic AMP in rat vascular smooth muscle cells
    • Imai T, Hirata Y, Kanno K, Marumo F: Induction of nitric oxide synthase by cyclic AMP in rat vascular smooth muscle cells. J Clin Invest 93:543, 1994
    • (1994) J Clin Invest , vol.93 , pp. 543
    • Imai, T.1    Hirata, Y.2    Kanno, K.3    Marumo, F.4
  • 218
    • 0028359305 scopus 로고
    • Bradykinin and angiotensin II: Activation of protein kinase C in arterial smooth muscle
    • Dixon BS, Sharma RV, Dickerson T, Fortune J: Bradykinin and angiotensin II: Activation of protein kinase C in arterial smooth muscle. Am J Physiol 266:C1406, 1994
    • (1994) Am J Physiol , vol.266
    • Dixon, B.S.1    Sharma, R.V.2    Dickerson, T.3    Fortune, J.4
  • 222
    • 85047678143 scopus 로고
    • Endothelial protection by converting enzyme inhibitors
    • Wiemer G, Scholkens BA, Linz W: Endothelial protection by converting enzyme inhibitors. Cardiovasc Res 28:166, 1994
    • (1994) Cardiovasc Res , vol.28 , pp. 166
    • Wiemer, G.1    Scholkens, B.A.2    Linz, W.3
  • 223
    • 85047676402 scopus 로고
    • Cardioprotection by angiotensin converting enzyme inhibitors-the experimental evidence
    • Parratt JR: Cardioprotection by angiotensin converting enzyme inhibitors-the experimental evidence. Circ Res 28:183, 1994
    • (1994) Circ Res , vol.28 , pp. 183
    • Parratt, J.R.1
  • 224
    • 0026665361 scopus 로고
    • ACE-inhibition induces NO-formation in cultured bovine endothelial cells and protects isolated ischemic rat hearts
    • Linz W, Wiemer G, Scholkens BA: ACE-inhibition induces NO-formation in cultured bovine endothelial cells and protects isolated ischemic rat hearts. Mol Cell Cardiol 24:909, 1992
    • (1992) Mol Cell Cardiol , vol.24 , pp. 909
    • Linz, W.1    Wiemer, G.2    Scholkens, B.A.3
  • 225
    • 0027052622 scopus 로고
    • Role of bradykinin in the cardiac effects of angiotensin-converting enzyme inhibitors
    • Linz W, Scholkens BA: Role of bradykinin in the cardiac effects of angiotensin-converting enzyme inhibitors. J Cardiovasc Pharm 20:S83, 1992 (suppl 9)
    • (1992) J Cardiovasc Pharm , vol.20 , Issue.9 SUPPL.
    • Linz, W.1    Scholkens, B.A.2
  • 227
    • 0028814997 scopus 로고
    • Resetting blood pressure in spontaneously hypertensive rats. the role of bradykinin
    • O'Sullivan JB, Harrap SB: Resetting blood pressure in spontaneously hypertensive rats. The role of bradykinin. Hypertension 25:162, 1995
    • (1995) Hypertension , vol.25 , pp. 162
    • O'Sullivan, J.B.1    Harrap, S.B.2
  • 230
    • 0028871228 scopus 로고
    • Intramuscular delivery of rat kallikrein-binding protein gene reverses hypotension in transgenic mice expressing human tissue kallikrein
    • Ma JX, Yang Z, Chao J, Chao L: Intramuscular delivery of rat kallikrein-binding protein gene reverses hypotension in transgenic mice expressing human tissue kallikrein. J Biol Chem 270:451, 1995
    • (1995) J Biol Chem , vol.270 , pp. 451
    • Ma, J.X.1    Yang, Z.2    Chao, J.3    Chao, L.4
  • 232
    • 0025162695 scopus 로고
    • Tissue kallikrein-binding protein is a serpin. I. Purification, characterization, and distribution in normotensive and spontaneously hypertensive rats
    • Chao J, Chai KX, Chen LM, Xiong W, Chao S, Woodley-Miller C, Wang LX, Chao L: Tissue kallikrein-binding protein is a serpin. I. Purification, characterization, and distribution in normotensive and spontaneously hypertensive rats. J Biol Chem 265:16394, 1990
    • (1990) J Biol Chem , vol.265 , pp. 16394
    • Chao, J.1    Chai, K.X.2    Chen, L.M.3    Xiong, W.4    Chao, S.5    Woodley-Miller, C.6    Wang, L.X.7    Chao, L.8
  • 233
    • 0027048724 scopus 로고
    • Kallistatin: A novel human tissue kallikrein inhibitor. Purification, characterization, and reactive center sequence
    • Zhou GX, Chao L, Chao J: Kallistatin: A novel human tissue kallikrein inhibitor. Purification, characterization, and reactive center sequence. J Biol Chem 267:25873, 1992
    • (1992) J Biol Chem , vol.267 , pp. 25873
    • Zhou, G.X.1    Chao, L.2    Chao, J.3
  • 234
    • 0028908138 scopus 로고
    • Direct gene delivery of human tissue kallikrein reduces blood pressure in spontaneously hypertensive rats
    • Wang C, Chao L, Chao J: Direct gene delivery of human tissue kallikrein reduces blood pressure in spontaneously hypertensive rats [see comments]. J Clin Invest 95:1710, 1995
    • (1995) J Clin Invest , vol.95 , pp. 1710
    • Wang, C.1    Chao, L.2    Chao, J.3
  • 235
    • 0028925801 scopus 로고
    • Muscle delivery of human kallikrein gene reduces blood pressure in hypertensive rats
    • Xiong W, Chao J, Chao L: Muscle delivery of human kallikrein gene reduces blood pressure in hypertensive rats. Hypertension 25:715, 1995
    • (1995) Hypertension , vol.25 , pp. 715
    • Xiong, W.1    Chao, J.2    Chao, L.3
  • 237
    • 0019972732 scopus 로고
    • Effects of tertiary amine local anesthetics on von Willebrand factor-dependent platelet function: Alteration of membrane reactivity and degradation of GPIb by a calcium-dependent protease(s)
    • Coller BS: Effects of tertiary amine local anesthetics on von Willebrand factor-dependent platelet function: Alteration of membrane reactivity and degradation of GPIb by a calcium-dependent protease(s). Blood 60:731, 1982
    • (1982) Blood , vol.60 , pp. 731
    • Coller, B.S.1
  • 238
    • 0024325179 scopus 로고
    • Modulation of thrombin-induced platelet aggregation by inhibition of calpain by a synthetic peptide derived from the thiol-protease inhibitory sequence of kininogens and S-(3-nitro-2-pyridinesulfenyl)-cysteine
    • Puri RN, Matsueda R, Umeyama H, Bradford HN, Colman RW: Modulation of thrombin-induced platelet aggregation by inhibition of calpain by a synthetic peptide derived from the thiol-protease inhibitory sequence of kininogens and S-(3-nitro-2-pyridinesulfenyl)-cysteine. Biochem Biophys Res Commun 162:1017, 1989
    • (1989) Biochem Biophys Res Commun , vol.162 , pp. 1017
    • Puri, R.N.1    Matsueda, R.2    Umeyama, H.3    Bradford, H.N.4    Colman, R.W.5
  • 239
    • 0028065814 scopus 로고
    • Design and synthesis of a kininogen-based selective inhibitor of thrombin-induced platelet aggregation
    • Matsueda R, Umeyama H, Puri RN, Bradford HN, Colman RW: Design and synthesis of a kininogen-based selective inhibitor of thrombin-induced platelet aggregation. Pept Res 7:32, 1994
    • (1994) Pept Res , vol.7 , pp. 32
    • Matsueda, R.1    Umeyama, H.2    Puri, R.N.3    Bradford, H.N.4    Colman, R.W.5
  • 240
    • 0017672833 scopus 로고
    • Interrelations of platelet aggregation and secretion
    • Charo IF, Feinman RD, Detwiler TC: Interrelations of platelet aggregation and secretion. J Clin Invest 60:866, 1977
    • (1977) J Clin Invest , vol.60 , pp. 866
    • Charo, I.F.1    Feinman, R.D.2    Detwiler, T.C.3
  • 241
    • 0026446856 scopus 로고
    • PPACK-thrombin is a noncompetitive inhibitor of alpha-thrombin binding to human platelets
    • Schmaier AH, Meloni FJ, Nawarawong W, Jiang YP: PPACK-thrombin is a noncompetitive inhibitor of alpha-thrombin binding to human platelets. Thromb Res 67:479, 1992
    • (1992) Thromb Res , vol.67 , pp. 479
    • Schmaier, A.H.1    Meloni, F.J.2    Nawarawong, W.3    Jiang, Y.P.4
  • 243
    • 0027466082 scopus 로고
    • Detection of the degradation products of bradykinin by enzyme immunoassays as markers for the release of kinin in vivo
    • Majima M, Sunahara N, Harada Y, Katori M: Detection of the degradation products of bradykinin by enzyme immunoassays as markers for the release of kinin in vivo. Biochem Pharmacol 45:559, 1993
    • (1993) Biochem Pharmacol , vol.45 , pp. 559
    • Majima, M.1    Sunahara, N.2    Harada, Y.3    Katori, M.4
  • 244
    • 0026457543 scopus 로고
    • A stable metabolite, Arg-Pro-Pro-Gly-Phe, of bradykinin in the degradation pathway in human plasma
    • Shima C, Majima M, Katori M: A stable metabolite, Arg-Pro-Pro-Gly-Phe, of bradykinin in the degradation pathway in human plasma. Jpn J Pharmacol 60:111, 1992
    • (1992) Jpn J Pharmacol , vol.60 , pp. 111
    • Shima, C.1    Majima, M.2    Katori, M.3
  • 245
    • 70449281229 scopus 로고
    • Role of the contact factor (Hageman factor) in fibrinolysis
    • Niewiarowski S, Prou-Wartelle O: Role of the contact factor (Hageman factor) in fibrinolysis. Thromb Diath Haemorrh 3:593, 1959
    • (1959) Thromb Diath Haemorrh , vol.3 , pp. 593
    • Niewiarowski, S.1    Prou-Wartelle, O.2
  • 246
    • 0014694698 scopus 로고
    • Activation of plasminogen by human plasma kallikrein
    • Colman RW: Activation of plasminogen by human plasma kallikrein. Biochem Biophys Res Commun 35:273, 1969
    • (1969) Biochem Biophys Res Commun , vol.35 , pp. 273
    • Colman, R.W.1
  • 247
    • 0017738854 scopus 로고
    • Human plasma prekallikrein: Mechanism of activation by Hageman factor and participation in Hageman-factor-dependent fibrinolysis
    • Mandle RJ Jr, Kaplan AP: Human plasma prekallikrein: Mechanism of activation by Hageman factor and participation in Hageman-factor-dependent fibrinolysis. J Biol Chem 252:6097, 1977
    • (1977) J Biol Chem , vol.252 , pp. 6097
    • Mandle Jr., R.J.1    Kaplan, A.P.2
  • 248
    • 0018103306 scopus 로고
    • The activation of plasminogen by Hageman FXII (factor XII) and Hageman factor fragments
    • Goldsmith G, Saito H, Ratnoff OD: The activation of plasminogen by Hageman FXII (factor XII) and Hageman factor fragments. J Clin Invest 62:54, 1978
    • (1978) J Clin Invest , vol.62 , pp. 54
    • Goldsmith, G.1    Saito, H.2    Ratnoff, O.D.3
  • 249
    • 0018716550 scopus 로고
    • Hageman-factor-dependent fibrinolysis: Generation of fibrinolytic activity by the interaction of human activated factor XI and plasminogen
    • Mandle RJ Jr, Kaplan AP: Hageman-factor-dependent fibrinolysis: Generation of fibrinolytic activity by the interaction of human activated factor XI and plasminogen. Blood 54:850, 1979
    • (1979) Blood , vol.54 , pp. 850
    • Mandle Jr., R.J.1    Kaplan, A.P.2
  • 250
    • 0027419518 scopus 로고
    • Pro-urokinase and prekallikrein are both associated with platelets. Implications for the intrinsic pathway of fibrinolysis and for therapeutic thrombolysis
    • Gurewich V, Johnstone M, Loza JP, Pannell R: Pro-urokinase and prekallikrein are both associated with platelets. Implications for the intrinsic pathway of fibrinolysis and for therapeutic thrombolysis. FEBS Lett 318:317, 1993
    • (1993) FEBS Lett , vol.318 , pp. 317
    • Gurewich, V.1    Johnstone, M.2    Loza, J.P.3    Pannell, R.4
  • 251
    • 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 RB, Van W, McCrae KR, Zhang H Colman RW: High molecular weight kininogen peptides inhibit the formation of kallikrein on endothelial cell surfaces and subsequent urokinase-dependent plasmin formation. Blood 90:690, 1997
    • (1997) Blood , vol.90 , pp. 690
    • Lin, Y.1    Harris, R.B.2    Van, W.3    McCrae, K.R.4    Zhang, H.5    Colman, R.W.6
  • 252
    • 0029149373 scopus 로고
    • Enhancement of the enzymatic activity of single-chain urokinase plasminogen activator by soluble urokinase receptor
    • Higazi A, Cohen RL, Henkin J, Kniss D, Schwartz BS, Cines DB: Enhancement of the enzymatic activity of single-chain urokinase plasminogen activator by soluble urokinase receptor. J Biol Chem 21:17375, 1995
    • (1995) J Biol Chem , vol.21 , pp. 17375
    • Higazi, A.1    Cohen, R.L.2    Henkin, J.3    Kniss, D.4    Schwartz, B.S.5    Cines, D.B.6
  • 253
    • 0014223259 scopus 로고
    • Possible involvement of fibrinogen and proteolysis in surface activation: A study with the recording ellipsometer
    • Vroman L, Adams A: Possible involvement of fibrinogen and proteolysis in surface activation: A study with the recording ellipsometer. Thromb Diath Haemorrh 18:510, 1967
    • (1967) Thromb Diath Haemorrh , vol.18 , pp. 510
    • Vroman, L.1    Adams, A.2
  • 255
    • 0023915422 scopus 로고
    • Mechanism of transient adsorption of fibrinogen from plasma to solid surfaces: Role of the contact and fibrinolytic systems
    • Brash JL, Scott CF, ten Hove P, Wojciechowski P, Colman RW: Mechanism of transient adsorption of fibrinogen from plasma to solid surfaces: Role of the contact and fibrinolytic systems. Blood 71:932, 1988
    • (1988) Blood , vol.71 , pp. 932
    • Brash, J.L.1    Scott, C.F.2    Ten Hove, P.3    Wojciechowski, P.4    Colman, R.W.5
  • 256
    • 0029949824 scopus 로고    scopus 로고
    • Neutrophil adhesion on surfaces preadsorbed with high molecular weight kininogen under well-defined flow conditions
    • Yung LL, Lim F, Khan MMH, Kunapuli SP, Rick L, Colman RW, Cooper SL: Neutrophil adhesion on surfaces preadsorbed with high molecular weight kininogen under well-defined flow conditions. Immunopharmacology 32:9, 1996
    • (1996) Immunopharmacology , vol.32 , pp. 9
    • Yung, L.L.1    Lim, F.2    Khan, M.M.H.3    Kunapuli, S.P.4    Rick, L.5    Colman, R.W.6    Cooper, S.L.7
  • 257
    • 50549190821 scopus 로고
    • Biochemical abnormality in hereditary angioneurotic edema
    • Donaldson VH, Evans RR: Biochemical abnormality in hereditary angioneurotic edema. Am J Med 35:37, 1963
    • (1963) Am J Med , vol.35 , pp. 37
    • Donaldson, V.H.1    Evans, R.R.2
  • 258
    • 0000144923 scopus 로고
    • Some properties of an esterase derived from preparations of the first component of complement
    • Ratnoff OD, Lepow IH: Some properties of an esterase derived from preparations of the first component of complement. J Exp Med 106:327, 1955
    • (1955) J Exp Med , vol.106 , pp. 327
    • Ratnoff, O.D.1    Lepow, I.H.2
  • 259
    • 33847577173 scopus 로고
    • Hereditary angioneurotic edema. I. Case reports and review of the literature
    • Landerman NS Hereditary angioneurotic edema. I. Case reports and review of the literature. J Allergy Clin Immunol 33:316, 1962
    • (1962) J Allergy Clin Immunol , vol.33 , pp. 316
    • Landerman, N.S.1
  • 262
    • 0022543615 scopus 로고
    • Detection of in vitro and in vivo cleavage of high molecular weight kininogen in human plasma by immunblotting with monoclonal antibodies
    • Berrettini M, Lammle B, White T, Heeb MJ, Schwarz HP, Zuraw B, Curd J, Griffin JH: Detection of in vitro and in vivo cleavage of high molecular weight kininogen in human plasma by immunblotting with monoclonal antibodies. Blood 68:455, 1986
    • (1986) Blood , vol.68 , pp. 455
    • Berrettini, M.1    Lammle, B.2    White, T.3    Heeb, M.J.4    Schwarz, H.P.5    Zuraw, B.6    Curd, J.7    Griffin, J.H.8
  • 263
    • 0020520854 scopus 로고
    • Kinin formation in hereditary angioedema plasma: Evidence aginst kinin derivation from C2 and in support of "spontaneous" formation of bradykinin
    • Fields AP, Ghebrehiwet B, Kaplan AP: Kinin formation in hereditary angioedema plasma: Evidence aginst kinin derivation from C2 and in support of "spontaneous" formation of bradykinin. J Allergy Clin Immunol 72:54, 1983
    • (1983) J Allergy Clin Immunol , vol.72 , pp. 54
    • Fields, A.P.1    Ghebrehiwet, B.2    Kaplan, A.P.3
  • 264
    • 0041597554 scopus 로고
    • Effect of glass upon the activation of various plasma clotting factors
    • Rapaport S, Aas K, Owen PA: Effect of glass upon the activation of various plasma clotting factors. J Clin Invest 34:9, 1955
    • (1955) J Clin Invest , vol.34 , pp. 9
    • Rapaport, S.1    Aas, K.2    Owen, P.A.3
  • 265
    • 0015531092 scopus 로고
    • Cold-promoted activation of factor VII. III. Relation to the kallikrein system
    • Gjonnaess H: Cold-promoted activation of factor VII. III. Relation to the kallikrein system. Thromb Diath Haemorrh 28:182, 1972
    • (1972) Thromb Diath Haemorrh , vol.28 , pp. 182
    • Gjonnaess, H.1
  • 267
    • 0022555655 scopus 로고
    • The effect of C1 inhibitor upon Hageman factor autoactivation
    • Weiss R, Kaplan AP: The effect of C1 inhibitor upon Hageman factor autoactivation. Blood 68:239, 1986
    • (1986) Blood , vol.68 , pp. 239
    • Weiss, R.1    Kaplan, A.P.2
  • 268
    • 0021871268 scopus 로고
    • Activation and inhibition of Hageman factor-dependent pathways and the complement system in uncomplicated bacteremia or bacterial shock
    • Kalter ES, Daha MR, Verhoef J, Bouma BN: Activation and inhibition of Hageman factor-dependent pathways and the complement system in uncomplicated bacteremia or bacterial shock. J Infect Dis 151:1019, 1985
    • (1985) J Infect Dis , vol.151 , pp. 1019
    • Kalter, E.S.1    Daha, M.R.2    Verhoef, J.3    Bouma, B.N.4
  • 269
    • 0024524898 scopus 로고
    • The role of plasma proteases in septic shock
    • Colman RW: The role of plasma proteases in septic shock. N Engl J Med 320:1207, 1989
    • (1989) N Engl J Med , vol.320 , pp. 1207
    • Colman, R.W.1
  • 271
    • 0015247178 scopus 로고
    • The role of Hageman factor in disseminated intravascular coagulation induced by septicemia, neoplasia, or liver disease
    • Mason JW, Colman RW: The role of Hageman factor in disseminated intravascular coagulation induced by septicemia, neoplasia, or liver disease. Thromb Diath Haemorrh 26:325, 1971
    • (1971) Thromb Diath Haemorrh , vol.26 , pp. 325
    • Mason, J.W.1    Colman, R.W.2
  • 273
    • 0017817930 scopus 로고
    • Plasma kallikrein activation and inhibition during typhoid fever
    • Colman RW, Edelman R, Scott CF, Gilman RH: Plasma kallikrein activation and inhibition during typhoid fever. J Clin Invest 61:287, 1978
    • (1978) J Clin Invest , vol.61 , pp. 287
    • Colman, R.W.1    Edelman, R.2    Scott, C.F.3    Gilman, R.H.4
  • 277
    • 0025848380 scopus 로고
    • Alpha 2-macroglobulin-kallikrein complexes detect contact system activation in hereditary angioedema and human sepsis
    • Kaufman N, Page JD, Pixley RA, Schein R, Schmaier AH, Colman RW: Alpha 2-macroglobulin-kallikrein complexes detect contact system activation in hereditary angioedema and human sepsis. Blood 77:2660, 1991
    • (1991) Blood , vol.77 , pp. 2660
    • Kaufman, N.1    Page, J.D.2    Pixley, R.A.3    Schein, R.4    Schmaier, A.H.5    Colman, R.W.6
  • 280
    • 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 RA, DeLa Cadena RA, Page JD, Kaufman N, Wyshock EG, Chang A, Taylor FB Jr, Colman RW: 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 91:61, 1993
    • (1993) J Clin Invest , vol.91 , pp. 61
    • Pixley, R.A.1    DeLa Cadena, R.A.2    Page, J.D.3    Kaufman, N.4    Wyshock, E.G.5    Chang, A.6    Taylor Jr., F.B.7    Colman, R.W.8
  • 282
    • 0024476498 scopus 로고
    • Formation of C1s-C1-inhibitor, kallikrein-C1-inhibitor, and plasminalpha 2-plasmin-inhibitor complexes during cardiopulmonary by-pass
    • Wachtfogel YT, Harpel PC, Edmunds LH Jr, Colman RW: Formation of C1s-C1-inhibitor, kallikrein-C1-inhibitor, and plasminalpha 2-plasmin-inhibitor complexes during cardiopulmonary by-pass. Blood 73:468, 1989
    • (1989) Blood , vol.73 , pp. 468
    • Wachtfogel, Y.T.1    Harpel, P.C.2    Edmunds Jr., L.H.3    Colman, R.W.4
  • 289
    • 0029986326 scopus 로고    scopus 로고
    • Inhibition of factor XII in septic baboons attenuates the activation of complement and fibrinolytic systems and reduces the release of interleukin-6 and neutrophil elastase
    • Jansen PM, Pixley RA, Brouwer M, DeJong IW, Chang AK, Hack CE, Taylor FB Jr, Colman RW: Inhibition of factor XII in septic baboons attenuates the activation of complement and fibrinolytic systems and reduces the release of interleukin-6 and neutrophil elastase. Blood 87:2337, 1996
    • (1996) Blood , vol.87 , pp. 2337
    • Jansen, P.M.1    Pixley, R.A.2    Brouwer, M.3    DeJong, I.W.4    Chang, A.K.5    Hack, C.E.6    Taylor Jr., F.B.7    Colman, R.W.8
  • 290
    • 0020565895 scopus 로고
    • Thrombosis or myocardial infarction in congenital clotting factor abnormalities and chronic thrombocytopenias: A report of 21 patients and a review of 50 previously reported cases
    • Baltimore
    • Goodnough LT, Saito H, Ratnoff OD: Thrombosis or myocardial infarction in congenital clotting factor abnormalities and chronic thrombocytopenias: A report of 21 patients and a review of 50 previously reported cases [Review]. Medicine (Baltimore) 62:248, 1983
    • (1983) Medicine , vol.62 , pp. 248
    • Goodnough, L.T.1    Saito, H.2    Ratnoff, O.D.3
  • 291
    • 0003371207 scopus 로고
    • Factor XII activity and antigen concentrations in patients suffering from recurrent thrombosis
    • Mannhalter C, Fisher M, Hopmeier P, Deutch E: Factor XII activity and antigen concentrations in patients suffering from recurrent thrombosis. Fibrinolysis 1:259, 1987
    • (1987) Fibrinolysis , vol.1 , pp. 259
    • Mannhalter, C.1    Fisher, M.2    Hopmeier, P.3    Deutch, E.4
  • 292
    • 0026065260 scopus 로고
    • Thromboembolism and bleeding tendency in congenital factor XII deficiency: A study on 74 subjects from 14 Swiss families
    • Lammle B, Wuillemin WA, Huber I, Krauskopf M, Zurcher C, Pflugshaupt R, Furlan M: Thromboembolism and bleeding tendency in congenital factor XII deficiency: A study on 74 subjects from 14 Swiss families. Thromb Haemost 65:117, 1991
    • (1991) Thromb Haemost , vol.65 , pp. 117
    • Lammle, B.1    Wuillemin, W.A.2    Huber, I.3    Krauskopf, M.4    Zurcher, C.5    Pflugshaupt, R.6    Furlan, M.7
  • 293
    • 0026803207 scopus 로고
    • The prevalence of factor XII deficiency in 103 orally anticoagulated outpatients suffering from recurrent venous and/or arterial thromboembolism
    • Halbmayer WM, Mannhalter C, Feichtinger C, Rubi K, Fischer M: The prevalence of factor XII deficiency in 103 orally anticoagulated outpatients suffering from recurrent venous and/or arterial thromboembolism. Thromb Haemost 68:285, 1992
    • (1992) Thromb Haemost , vol.68 , pp. 285
    • Halbmayer, W.M.1    Mannhalter, C.2    Feichtinger, C.3    Rubi, K.4    Fischer, M.5
  • 294
    • 0026458603 scopus 로고
    • Factor XII clotting activity and antigen levels in patients with thromboembolic disease
    • von Kanel R, Wuillemin WA, Furlan M, Lammle B: Factor XII clotting activity and antigen levels in patients with thromboembolic disease. Blood Coagul Fibrinolysis 3:555, 1992
    • (1992) Blood Coagul Fibrinolysis , vol.3 , pp. 555
    • Von Kanel, R.1    Wuillemin, W.A.2    Furlan, M.3    Lammle, B.4
  • 295
    • 0027057953 scopus 로고
    • Evidence for a role of factor XII-dependent fibrinolysis in cardiovascular diseases
    • Jespersen J, Munkvad S, Pedersen OD, Gram J, Kluft C: Evidence for a role of factor XII-dependent fibrinolysis in cardiovascular diseases. Ann NY Acad Sci 667:454, 1992
    • (1992) Ann NY Acad Sci , vol.667 , pp. 454
    • Jespersen, J.1    Munkvad, S.2    Pedersen, O.D.3    Gram, J.4    Kluft, C.5
  • 296
    • 44949281924 scopus 로고
    • Long-lasting depression of the factor XII-dependent fibrinolytic system in patients with myocardial infarction undergoing thrombolytic therapy with recombinant tissue-type plasminogen activator: A randomized placebo-controlled study
    • Munkvad S, Jespersen J, Gram J, Kluft C: Long-lasting depression of the factor XII-dependent fibrinolytic system in patients with myocardial infarction undergoing thrombolytic therapy with recombinant tissue-type plasminogen activator: A randomized placebo-controlled study. J Am Coll Cardiol 17:957, 1991
    • (1991) J Am Coll Cardiol , vol.17 , pp. 957
    • Munkvad, S.1    Jespersen, J.2    Gram, J.3    Kluft, C.4


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