메뉴 건너뛰기




Volumn 92, Issue 6, 2004, Pages 1277-1283

Inhibition of plasma kallikrein by CI-inhibitor: Role of endothelial cells and the amino-terminal domain of CI-inhibitor

Author keywords

Coagulation inhibitors; Contact phase; Endothelial cells; Proteases inhibitors

Indexed keywords

COMPLEMENT COMPONENT C1S INHIBITOR; HIGH MOLECULAR WEIGHT KININOGEN; KALLIKREIN; METALLOPROTEINASE; PREKALLIKREIN;

EID: 10444240277     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH04-01-0008     Document Type: Article
Times cited : (26)

References (34)
  • 2
    • 0023099697 scopus 로고
    • Molecular basis for the deficiency of complement 1 inhibitor in type I hereditary angioneurotic edema
    • Cicardi M, Igarashi T, Rosen FS, et al. Molecular basis for the deficiency of complement 1 inhibitor in type I hereditary angioneurotic edema. J Clin Invest 1987; 79: 698-702.
    • (1987) J. Clin. Invest. , vol.79 , pp. 698-702
    • Cicardi, M.1    Igarashi, T.2    Rosen, F.S.3
  • 3
    • 0027404944 scopus 로고
    • Transinhibition of C1 inhibitor synthesis in type I hereditary angioneurotic edema
    • Kramer J, Rosen FS, Cohen HR, et al. Transinhibition of C1 inhibitor synthesis in type I hereditary angioneurotic edema. J Clin Invest 1993; 91: 1258-62.
    • (1993) J. Clin. Invest. , vol.91 , pp. 1258-1262
    • Kramer, J.1    Rosen, F.S.2    Cohen, H.R.3
  • 4
    • 4444221542 scopus 로고    scopus 로고
    • C1 inhibitor gene expression in patients with hereditary angioedema: Quantitative evaluation by means of real-time RT-PCR
    • Pappalardo E, Zingale LC, Cicardi M. C1 inhibitor gene expression in patients with hereditary angioedema: Quantitative evaluation by means of real-time RT-PCR. J Allergy Clin Immunol 2004; 114: 638-44.
    • (2004) J. Allergy Clin. Immunol. , vol.114 , pp. 638-644
    • Pappalardo, E.1    Zingale, L.C.2    Cicardi, M.3
  • 6
    • 0142169437 scopus 로고    scopus 로고
    • The pathogenesis of hereditary angioedema
    • Davis AE 3rd. The pathogenesis of hereditary angioedema. Transfusion Apher Sci 2003; 29: 195-203.
    • (2003) Transfusion Apher. Sci. , vol.29 , pp. 195-203
    • Davis III, A.E.1
  • 7
    • 0031973492 scopus 로고    scopus 로고
    • High molecular weight kininogen regulates prekallikrein assembly and activation on endothelial cells: A novel mechanism for contact activation
    • Motta G, Rojkjaer R, Hasan AAK, et al. High molecular weight kininogen regulates prekallikrein assembly and activation on endothelial cells: A novel mechanism for contact activation. Blood 1998; 91: 516-28.
    • (1998) Blood , vol.91 , pp. 516-528
    • Motta, G.1    Rojkjaer, R.2    Hasan, A.A.K.3
  • 8
    • 0032695008 scopus 로고    scopus 로고
    • Activation of the plasma kallikrein/kinin system on cells: A revised hypothesis
    • Schmaier AH, Røjkjær R, Shariat-Madar Z. Activation of the plasma kallikrein/kinin system on cells: A revised hypothesis. Thromb Haemost 1999; 82: 226-33.
    • (1999) Thromb. Haemost. , vol.82 , pp. 226-233
    • Schmaier, A.H.1    Røjkjær, R.2    Shariat-Madar, Z.3
  • 9
    • 0036120563 scopus 로고    scopus 로고
    • The plasma kallikrein-kinin system counterbalances the renin-angiotensin system
    • Schmaier AH. The plasma kallikrein-kinin system counterbalances the renin-angiotensin system. J Clin Invest 2002; 109: 1007-9.
    • (2002) J. Clin. Invest. , vol.109 , pp. 1007-1009
    • Schmaier, A.H.1
  • 10
    • 0037124049 scopus 로고    scopus 로고
    • Identification and characterization of prolylcarboxypeptidase as an endothelial cell prekallikrein activator
    • Shariat-Madar Z, Mahdi F, Schmaier AH. Identification and characterization of prolylcarboxypeptidase as an endothelial cell prekallikrein activator. J Biol Chem 2002; 277; 17962-9.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17962-17969
    • Shariat-Madar, Z.1    Mahdi, F.2    Schmaier, A.H.3
  • 11
    • 0037125229 scopus 로고    scopus 로고
    • Identification of prolylcarboxypeptidase as the cell matrix-associated prekallikrein activator
    • Moreira CR, Schmaier AH, Mahdi F, et al. Identification of prolylcarboxypeptidase as the cell matrix-associated prekallikrein activator. FEBS Lett 2002; 523: 167-70.
    • (2002) FEBS Lett. , vol.523 , pp. 167-170
    • Moreira, C.R.1    Schmaier, A.H.2    Mahdi, F.3
  • 12
    • 0035115246 scopus 로고    scopus 로고
    • Activation of the kinin-forming cascade on the surface of endothelial cells
    • Joseph K, Ghebrehiwet B, Kaplan AP. Activation of the kinin-forming cascade on the surface of endothelial cells. Biol Chem 2001; 382: 71-5.
    • (2001) Biol. Chem. , vol.382 , pp. 71-75
    • Joseph, K.1    Ghebrehiwet, B.2    Kaplan, A.P.3
  • 13
    • 0037154220 scopus 로고    scopus 로고
    • Heat shock protein 90 catalyzes activation of the prekallikrein-kininogen complex in the absence of factor XII
    • Joseph K, Tholanikunnel BG, Kaplan AP. Heat shock protein 90 catalyzes activation of the prekallikrein-kininogen complex in the absence of factor XII. Proc Natl Acad Sci USA 2002; 99: 896-900.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 896-900
    • Joseph, K.1    Tholanikunnel, B.G.2    Kaplan, A.P.3
  • 14
    • 0037093204 scopus 로고    scopus 로고
    • Factor XII interacts with the multiprotein assembly of urokinase plasminogen activator receptor, gC1qR, and cytokeratin 1 on endothelial cell membranes
    • Mahdi F, Shariat-Madar Z, Figueroa CD, et al. Factor XII interacts with the multiprotein assembly of urokinase plasminogen activator receptor, gC1qR, and cytokeratin 1 on endothelial cell membranes. Blood 2002; 99: 3585-96.
    • (2002) Blood , vol.99 , pp. 3585-3596
    • Mahdi, F.1    Shariat-Madar, Z.2    Figueroa, C.D.3
  • 15
    • 0031878996 scopus 로고    scopus 로고
    • Factor XII does not initiate prekallikrein activation on endothelial cells
    • Rojkjaer R, Hasan AA, Motta G, et al. Factor XII does not initiate prekallikrein activation on endothelial cells. Thromb Haemost 1998; 80: 74-81.
    • (1998) Thromb. Haemost. , vol.80 , pp. 74-81
    • Rojkjaer, R.1    Hasan, A.A.2    Motta, G.3
  • 16
    • 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 1982; 69: 462-8.
    • (1982) J. Clin. Invest. , vol.69 , pp. 462-468
    • Schapira, M.1    Scott, C.F.2    Colman, R.W.3
  • 19
    • 0020629994 scopus 로고
    • Interaction of human plasma kallikrein and its light chain with C1 inhibitor
    • van der Graaf F, Koedam JA, Griffin JH, et al. Interaction of human plasma kallikrein and its light chain with C1 inhibitor. Biochemistry 1983; 22: 4860-6.
    • (1983) Biochemistry , vol.22 , pp. 4860-4866
    • van der Graaf, F.1    Koedam, J.A.2    Griffin, J.H.3
  • 20
    • 0024476498 scopus 로고
    • Formation of C1s-C1-inhibitor, kallikrein-C1-inhibitor, and plasmin-α2-plasmin-inhibitor complexes during cardiopulmonary bypass
    • Wachtfogel Y, Harpel PC, Edmunds Jr H, et al. Formation of C1s-C1-inhibitor, kallikrein-C1-inhibitor, and plasmin-α2-plasmin-inhibitor complexes during cardiopulmonary bypass. Blood 1989; 73: 468-71.
    • (1989) Blood , vol.73 , pp. 468-471
    • Wachtfogel, Y.1    Harpel, P.C.2    Edmunds Jr., H.3
  • 21
    • 0025911486 scopus 로고
    • Western blot analyses of prekallikrein and its activation products in human plasma
    • Veloso D, Colman RW. Western blot analyses of prekallikrein and its activation products in human plasma. Thromb Haemost 1991; 65: 382-8.
    • (1991) Thromb. Haemost. , vol.65 , pp. 382-388
    • Veloso, D.1    Colman, R.W.2
  • 22
    • 0036919373 scopus 로고    scopus 로고
    • The reaction between plasmin and C1-inhibitor results in plasmin inhibition by the serpin mechanism
    • Brown EW, Ravindran S, Patston PA. The reaction between plasmin and C1-inhibitor results in plasmin inhibition by the serpin mechanism. Blood Coag Fibrinolys 2002; 13: 711-4.
    • (2002) Blood Coag. Fibrinolys. , vol.13 , pp. 711-714
    • Brown, E.W.1    Ravindran, S.2    Patston, P.A.3
  • 23
    • 0036065259 scopus 로고    scopus 로고
    • StcE, a metalloprotease secreted by Escherichia coli O157:H7, specifically cleaves C1 esterase inhibitor
    • Lathem WW, Grys TE, Witowski SE, et al. StcE, a metalloprotease secreted by Escherichia coli O157:H7, specifically cleaves C1 esterase inhibitor. Mol Microbiol 2002; 45: 277-88.
    • (2002) Mol. Microbiol. , vol.45 , pp. 277-288
    • Lathem, W.W.1    Grys, T.E.2    Witowski, S.E.3
  • 24
    • 0025788321 scopus 로고
    • Mechanism of serpin action: Evidence that C1 inhibitor functions as a suicide substrate
    • Patston PA, Gettins P, Beechem J, et al. Mechanism of serpin action: evidence that C1 inhibitor functions as a suicide substrate. Biochemistry 1991; 30: 8876-82.
    • (1991) Biochemistry , vol.30 , pp. 8876-8882
    • Patston, P.A.1    Gettins, P.2    Beechem, J.3
  • 25
    • 0036708006 scopus 로고    scopus 로고
    • 1-Proteinase inhibitor mutants with specificity for plasma kallikrein and C1s but not C1
    • 1-Proteinase inhibitor mutants with specificity for plasma kallikrein and C1s but not C1. Protein Sci 2002; 11: 2230-6.
    • (2002) Protein. Sci. , vol.11 , pp. 2230-2236
    • Sulikowski, T.1    Bauer, B.A.2    Patston, P.A.3
  • 26
    • 0020364908 scopus 로고
    • Isolation and functional properties of the heavy and light chains of human plasma kallikrein
    • van der Graaf F, Tans G, Bouma BN, et al. Isolation and functional properties of the heavy and light chains of human plasma kallikrein. J Biol Chem 1982; 257: 14300-5.
    • (1982) J. Biol. Chem. , vol.257 , pp. 14300-14305
    • van der Graaf, F.1    Tans, G.2    Bouma, B.N.3
  • 27
    • 0037221757 scopus 로고    scopus 로고
    • Binding of activated Factor XII to endothelial cells affects its inactivation by the C1-esterase inhibitor
    • Schousboe I. Binding of activated Factor XII to endothelial cells affects its inactivation by the C1-esterase inhibitor. Eur J Biochem 2003; 270: 111-8.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 111-118
    • Schousboe, I.1
  • 28
    • 2442509635 scopus 로고    scopus 로고
    • Potentiation of C1 esterase inhibitor by StcE, a metalloprotease secreted by Escherichia coli O157:H7
    • Lathem WW, Bergsbaken T, Welch RA. Potentiation of C1 esterase inhibitor by StcE, a metalloprotease secreted by Escherichia coli O157:H7. J Exp Med 2004; 199: 1077-87.
    • (2004) J. Exp. Med. , vol.199 , pp. 1077-1087
    • Lathem, W.W.1    Bergsbaken, T.2    Welch, R.A.3
  • 29
    • 0022556870 scopus 로고
    • Human C1 inhibitor: Primary structure, cDNA cloning, and chromosomal localization
    • Bock SC, Skriver K, Nielsen E, et al. Human C1 inhibitor: primary structure, cDNA cloning, and chromosomal localization. Biochemistry 1986; 25: 4292-301.
    • (1986) Biochemistry , vol.25 , pp. 4292-4301
    • Bock, S.C.1    Skriver, K.2    Nielsen, E.3
  • 30
    • 0025180336 scopus 로고
    • Two-domain structure of the native and reactive centre cleaved forms of C1 inhibitor of human complement by neutron scattering
    • Perkins SJ, Smith KF, Amatayakul S, et al. Two-domain structure of the native and reactive centre cleaved forms of C1 inhibitor of human complement by neutron scattering. J Mol Biol 1990; 214: 751-63.
    • (1990) J. Mol. Biol. , vol.214 , pp. 751-763
    • Perkins, S.J.1    Smith, K.F.2    Amatayakul, S.3
  • 31
    • 0041929232 scopus 로고    scopus 로고
    • C1 inhibitor prevents endotoxin shock via a direct interaction with lipopolysaccharide
    • Liu D, Cai S, Gu X, et al. C1 inhibitor prevents endotoxin shock via a direct interaction with lipopolysaccharide. J Immunol 2003; 171: 2594-601.
    • (2003) J. Immunol. , vol.171 , pp. 2594-2601
    • Liu, D.1    Cai, S.2    Gu, X.3
  • 32
    • 1842536366 scopus 로고    scopus 로고
    • N-linked glycosylation is required for C1 inhibitor-mediated protection from endotoxin shock in mice
    • Liu D, Gu X, Scafidi J, et al. N-linked glycosylation is required for C1 inhibitor-mediated protection from endotoxin shock in mice. Infect Immun 2004; 72: 1946-55.
    • (2004) Infect. Immun. , vol.72 , pp. 1946-1955
    • Liu, D.1    Gu, X.2    Scafidi, J.3
  • 33
    • 0036122075 scopus 로고    scopus 로고
    • Increased vascular permeability in C1 inhibitor-deficient mice mediated by the bradykinin type 2 receptor
    • Han ED, MacFarlane RC, Mulligan AN, et al. Increased vascular permeability in C1 inhibitor-deficient mice mediated by the bradykinin type 2 receptor. J Clin Invest 2002; 109: 1057-63.
    • (2002) J. Clin. Invest. , vol.109 , pp. 1057-1063
    • Han, E.D.1    MacFarlane, R.C.2    Mulligan, A.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.