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Volumn 33, Issue 4, 2013, Pages 513-533

Contact System Activation in Patients with HAE and Normal C1Inhibitor Function

Author keywords

Contact phase; Factor XII; Kallikrein; Kinin forming enzymes; Kininogen

Indexed keywords

ALPHA 2 ANTIPLASMIN; ALPHA 2 MACROGLOBULIN; AMIDASE; ANTITHROMBIN III; BLOOD CLOTTING FACTOR 12; BRADYKININ; CHONDROITIN SULFATE; COMPLEMENT; COMPLEMENT COMPONENT C1S INHIBITOR; DEXTRAN SULFATE; GLYCOSAMINOGLYCAN; INFUSORIAL EARTH; KALLIKREIN; KAOLIN; KININ; KININOGEN; PLASMA KALLIKREIN; PREKALLIKREIN; PROTEINASE; SERINE PROTEINASE INHIBITOR; TISSUE KALLIKREIN; TRANEXAMIC ACID;

EID: 84886721308     PISSN: 08898561     EISSN: 15578607     Source Type: Journal    
DOI: 10.1016/j.iac.2013.07.007     Document Type: Review
Times cited : (9)

References (91)
  • 1
    • 0020614813 scopus 로고
    • Prekallikrein activation and high-molecular-weight kininogen consumption in hereditary angioedema
    • Schapira M., Silver L.D., Scott C.F., et al. Prekallikrein activation and high-molecular-weight kininogen consumption in hereditary angioedema. NEngl J Med 1983, 308:1050-1053.
    • (1983) NEngl J Med , vol.308 , pp. 1050-1053
    • Schapira, M.1    Silver, L.D.2    Scott, C.F.3
  • 2
    • 84874786526 scopus 로고    scopus 로고
    • Hereditary angioedema: a bradykinin-mediated swelling disorder
    • Björkqvist J., Sala-Cunill A., Renné T. Hereditary angioedema: a bradykinin-mediated swelling disorder. Thromb Haemost 2013, 109:368-374.
    • (2013) Thromb Haemost , vol.109 , pp. 368-374
    • Björkqvist, J.1    Sala-Cunill, A.2    Renné, T.3
  • 3
    • 25444504534 scopus 로고    scopus 로고
    • The kallikrein-kinin system: current and future pharmacological targets
    • Moreau M.E., Garbacki N., Molinaro G., et al. The kallikrein-kinin system: current and future pharmacological targets. JPharmacol Sci 2005, 99:6-38.
    • (2005) JPharmacol Sci , vol.99 , pp. 6-38
    • Moreau, M.E.1    Garbacki, N.2    Molinaro, G.3
  • 4
    • 34447128795 scopus 로고    scopus 로고
    • Nonallergic angioedema: role of bradykinin
    • Bas M., Adams V., Suvorava T., et al. Nonallergic angioedema: role of bradykinin. Allergy 2007, 62:842-856.
    • (2007) Allergy , vol.62 , pp. 842-856
    • Bas, M.1    Adams, V.2    Suvorava, T.3
  • 5
    • 84861735451 scopus 로고    scopus 로고
    • Plasma kallikrein: novel functions for an old protease
    • Renné T., Gruber A. Plasma kallikrein: novel functions for an old protease. Thromb Haemost 2012, 107:1012-1013.
    • (2012) Thromb Haemost , vol.107 , pp. 1012-1013
    • Renné, T.1    Gruber, A.2
  • 6
    • 0018821108 scopus 로고
    • Detection of active kallikrein in induced blister fluids of hereditary angioedema patients
    • Curd J.G., Prograis L.J., Cochrane C.G. Detection of active kallikrein in induced blister fluids of hereditary angioedema patients. JExp Med 1980, 152:742-747.
    • (1980) JExp Med , vol.152 , pp. 742-747
    • Curd, J.G.1    Prograis, L.J.2    Cochrane, C.G.3
  • 7
    • 60949104520 scopus 로고    scopus 로고
    • C1-inhibitor deficiency and angioedema: molecular mechanisms and clinical progress
    • Cugno M., Zanichelli A., Foieni F., et al. C1-inhibitor deficiency and angioedema: molecular mechanisms and clinical progress. Trends Mol Med 2009, 15:69-78.
    • (2009) Trends Mol Med , vol.15 , pp. 69-78
    • Cugno, M.1    Zanichelli, A.2    Foieni, F.3
  • 8
    • 80051740953 scopus 로고    scopus 로고
    • Consensus statement on the diagnosis, management, and treatment of angioedema mediated by bradykinin. Part I. Classification, epidemiology, pathophysiology, genetics, clinical symptoms, and diagnosis
    • [quiz: 347]
    • Caballero T., Baeza M.L., Cabañas R., et al. Consensus statement on the diagnosis, management, and treatment of angioedema mediated by bradykinin. Part I. Classification, epidemiology, pathophysiology, genetics, clinical symptoms, and diagnosis. JInvestig Allergol Clin Immunol 2011, 21:333-347. [quiz: 347].
    • (2011) JInvestig Allergol Clin Immunol , vol.21 , pp. 333-347
    • Caballero, T.1    Baeza, M.L.2    Cabañas, R.3
  • 9
    • 0035032184 scopus 로고    scopus 로고
    • Hereditary angioedema type III: an additional French pedigree with autosomal dominant transmission
    • Martin L., Degenne D., Toutain A., et al. Hereditary angioedema type III: an additional French pedigree with autosomal dominant transmission. JAllergy Clin Immunol 2001, 107:747-748.
    • (2001) JAllergy Clin Immunol , vol.107 , pp. 747-748
    • Martin, L.1    Degenne, D.2    Toutain, A.3
  • 10
    • 0034661804 scopus 로고    scopus 로고
    • Hereditary angioedema with normal C1-inhibitor activity in women
    • Bork K., Barnstedt S.E., Koch P., et al. Hereditary angioedema with normal C1-inhibitor activity in women. Lancet 2000, 356:213-217.
    • (2000) Lancet , vol.356 , pp. 213-217
    • Bork, K.1    Barnstedt, S.E.2    Koch, P.3
  • 11
    • 0034508657 scopus 로고    scopus 로고
    • Clinical, biochemical, and genetic characterization of anovel estrogen-dependent inherited form of angioedema
    • Binkley K.E., Davis A. Clinical, biochemical, and genetic characterization of anovel estrogen-dependent inherited form of angioedema. JAllergy Clin Immunol 2000, 106:546-550.
    • (2000) JAllergy Clin Immunol , vol.106 , pp. 546-550
    • Binkley, K.E.1    Davis, A.2
  • 12
    • 33845219794 scopus 로고    scopus 로고
    • Increased activity of coagulation factor XII (Hageman factor) causes hereditary angioedema type III
    • Cichon S., Martin L., Hennies H.C., et al. Increased activity of coagulation factor XII (Hageman factor) causes hereditary angioedema type III. Am J Hum Genet 2006, 79:1098-1104.
    • (2006) Am J Hum Genet , vol.79 , pp. 1098-1104
    • Cichon, S.1    Martin, L.2    Hennies, H.C.3
  • 13
    • 68349117147 scopus 로고    scopus 로고
    • Hereditary angioedema with normal C1 inhibition
    • Bork K. Hereditary angioedema with normal C1 inhibition. Curr Allergy Asthma Rep 2009, 9:280-285.
    • (2009) Curr Allergy Asthma Rep , vol.9 , pp. 280-285
    • Bork, K.1
  • 14
    • 34948849184 scopus 로고    scopus 로고
    • Hereditary angioedema with normal C1 inhibitor gene in a family with affected women and men is associated with the p.Thr328Lys mutation in the F12 gene
    • Martin L., Raison-Peyron N., Nöthen M.M., et al. Hereditary angioedema with normal C1 inhibitor gene in a family with affected women and men is associated with the p.Thr328Lys mutation in the F12 gene. JAllergy Clin Immunol 2007, 120:975-977.
    • (2007) JAllergy Clin Immunol , vol.120 , pp. 975-977
    • Martin, L.1    Raison-Peyron, N.2    Nöthen, M.M.3
  • 15
    • 84874984500 scopus 로고    scopus 로고
    • Hereditary angioedema with normal C1 inhibitor function: consensus of an international expert panel
    • Zuraw B.L., Bork K., Binkley K.E., et al. Hereditary angioedema with normal C1 inhibitor function: consensus of an international expert panel. Allergy Asthma Proc 2012, 33(Suppl 1):S145-S156.
    • (2012) Allergy Asthma Proc , vol.33 , Issue.SUPPL 1
    • Zuraw, B.L.1    Bork, K.2    Binkley, K.E.3
  • 16
    • 77956438524 scopus 로고    scopus 로고
    • Type III hereditary angio-oedema: clinical and biological features in a French cohort
    • Vitrat-Hincky V., Gompel A., Dumestre-Perard C., et al. Type III hereditary angio-oedema: clinical and biological features in a French cohort. Allergy 2010, 65:1331-1336.
    • (2010) Allergy , vol.65 , pp. 1331-1336
    • Vitrat-Hincky, V.1    Gompel, A.2    Dumestre-Perard, C.3
  • 17
    • 84881095783 scopus 로고    scopus 로고
    • Enzymatic assays for the biological diagnosis of bradykinin-dependent angioedema
    • Defendi F., Charignon D., Ghannam A., et al. Enzymatic assays for the biological diagnosis of bradykinin-dependent angioedema. PLoS One 2013, 8:e70140.
    • (2013) PLoS One , vol.8
    • Defendi, F.1    Charignon, D.2    Ghannam, A.3
  • 18
    • 35848964833 scopus 로고    scopus 로고
    • Contact activation (Kallikrein-Kinin) pathway: multiple physiologic and pathophysiologic activities
    • Lippincott Williams & Wilkins, Philadelphia, R.W. Colman, V.J. Marder, A.W. Clowes (Eds.)
    • Colman R.W. Contact activation (Kallikrein-Kinin) pathway: multiple physiologic and pathophysiologic activities. Hemostasis and thrombosis. Basic principles and clinical practice 2006, 109-113. Lippincott Williams & Wilkins, Philadelphia. R.W. Colman, V.J. Marder, A.W. Clowes (Eds.).
    • (2006) Hemostasis and thrombosis. Basic principles and clinical practice , pp. 109-113
    • Colman, R.W.1
  • 19
    • 0035085180 scopus 로고    scopus 로고
    • Factor XI assembly and activation on human umbilical vein endothelial cells in culture
    • Shariat-Madar Z., Mahdi F., Schmaier A.H. Factor XI assembly and activation on human umbilical vein endothelial cells in culture. Thromb Haemost 2001, 85:544-551.
    • (2001) Thromb Haemost , vol.85 , pp. 544-551
    • Shariat-Madar, Z.1    Mahdi, F.2    Schmaier, A.H.3
  • 20
    • 0022593032 scopus 로고
    • The contact activation system: biochemistry and interactions of these surface-mediated defense reactions
    • Colman R.W., Schmaier A.H. The contact activation system: biochemistry and interactions of these surface-mediated defense reactions. Crit Rev Oncol Hematol 1986, 5:57-85.
    • (1986) Crit Rev Oncol Hematol , vol.5 , pp. 57-85
    • Colman, R.W.1    Schmaier, A.H.2
  • 21
    • 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., et al. Structural dissection of the multidomain kininogens. Fine mapping of the target epitopes of antibodies interfering with their functional properties. JBiol Chem 1993, 268:9079-9091.
    • (1993) JBiol Chem , vol.268 , pp. 9079-9091
    • Kaufmann, J.1    Haasemann, M.2    Modrow, S.3
  • 22
    • 0026784525 scopus 로고
    • Domain 3 of kininogens contains a cell-binding site and a site that modifies thrombin activation of platelets
    • Jiang Y.P., Muller-Esterl W., Schmaier A.H. Domain 3 of kininogens contains a cell-binding site and a site that modifies thrombin activation of platelets. JBiol Chem 1992, 267:3712-3717.
    • (1992) JBiol Chem , vol.267 , pp. 3712-3717
    • Jiang, Y.P.1    Muller-Esterl, W.2    Schmaier, A.H.3
  • 23
    • 0034721787 scopus 로고    scopus 로고
    • High molecular weight kininogen utilizes heparan sulfate proteoglycans for accumulation on endothelial cells
    • Renné T., Dedio J., David G., et al. High molecular weight kininogen utilizes heparan sulfate proteoglycans for accumulation on endothelial cells. JBiol Chem 2000, 275:33688-33696.
    • (2000) JBiol Chem , vol.275 , pp. 33688-33696
    • Renné, T.1    Dedio, J.2    David, G.3
  • 24
    • 0033295653 scopus 로고    scopus 로고
    • Kininogen-cytokeratin 1 interactions in endothelial cell biology
    • Shariat-Madar Z., Schmaier A.H. Kininogen-cytokeratin 1 interactions in endothelial cell biology. Trends Cardiovasc Med 1999, 9:238-244.
    • (1999) Trends Cardiovasc Med , vol.9 , pp. 238-244
    • Shariat-Madar, Z.1    Schmaier, A.H.2
  • 25
    • 0023257512 scopus 로고
    • Primary structure requirements for the binding of human high molecular weight kininogen to plasma prekallikrein and factor XI
    • Tait J.F., Fujikawa K. Primary structure requirements for the binding of human high molecular weight kininogen to plasma prekallikrein and factor XI. JBiol Chem 1987, 262:11651-11656.
    • (1987) JBiol Chem , vol.262 , pp. 11651-11656
    • Tait, J.F.1    Fujikawa, K.2
  • 26
    • 0019165199 scopus 로고
    • The mechanism by which the light chain of cleaved HMW-kininogen augments the activation of prekallikrein, factor XI and Hageman factor
    • Silverberg M., Nicoll J.E., Kaplan A.P. The mechanism by which the light chain of cleaved HMW-kininogen augments the activation of prekallikrein, factor XI and Hageman factor. Thromb Res 1980, 20:173-189.
    • (1980) Thromb Res , vol.20 , pp. 173-189
    • Silverberg, M.1    Nicoll, J.E.2    Kaplan, A.P.3
  • 27
    • 0022340098 scopus 로고
    • Human kininogens of low and high molecular mass: quantification by radioimmunoassay and determination of reference values
    • Adam A., Albert A., Calay G., et al. Human kininogens of low and high molecular mass: quantification by radioimmunoassay and determination of reference values. Clin Chem 1985, 31:423-426.
    • (1985) Clin Chem , vol.31 , pp. 423-426
    • Adam, A.1    Albert, A.2    Calay, G.3
  • 28
    • 51349169451 scopus 로고    scopus 로고
    • The elusive physiologic role of Factor XII
    • Schmaier A.H. The elusive physiologic role of Factor XII. JClin Invest 2008, 118:3006-3009.
    • (2008) JClin Invest , vol.118 , pp. 3006-3009
    • Schmaier, A.H.1
  • 29
    • 0028827650 scopus 로고
    • Molecular basis of estrogen regulation of Hageman factor XII gene expression
    • Farsetti A., Misiti S., Citarella F., et al. Molecular basis of estrogen regulation of Hageman factor XII gene expression. Endocrinology 1995, 136:5076-5083.
    • (1995) Endocrinology , vol.136 , pp. 5076-5083
    • Farsetti, A.1    Misiti, S.2    Citarella, F.3
  • 30
    • 76949094364 scopus 로고    scopus 로고
    • Factor XII: what does it contribute to our understanding of the physiology and pathophysiology of hemostasis & thrombosis
    • Stavrou E., Schmaier A.H. Factor XII: what does it contribute to our understanding of the physiology and pathophysiology of hemostasis & thrombosis. Thromb Res 2010, 125:210-215.
    • (2010) Thromb Res , vol.125 , pp. 210-215
    • Stavrou, E.1    Schmaier, A.H.2
  • 31
    • 0026701990 scopus 로고
    • Human factor XII (Hageman factor) autoactivation by dextran sulfate. Circular dichroism, fluorescence, and ultraviolet difference spectroscopic studies
    • Samuel M., Pixley R.A., Villanueva M.A., et al. Human factor XII (Hageman factor) autoactivation by dextran sulfate. Circular dichroism, fluorescence, and ultraviolet difference spectroscopic studies. JBiol Chem 1992, 267:19691-19697.
    • (1992) JBiol Chem , vol.267 , pp. 19691-19697
    • Samuel, M.1    Pixley, R.A.2    Villanueva, M.A.3
  • 32
    • 0025891440 scopus 로고
    • Gene structure and chromosomal localization of plasma kallikrein
    • Beaubien G., Rosinski-Chupin I., Mattei M.G., et al. Gene structure and chromosomal localization of plasma kallikrein. Biochemistry 1991, 30:1628-1635.
    • (1991) Biochemistry , vol.30 , pp. 1628-1635
    • Beaubien, G.1    Rosinski-Chupin, I.2    Mattei, M.G.3
  • 33
    • 36349018844 scopus 로고    scopus 로고
    • The plasma kallikrein-kinin system: its evolution from contact activation
    • Schmaier A.H., McCrae K.R. The plasma kallikrein-kinin system: its evolution from contact activation. JThromb Haemost 2007, 5:2323-2329.
    • (2007) JThromb Haemost , vol.5 , pp. 2323-2329
    • Schmaier, A.H.1    McCrae, K.R.2
  • 34
    • 3042750282 scopus 로고    scopus 로고
    • The tissue kallikrein family of serine proteases: functional roles in human disease and potential as clinical biomarkers
    • Clements J.A., Willemsen N.M., Myers S.A., et al. The tissue kallikrein family of serine proteases: functional roles in human disease and potential as clinical biomarkers. Crit Rev Clin Lab Sci 2004, 41:265-312.
    • (2004) Crit Rev Clin Lab Sci , vol.41 , pp. 265-312
    • Clements, J.A.1    Willemsen, N.M.2    Myers, S.A.3
  • 35
    • 57649112534 scopus 로고    scopus 로고
    • Reflections on the tissue kallikrein and kallikrein-related peptidase family - from mice to men - what have we learnt in the last two decades?
    • Clements J.A. Reflections on the tissue kallikrein and kallikrein-related peptidase family - from mice to men - what have we learnt in the last two decades?. Biol Chem 2008, 389:1447-1454.
    • (2008) Biol Chem , vol.389 , pp. 1447-1454
    • Clements, J.A.1
  • 36
    • 0027048724 scopus 로고
    • Kallistatin: a novel human tissue kallikrein inhibitor. Purification, characterization, and reactive center sequence
    • Zhou G.X., Chao L., Chao J. Kallistatin: a novel human tissue kallikrein inhibitor. Purification, characterization, and reactive center sequence. JBiol Chem 1992, 267:25873-25880.
    • (1992) JBiol Chem , vol.267 , pp. 25873-25880
    • Zhou, G.X.1    Chao, L.2    Chao, J.3
  • 37
    • 77955484566 scopus 로고    scopus 로고
    • Kallistatin inhibits vascular inflammation by antagonizing tumor necrosis factor-alpha-induced nuclear factor kappaB activation
    • Yin H., Gao L., Shen Bo, et al. Kallistatin inhibits vascular inflammation by antagonizing tumor necrosis factor-alpha-induced nuclear factor kappaB activation. Hypertension 2010, 56:260-267.
    • (2010) Hypertension , vol.56 , pp. 260-267
    • Yin, H.1    Gao, L.2    Shen, B.3
  • 38
    • 0037124049 scopus 로고    scopus 로고
    • Identification and characterization of prolylcarboxypeptidase as an endothelial cell prekallikrein activator
    • Shariat-Madar Z., Mahdi F., Schmaier A.H. Identification and characterization of prolylcarboxypeptidase as an endothelial cell prekallikrein activator. JBiol Chem 2002, 277:17962-17969.
    • (2002) JBiol Chem , vol.277 , pp. 17962-17969
    • Shariat-Madar, Z.1    Mahdi, F.2    Schmaier, A.H.3
  • 39
    • 23844555133 scopus 로고    scopus 로고
    • Local bradykinin formation is controlled by glycosaminoglycans
    • Renné T., Schuh K., Müller-Esterl W. Local bradykinin formation is controlled by glycosaminoglycans. JImmunol 2005, 175:3377-3385.
    • (2005) JImmunol , vol.175 , pp. 3377-3385
    • Renné, T.1    Schuh, K.2    Müller-Esterl, W.3
  • 40
    • 0035060730 scopus 로고    scopus 로고
    • The region 1-11 of Alzheimer amyloid-beta is critical for activation of contact-kinin system
    • Bergamaschini L., Donarini C., Foddi C., et al. The region 1-11 of Alzheimer amyloid-beta is critical for activation of contact-kinin system. Neurobiol Aging 2001, 22:63-69.
    • (2001) Neurobiol Aging , vol.22 , pp. 63-69
    • Bergamaschini, L.1    Donarini, C.2    Foddi, C.3
  • 41
    • 0013853269 scopus 로고
    • Availability of platelet factor 3 and activation of factor XII in thrombasthenia
    • Castaldi P.A., Larrieu M.J., Caen J. Availability of platelet factor 3 and activation of factor XII in thrombasthenia. Nature 1965, 207:422-424.
    • (1965) Nature , vol.207 , pp. 422-424
    • Castaldi, P.A.1    Larrieu, M.J.2    Caen, J.3
  • 42
    • 32344441350 scopus 로고    scopus 로고
    • Platelets promote coagulation factor XII-mediated proteolytic cascade systems in plasma
    • Johne J., Blume C., Benz P.M., et al. Platelets promote coagulation factor XII-mediated proteolytic cascade systems in plasma. Biol Chem 2006, 387:173-178.
    • (2006) Biol Chem , vol.387 , pp. 173-178
    • Johne, J.1    Blume, C.2    Benz, P.M.3
  • 43
    • 71149116751 scopus 로고    scopus 로고
    • Platelet polyphosphates are proinflammatory and procoagulant mediators invivo
    • Müller F., Mutch N.J., Schenk W.A., et al. Platelet polyphosphates are proinflammatory and procoagulant mediators invivo. Cell 2009, 139:1143-1156.
    • (2009) Cell , vol.139 , pp. 1143-1156
    • Müller, F.1    Mutch, N.J.2    Schenk, W.A.3
  • 44
    • 0028589888 scopus 로고
    • Dextran sulfate activates contact system and mediates arterial hypotension via B2 kinin receptors
    • Siebeck M., Cheronis J.C., Fink E., et al. Dextran sulfate activates contact system and mediates arterial hypotension via B2 kinin receptors. JAppl Physiol 1994, 77:2675-2680.
    • (1994) JAppl Physiol , vol.77 , pp. 2675-2680
    • Siebeck, M.1    Cheronis, J.C.2    Fink, E.3
  • 45
    • 45149118311 scopus 로고    scopus 로고
    • Oversulfated chondroitin sulfate is a contaminant in heparin associated with adverse clinical events
    • Guerrini M., Beccati D., Shriver Z., et al. Oversulfated chondroitin sulfate is a contaminant in heparin associated with adverse clinical events. Nat Biotechnol 2008, 26:669-675.
    • (2008) Nat Biotechnol , vol.26 , pp. 669-675
    • Guerrini, M.1    Beccati, D.2    Shriver, Z.3
  • 46
    • 44849115945 scopus 로고    scopus 로고
    • Contaminated heparin associated with adverse clinical events and activation of the contact system
    • Kishimoto T.K., Viswanathan K., Ganguly T., et al. Contaminated heparin associated with adverse clinical events and activation of the contact system. NEngl J Med 2008, 358:2457-2467.
    • (2008) NEngl J Med , vol.358 , pp. 2457-2467
    • Kishimoto, T.K.1    Viswanathan, K.2    Ganguly, T.3
  • 47
    • 0021235057 scopus 로고
    • Invitro activation of the contact (Hageman factor) system of plasma by heparin and chondroitin sulfate E
    • Hojima Y., Cochrane C.G., Wiggins R.C., et al. Invitro activation of the contact (Hageman factor) system of plasma by heparin and chondroitin sulfate E. Blood 1984, 63:1453-1459.
    • (1984) Blood , vol.63 , pp. 1453-1459
    • Hojima, Y.1    Cochrane, C.G.2    Wiggins, R.C.3
  • 48
    • 0027394049 scopus 로고
    • Ramiprilat increases bradykinin outflow from isolated hearts of rat
    • Baumgarten C.R., Linz W., Kunkel G., et al. Ramiprilat increases bradykinin outflow from isolated hearts of rat. Br J Pharmacol 1993, 108:293-295.
    • (1993) Br J Pharmacol , vol.108 , pp. 293-295
    • Baumgarten, C.R.1    Linz, W.2    Kunkel, G.3
  • 49
    • 0028999506 scopus 로고
    • Effect of enalaprilat on bradykinin and des-Arg9-bradykinin release following reperfusion of the ischaemic rat heart
    • Lamontagne D., Nadeau R., Adam A. Effect of enalaprilat on bradykinin and des-Arg9-bradykinin release following reperfusion of the ischaemic rat heart. Br J Pharmacol 1995, 115:476-478.
    • (1995) Br J Pharmacol , vol.115 , pp. 476-478
    • Lamontagne, D.1    Nadeau, R.2    Adam, A.3
  • 50
    • 34249821061 scopus 로고    scopus 로고
    • Mice deficient for both kinin receptors are normotensive and protected from endotoxin-induced hypotension
    • Cayla C., Todiras M., Iliescu R., et al. Mice deficient for both kinin receptors are normotensive and protected from endotoxin-induced hypotension. FASEB J 2007, 21:1689-1698.
    • (2007) FASEB J , vol.21 , pp. 1689-1698
    • Cayla, C.1    Todiras, M.2    Iliescu, R.3
  • 51
    • 0035702413 scopus 로고    scopus 로고
    • The bradykinin response and early hypotension at the introduction of continuous renal replacement therapy in the intensive care unit
    • Stoves J., Goode N.P., Visvanathan R., et al. The bradykinin response and early hypotension at the introduction of continuous renal replacement therapy in the intensive care unit. Artif Organs 2001, 25:1009-1013.
    • (2001) Artif Organs , vol.25 , pp. 1009-1013
    • Stoves, J.1    Goode, N.P.2    Visvanathan, R.3
  • 52
    • 0037154220 scopus 로고    scopus 로고
    • Heat shock protein 90 catalyzes activation of the prekallikrein-kininogen complex in the absence of factor XII
    • Joseph K., Tholanikunnel B.G., Kaplan A.P. Heat shock protein 90 catalyzes activation of the prekallikrein-kininogen complex in the absence of factor XII. Proc Natl Acad Sci USA 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
  • 53
    • 0015256028 scopus 로고
    • Aprealbumin activator of prekallikrein. 3. Appearance of chemotactic activity for human neutrophils by the conversion of human prekallikrein to kallikrein
    • Kaplan A.P., Kay A.B., Austen K.F. Aprealbumin activator of prekallikrein. 3. Appearance of chemotactic activity for human neutrophils by the conversion of human prekallikrein to kallikrein. JExp Med 1972, 135:81-97.
    • (1972) JExp Med , vol.135 , pp. 81-97
    • Kaplan, A.P.1    Kay, A.B.2    Austen, K.F.3
  • 54
    • 0020040377 scopus 로고
    • Purified human plasma kallikrein aggregates human blood neutrophils
    • Schapira M., Despland E., Scott C.F., et al. Purified human plasma kallikrein aggregates human blood neutrophils. JClin Invest 1982, 69:1199-1202.
    • (1982) JClin Invest , vol.69 , pp. 1199-1202
    • Schapira, M.1    Despland, E.2    Scott, C.F.3
  • 55
    • 0021052373 scopus 로고
    • Human plasma kallikrein releases neutrophil elastase during blood coagulation
    • Wachtfogel Y.T., Kucich U., James H.L., et al. Human plasma kallikrein releases neutrophil elastase during blood coagulation. JClin Invest 1983, 72:1672-1677.
    • (1983) JClin Invest , vol.72 , pp. 1672-1677
    • Wachtfogel, Y.T.1    Kucich, U.2    James, H.L.3
  • 56
    • 0022545432 scopus 로고
    • Purified plasma factor XIIa aggregates human neutrophils and causes degranulation
    • Wachtfogel Y.T., Pixley R.A., Kucich U., et al. Purified plasma factor XIIa aggregates human neutrophils and causes degranulation. Blood 1986, 67:1731-1737.
    • (1986) Blood , vol.67 , pp. 1731-1737
    • Wachtfogel, Y.T.1    Pixley, R.A.2    Kucich, U.3
  • 57
    • 33751548241 scopus 로고    scopus 로고
    • Activation of kinin B1 receptors induces chemotaxis of human neutrophils
    • Ehrenfeld P., Millan C., Matus C.E., et al. Activation of kinin B1 receptors induces chemotaxis of human neutrophils. JLeukoc Biol 2006, 80:117-124.
    • (2006) JLeukoc Biol , vol.80 , pp. 117-124
    • Ehrenfeld, P.1    Millan, C.2    Matus, C.E.3
  • 58
    • 42449094278 scopus 로고    scopus 로고
    • Anovel inflammatory pathway involved in leukocyte recruitment: role for the kinin B1 receptor and the chemokine CXCL5
    • Duchene J., Lecomte F., Ahmed S., et al. Anovel inflammatory pathway involved in leukocyte recruitment: role for the kinin B1 receptor and the chemokine CXCL5. JImmunol 2007, 179:4849-4856.
    • (2007) JImmunol , vol.179 , pp. 4849-4856
    • Duchene, J.1    Lecomte, F.2    Ahmed, S.3
  • 59
    • 0027934793 scopus 로고
    • High molecular weight kininogen binds to Mac-1 on neutrophils by its heavy chain (domain 3) and its light chain (domain 5)
    • Wachtfogel Y.T., DeLa Cadena R.A., Kunapuli S.P., et al. High molecular weight kininogen binds to Mac-1 on neutrophils by its heavy chain (domain 3) and its light chain (domain 5). JBiol Chem 1994, 269:19307-19312.
    • (1994) JBiol Chem , vol.269 , pp. 19307-19312
    • Wachtfogel, Y.T.1    DeLa Cadena, R.A.2    Kunapuli, S.P.3
  • 60
    • 0026556434 scopus 로고
    • Bioregulation of kinins: kallikreins, kininogens, and kininases
    • Bhoola K.D., Figueroa C.D., Worthy K. Bioregulation of kinins: kallikreins, kininogens, and kininases. Pharmacol Rev 1992, 44:1-80.
    • (1992) Pharmacol Rev , vol.44 , pp. 1-80
    • Bhoola, K.D.1    Figueroa, C.D.2    Worthy, K.3
  • 61
    • 0029964503 scopus 로고    scopus 로고
    • Induction of vascular permeability enhancement by human tryptase: dependence on activation of prekallikrein and direct release of bradykinin from kininogens
    • Imamura T., Dubin A., Moore W., et al. Induction of vascular permeability enhancement by human tryptase: dependence on activation of prekallikrein and direct release of bradykinin from kininogens. Lab Invest 1996, 74:861-870.
    • (1996) Lab Invest , vol.74 , pp. 861-870
    • Imamura, T.1    Dubin, A.2    Moore, W.3
  • 63
    • 0033584324 scopus 로고    scopus 로고
    • Abnormal mast cells in mice deficient in a heparin-synthesizing enzyme
    • Forsberg E., Pejler G., Ringvall M., et al. Abnormal mast cells in mice deficient in a heparin-synthesizing enzyme. Nature 1999, 400:773-776.
    • (1999) Nature , vol.400 , pp. 773-776
    • Forsberg, E.1    Pejler, G.2    Ringvall, M.3
  • 64
    • 34247326977 scopus 로고    scopus 로고
    • Acase of hereditary angio-oedema type III presenting with C1-inhibitor cleavage and a missense mutation in the F12 gene
    • Bouillet L., Ponard D., Rousset H., et al. Acase of hereditary angio-oedema type III presenting with C1-inhibitor cleavage and a missense mutation in the F12 gene. Br J Dermatol 2007, 156:1063-1065.
    • (2007) Br J Dermatol , vol.156 , pp. 1063-1065
    • Bouillet, L.1    Ponard, D.2    Rousset, H.3
  • 65
    • 0028360198 scopus 로고
    • Activation of the contact system and fibrinolysis in autoimmune acquired angioedema: a rationale for prophylactic use of tranexamic acid
    • Cugno M., Cicardi M., Agostoni A. Activation of the contact system and fibrinolysis in autoimmune acquired angioedema: a rationale for prophylactic use of tranexamic acid. JAllergy Clin Immunol 1994, 93:870-876.
    • (1994) JAllergy Clin Immunol , vol.93 , pp. 870-876
    • Cugno, M.1    Cicardi, M.2    Agostoni, A.3
  • 66
    • 0018765162 scopus 로고
    • Factor XII-dependent fibrinolysis: a double function of plasma kallikrein and the occurrence of a previously undescribed factor XII- and kallikrein-dependent plasminogen proactivator
    • Kluft C., Trumpi-Kalshoven M.M., Jie A.F., et al. Factor XII-dependent fibrinolysis: a double function of plasma kallikrein and the occurrence of a previously undescribed factor XII- and kallikrein-dependent plasminogen proactivator. Thromb Haemost 1979, 41:756-773.
    • (1979) Thromb Haemost , vol.41 , pp. 756-773
    • Kluft, C.1    Trumpi-Kalshoven, M.M.2    Jie, A.F.3
  • 67
    • 0033048762 scopus 로고    scopus 로고
    • Bradykinin stimulates tissue plasminogen activator release in human vasculature
    • Brown N.J., Gainer J.V., Stein C.M., et al. Bradykinin stimulates tissue plasminogen activator release in human vasculature. Hypertension 1999, 33:1431-1435.
    • (1999) Hypertension , vol.33 , pp. 1431-1435
    • Brown, N.J.1    Gainer, J.V.2    Stein, C.M.3
  • 68
    • 0026749660 scopus 로고
    • Mechanism of enhanced kinin release from high molecular weight kininogen by plasma kallikrein after its exposure to plasmin
    • Kleniewski J., Blankenship D.T., Cardin A.D., et al. Mechanism of enhanced kinin release from high molecular weight kininogen by plasma kallikrein after its exposure to plasmin. JLab Clin Med 1992, 120:129-139.
    • (1992) JLab Clin Med , vol.120 , pp. 129-139
    • Kleniewski, J.1    Blankenship, D.T.2    Cardin, A.D.3
  • 69
    • 77951906428 scopus 로고    scopus 로고
    • Efficacy of tranexamic acid in sporadic idiopathic bradykinin angioedema
    • Du-Thanh A., Raison-Peyron N., Drouet C., et al. Efficacy of tranexamic acid in sporadic idiopathic bradykinin angioedema. Allergy 2010, 65:793-795.
    • (2010) Allergy , vol.65 , pp. 793-795
    • Du-Thanh, A.1    Raison-Peyron, N.2    Drouet, C.3
  • 70
    • 0019471542 scopus 로고
    • Activation of the classical pathway of complement by Hageman factor fragment
    • Ghebrehiwet B., Silverberg M., Kaplan A.P. Activation of the classical pathway of complement by Hageman factor fragment. JExp Med 1981, 153:665-676.
    • (1981) JExp Med , vol.153 , pp. 665-676
    • Ghebrehiwet, B.1    Silverberg, M.2    Kaplan, A.P.3
  • 71
    • 0020529790 scopus 로고
    • Mechanisms of activation of the classical pathway of complement by Hageman factor fragment
    • Ghebrehiwet B., Randazzo B.P., Dunn J.T., et al. Mechanisms of activation of the classical pathway of complement by Hageman factor fragment. JClin Invest 1983, 71:1450-1456.
    • (1983) JClin Invest , vol.71 , pp. 1450-1456
    • Ghebrehiwet, B.1    Randazzo, B.P.2    Dunn, J.T.3
  • 72
    • 0020047810 scopus 로고
    • The activation of the alternative pathway C3 convertase by human plasma kallikrein
    • Discipio R.G. The activation of the alternative pathway C3 convertase by human plasma kallikrein. Immunology 1982, 45:587-595.
    • (1982) Immunology , vol.45 , pp. 587-595
    • Discipio, R.G.1
  • 73
    • 0019440292 scopus 로고
    • Chemotactic activity generated from the fifth component of complement by plasma kallikrein of the rabbit
    • Wiggins R.C., Giclas P.C., Henson P.M. Chemotactic activity generated from the fifth component of complement by plasma kallikrein of the rabbit. JExp Med 1981, 153:1391-1404.
    • (1981) JExp Med , vol.153 , pp. 1391-1404
    • Wiggins, R.C.1    Giclas, P.C.2    Henson, P.M.3
  • 74
    • 0037100538 scopus 로고    scopus 로고
    • C5a stimulates production of plasminogen activator inhibitor-1 in human mast cells and basophils
    • Wojta J., Kaun C., Zorn G., et al. C5a stimulates production of plasminogen activator inhibitor-1 in human mast cells and basophils. Blood 2002, 100:517-523.
    • (2002) Blood , vol.100 , pp. 517-523
    • Wojta, J.1    Kaun, C.2    Zorn, G.3
  • 75
    • 10644286657 scopus 로고    scopus 로고
    • The pathophysiology of hereditary angioedema
    • Davis A.E. The pathophysiology of hereditary angioedema. Clin Immunol 2005, 114:3-9.
    • (2005) Clin Immunol , vol.114 , pp. 3-9
    • Davis, A.E.1
  • 76
    • 9144246217 scopus 로고    scopus 로고
    • Platelet-activating factor and kinin-dependent vascular leakage as a novel functional activity of the soluble terminal complement complex
    • Bossi F., Fischetti F., Pellis V., et al. Platelet-activating factor and kinin-dependent vascular leakage as a novel functional activity of the soluble terminal complement complex. JImmunol 2004, 173:6921-6927.
    • (2004) JImmunol , vol.173 , pp. 6921-6927
    • Bossi, F.1    Fischetti, F.2    Pellis, V.3
  • 77
    • 0032823979 scopus 로고    scopus 로고
    • Cytokeratin 1 and gC1qR mediate high molecular weight kininogen binding to endothelial cells
    • Joseph K., Ghebrehiwet B., Kaplan A.P. Cytokeratin 1 and gC1qR mediate high molecular weight kininogen binding to endothelial cells. Clin Immunol 1999, 92:246-255.
    • (1999) Clin Immunol , vol.92 , pp. 246-255
    • Joseph, K.1    Ghebrehiwet, B.2    Kaplan, A.P.3
  • 78
    • 0033045040 scopus 로고    scopus 로고
    • Idiopathic nonhistaminergic angioedema
    • Cicardi M., Bergamaschini L., Zingale L.C., et al. Idiopathic nonhistaminergic angioedema. Am J Med 1999, 106:650-654.
    • (1999) Am J Med , vol.106 , pp. 650-654
    • Cicardi, M.1    Bergamaschini, L.2    Zingale, L.C.3
  • 79
    • 0034067425 scopus 로고    scopus 로고
    • Asphyxiation by laryngeal edema in patients with hereditary angioedema
    • Bork K., Siedlecki K., Bosch S., et al. Asphyxiation by laryngeal edema in patients with hereditary angioedema. Mayo Clin Proc 2000, 75:349-354.
    • (2000) Mayo Clin Proc , vol.75 , pp. 349-354
    • Bork, K.1    Siedlecki, K.2    Bosch, S.3
  • 80
    • 33646026697 scopus 로고    scopus 로고
    • Missense mutations in the coagulation factor XII (Hageman factor) gene in hereditary angioedema with normal C1 inhibitor
    • Dewald G., Bork K. Missense mutations in the coagulation factor XII (Hageman factor) gene in hereditary angioedema with normal C1 inhibitor. Biochem Biophys Res Commun 2006, 343:1286-1289.
    • (2006) Biochem Biophys Res Commun , vol.343 , pp. 1286-1289
    • Dewald, G.1    Bork, K.2
  • 81
    • 63649128831 scopus 로고    scopus 로고
    • Genetic analysis of Factor XII and bradykinin catabolic enzymes in a family with estrogen-dependent inherited angioedema
    • Duan Q.L., Binkley K., Rouleau G.A. Genetic analysis of Factor XII and bradykinin catabolic enzymes in a family with estrogen-dependent inherited angioedema. JAllergy Clin Immunol 2009, 123:906-910.
    • (2009) JAllergy Clin Immunol , vol.123 , pp. 906-910
    • Duan, Q.L.1    Binkley, K.2    Rouleau, G.A.3
  • 82
    • 84886721303 scopus 로고    scopus 로고
    • Hereditary angioedema caused by the Thr309Lys mutation in the F12 gene: a multifactorial disease. J Allergy Clin Immunol, in press.
    • Gómez-Traseira C, López-Lera A, Drouet C, etal. Hereditary angioedema caused by the p.Thr309Lys mutation in the F12 gene: a multifactorial disease. J Allergy Clin Immunol, in press.
    • Gómez-Traseira, C.1    López-Lera, A.2    Drouet, C.3
  • 83
    • 58149199899 scopus 로고    scopus 로고
    • Angioedema and estrogen-dependent angioedema with activation of the contact system
    • Hentges F., Hilger C., Kohnen M., et al. Angioedema and estrogen-dependent angioedema with activation of the contact system. JAllergy Clin Immunol 2009, 123:262-264.
    • (2009) JAllergy Clin Immunol , vol.123 , pp. 262-264
    • Hentges, F.1    Hilger, C.2    Kohnen, M.3
  • 84
    • 84886724653 scopus 로고    scopus 로고
    • Diagnostic et traitement de l'angioedème. EP1153239 (2011).
    • Ghannam A, Luyasu S, Drouet C. Diagnostic et traitement de l'angioedème. EP1153239 (2011).
    • Ghannam, A.1    Luyasu, S.2    Drouet, C.3
  • 85
    • 0014497034 scopus 로고
    • Permeability-increasing activity in hereditary angioneurotic edema plasma. II. Mechanism of formation and partial characterization
    • Donaldson V.H., Ratnoff O.D., Dias Da Silva W., et al. Permeability-increasing activity in hereditary angioneurotic edema plasma. II. Mechanism of formation and partial characterization. JClin Invest 1969, 48:642-653.
    • (1969) JClin Invest , vol.48 , pp. 642-653
    • Donaldson, V.H.1    Ratnoff, O.D.2    Dias Da Silva, W.3
  • 86
    • 84879554727 scopus 로고    scopus 로고
    • Oestrogen-independent hereditary angioedema with normal C1 inhibitor function in a 10-year-old boy
    • Bergmann M.M., Caubet J.C., Defendi F., et al. Oestrogen-independent hereditary angioedema with normal C1 inhibitor function in a 10-year-old boy. Ann Allergy Asthma Immunol 2013, 11:67-69.
    • (2013) Ann Allergy Asthma Immunol , vol.11 , pp. 67-69
    • Bergmann, M.M.1    Caubet, J.C.2    Defendi, F.3
  • 87
    • 79961021066 scopus 로고    scopus 로고
    • One hypovolaemic shock... two kinin pathway abnormalities
    • Guichon C., Floccard B., Coppéré B., et al. One hypovolaemic shock... two kinin pathway abnormalities. Intensive Care Med 2011, 37:1227-1228.
    • (2011) Intensive Care Med , vol.37 , pp. 1227-1228
    • Guichon, C.1    Floccard, B.2    Coppéré, B.3
  • 88
    • 84867741227 scopus 로고    scopus 로고
    • Angio-oedema induced by oestrogen contraceptives is mediated by bradykinin and is frequently associated with urticaria
    • Giard C., Nicolie B., Drouet M., et al. Angio-oedema induced by oestrogen contraceptives is mediated by bradykinin and is frequently associated with urticaria. Dermatology 2012, 225:62-69.
    • (2012) Dermatology , vol.225 , pp. 62-69
    • Giard, C.1    Nicolie, B.2    Drouet, M.3
  • 89
    • 38449094810 scopus 로고    scopus 로고
    • Disentangling genetic variation for resistance and tolerance to infectious diseases in animals
    • Råberg L., Sim D., Read A.F. Disentangling genetic variation for resistance and tolerance to infectious diseases in animals. Science 2007, 318:812-814.
    • (2007) Science , vol.318 , pp. 812-814
    • Råberg, L.1    Sim, D.2    Read, A.F.3
  • 91
    • 0003338119 scopus 로고
    • Extracellular protein modules: a proposed nomenclature
    • Bork P., Bairoch A. Extracellular protein modules: a proposed nomenclature. Trends Biochem Sci 1995, 20.
    • (1995) Trends Biochem Sci , vol.20
    • Bork, P.1    Bairoch, A.2


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