메뉴 건너뛰기




Volumn 125, Issue 8, 2015, Pages 3132-3146

Defective glycosylation of coagulation factor XII underlies hereditary angioedema type III

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CLOTTING FACTOR 12; BRADYKININ; COMPLEMENT COMPONENT C1S INHIBITOR; ENZYME PRECURSOR; KALLIKREIN; KININ; NEUTRALIZING ANTIBODY;

EID: 84939227812     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI77139     Document Type: Article
Times cited : (138)

References (72)
  • 1
    • 50949089029 scopus 로고    scopus 로고
    • Clinical practice. Hereditary angioedema
    • Zuraw BL. Clinical practice. Hereditary angioedema. N Engl J Med. 2008;359(10):1027-1036.
    • (2008) N Engl J Med. , vol.359 , Issue.10 , pp. 1027-1036
    • Zuraw, B.L.1
  • 2
    • 51649127755 scopus 로고    scopus 로고
    • Studies of the mechanisms of bradykinin generation in hereditary angioedema plasma
    • Joseph K, Tuscano TB, Kaplan AP. Studies of the mechanisms of bradykinin generation in hereditary angioedema plasma. Ann Allergy Asthma Immunol. 2008;101(3):279-286.
    • (2008) Ann Allergy Asthma Immunol. , vol.101 , Issue.3 , pp. 279-286
    • Joseph, K.1    Tuscano, T.B.2    Kaplan, A.P.3
  • 4
    • 0020614813 scopus 로고
    • Prekallikrein activation and high-molecular-weight kininogen consumption in hereditary angioedema
    • Schapira M, et al. Prekallikrein activation and high-molecular-weight kininogen consumption in hereditary angioedema. N Engl J Med. 1983;308(18):1050-1053.
    • (1983) N Engl J Med. , vol.308 , Issue.18 , pp. 1050-1053
    • Schapira, M.1
  • 6
    • 14144251086 scopus 로고    scopus 로고
    • International union of pharmacology. XLV. Classification of the kinin receptor family: From molecular mechanisms to pathophysiological consequences
    • Leeb-Lundberg LM, Marceau F, Muller-Esterl W, Pettibone DJ, Zuraw BL. International union of pharmacology. XLV. Classification of the kinin receptor family: from molecular mechanisms to pathophysiological consequences. Pharmacol Rev. 2005;57(1):27-77.
    • (2005) Pharmacol Rev. , vol.57 , Issue.1 , pp. 27-77
    • Leeb-Lundberg, L.M.1    Marceau, F.2    Muller-Esterl, W.3    Pettibone, D.J.4    Zuraw, B.L.5
  • 7
    • 84874786526 scopus 로고    scopus 로고
    • Hereditary angioedema: A bradykinin-mediated swelling disorder
    • Bjorkqvist J, Sala-Cunill A, Renne T. Hereditary angioedema: a bradykinin-mediated swelling disorder. Thromb Haemost. 2013;109(3):368-374.
    • (2013) Thromb Haemost. , vol.109 , Issue.3 , pp. 368-374
    • Bjorkqvist, J.1    Sala-Cunill, A.2    Renne, T.3
  • 8
    • 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, Scafidi J, Davis AE 3rd. Increased vascular permeability in C1 inhibitor-deficient mice mediated by the bradykinin type 2 receptor. J Clin Invest. 2002;109(8):1057-1063.
    • (2002) J Clin Invest. , vol.109 , Issue.8 , pp. 1057-1063
    • Han, E.D.1    MacFarlane, R.C.2    Mulligan, A.N.3    Scafidi, J.4    Davis, A.E.5
  • 9
    • 77955299623 scopus 로고    scopus 로고
    • Nanofiltered C1 inhibitor concentrate for treatment of hereditary angioedema
    • Zuraw BL, et al. Nanofiltered C1 inhibitor concentrate for treatment of hereditary angioedema. N Engl J Med. 2010;363(6):513-522.
    • (2010) N Engl J Med. , vol.363 , Issue.6 , pp. 513-522
    • Zuraw, B.L.1
  • 10
    • 77955295556 scopus 로고    scopus 로고
    • Icatibant, a new bradykinin-receptor antagonist, in hereditary angioedema
    • Cicardi M, et al. Icatibant, a new bradykinin-receptor antagonist, in hereditary angioedema. N Engl J Med. 2010;363(6):532-541.
    • (2010) N Engl J Med. , vol.363 , Issue.6 , pp. 532-541
    • Cicardi, M.1
  • 11
    • 77955296289 scopus 로고    scopus 로고
    • Ecallantide for the treatment of acute attacks in hereditary angioedema
    • Cicardi M, et al. Ecallantide for the treatment of acute attacks in hereditary angioedema. N Engl J Med. 2010;363(6):523-531.
    • (2010) N Engl J Med. , vol.363 , Issue.6 , pp. 523-531
    • Cicardi, M.1
  • 12
    • 0034661804 scopus 로고    scopus 로고
    • Hereditary angioedema with normal C1-inhibitor activity in women
    • Bork K, Barnstedt SE, Koch P, Traupe H. Hereditary angioedema with normal C1-inhibitor activity in women. Lancet. 2000;356(9225):213-217.
    • (2000) Lancet. , vol.356 , Issue.9225 , pp. 213-217
    • Bork, K.1    Barnstedt, S.E.2    Koch, P.3    Traupe, H.4
  • 13
    • 33845219794 scopus 로고    scopus 로고
    • Increased activity of coagulation factor XII (Hageman factor) causes hereditary angioedema type III
    • Cichon S, et al. Increased activity of coagulation factor XII (Hageman factor) causes hereditary angioedema type III. Am J Hum Genet. 2006;79(6):1098-1104.
    • (2006) Am J Hum Genet. , vol.79 , Issue.6 , pp. 1098-1104
    • Cichon, S.1
  • 14
    • 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(4):1286-1289.
    • (2006) Biochem Biophys Res Commun. , vol.343 , Issue.4 , pp. 1286-1289
    • Dewald, G.1    Bork, K.2
  • 15
    • 84874984500 scopus 로고    scopus 로고
    • Hereditary angioedema with normal C1 inhibitor function: Consensus of an international expert panel
    • Zuraw BL, 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 , pp. S145-S156
    • Zuraw, B.L.1
  • 16
    • 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
    • Citarella 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. 1996;238(1):240-249.
    • (1996) Eur J Biochem. , vol.238 , Issue.1 , pp. 240-249
    • Citarella, F.1    Ravon, D.M.2    Pascucci, B.3    Felici, A.4    Fantoni, A.5    Hack, C.E.6
  • 17
    • 0021859293 scopus 로고
    • Amino acid sequence of the heavy chain of human alpha-factor XIIa (activated Hageman factor)
    • McMullen BA, Fujikawa K. Amino acid sequence of the heavy chain of human alpha-factor XIIa (activated Hageman factor). J Biol Chem. 1985;260(9):5328-5341.
    • (1985) J Biol Chem. , vol.260 , Issue.9 , pp. 5328-5341
    • McMullen, B.A.1    Fujikawa, K.2
  • 18
    • 84881534476 scopus 로고    scopus 로고
    • Zinc-dependent contact system activation induces vascular leakage and hypotension in rodents
    • Björkqvist J, Lecher B, Maas C, Renné T. Zinc-dependent contact system activation induces vascular leakage and hypotension in rodents. Biol Chem. 2013;394(9):1195-1204.
    • (2013) Biol Chem. , vol.394 , Issue.9 , pp. 1195-1204
    • Björkqvist, J.1    Lecher, B.2    Maas, C.3    Renné, T.4
  • 19
    • 84881137902 scopus 로고    scopus 로고
    • Factor XII-independent activation of the bradykinin-forming cascade: Implications for the pathogenesis of hereditary angioedema types I and II
    • Joseph K, Tholanikunnel BG, Bygum A, Ghebrehiwet B, Kaplan AP. Factor XII-independent activation of the bradykinin-forming cascade: Implications for the pathogenesis of hereditary angioedema types I and II. J Allergy Clin Immunol. 2013;132(2):470-475.
    • (2013) J Allergy Clin Immunol. , vol.132 , Issue.2 , pp. 470-475
    • Joseph, K.1    Tholanikunnel, B.G.2    Bygum, A.3    Ghebrehiwet, B.4    Kaplan, A.P.5
  • 20
    • 84881527790 scopus 로고    scopus 로고
    • A nanobody-based method for tracking factor XII activation in plasma
    • de Maat S, van Dooremalen S, de Groot PG, Maas C. A nanobody-based method for tracking factor XII activation in plasma. Thromb Haemost. 2013;110(3):458-468.
    • (2013) Thromb Haemost. , vol.110 , Issue.3 , pp. 458-468
    • De Maat, S.1    Van Dooremalen, S.2    De Groot, P.G.3    Maas, C.4
  • 21
    • 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(1):111-118.
    • (2003) Eur J Biochem. , vol.270 , Issue.1 , pp. 111-118
    • Schousboe, I.1
  • 22
    • 0027467583 scopus 로고
    • Inhibition of plasma kallikrein with aprotinin in porcine endotoxin shock
    • Siebeck M, et al. Inhibition of plasma kallikrein with aprotinin in porcine endotoxin shock. J Trauma. 1993;34(2):193-198.
    • (1993) J Trauma. , vol.34 , Issue.2 , pp. 193-198
    • Siebeck, M.1
  • 23
    • 84893834884 scopus 로고    scopus 로고
    • A factor XIIa inhibitory antibody provides thromboprotection in extracorporeal circulation without increasing bleeding risk
    • Larsson M, et al. A factor XIIa inhibitory antibody provides thromboprotection in extracorporeal circulation without increasing bleeding risk. Sci Transl Med. 2014;6(222):222ra17.
    • (2014) Sci Transl Med , vol.6 , Issue.222
    • Larsson, M.1
  • 24
    • 79951741353 scopus 로고    scopus 로고
    • Mast cells increase vascular permeability by heparin-initiated bradykinin formation in vivo
    • Oschatz C, et al. Mast cells increase vascular permeability by heparin-initiated bradykinin formation in vivo. Immunity. 2011;34(2):258-268.
    • (2011) Immunity. , vol.34 , Issue.2 , pp. 258-268
    • Oschatz, C.1
  • 25
    • 0029763587 scopus 로고    scopus 로고
    • Doxycycline-mediated quantitative and tissue-specific control of gene expression in transgenic mice
    • Kistner A, et al. Doxycycline-mediated quantitative and tissue-specific control of gene expression in transgenic mice. Proc Natl Acad Sci U S A. 1996;93(20):10933-10938.
    • (1996) Proc Natl Acad Sci U S A. , vol.93 , Issue.20 , pp. 10933-10938
    • Kistner, A.1
  • 26
    • 22944462705 scopus 로고    scopus 로고
    • Defective thrombus formation in mice lacking coagulation factor XII
    • Renne T, et al. Defective thrombus formation in mice lacking coagulation factor XII. J Exp Med. 2005;202(2):271-281.
    • (2005) J Exp Med. , vol.202 , Issue.2 , pp. 271-281
    • Renne, T.1
  • 27
    • 84940142489 scopus 로고
    • Vascular reactions to histamine, histamine-liberator and leukotaxine in the skin of guinea-pigs
    • Miles AA, Miles EM. Vascular reactions to histamine, histamine-liberator and leukotaxine in the skin of guinea-pigs. J Physiol. 1952;118(2):228-257.
    • (1952) J Physiol. , vol.118 , Issue.2 , pp. 228-257
    • Miles, A.A.1    Miles, E.M.2
  • 28
    • 67649224409 scopus 로고    scopus 로고
    • Kallikreinkinin system and fibrinolysis in hereditary angioedema due to factor XII gene mutation Thr309Lys
    • Bork K, Kleist R, Hardt J, Witzke G. Kallikreinkinin system and fibrinolysis in hereditary angioedema due to factor XII gene mutation Thr309Lys. Blood Coagul Fibrinolysis. 2009;20(5):325-332.
    • (2009) Blood Coagul Fibrinolysis. , vol.20 , Issue.5 , pp. 325-332
    • Bork, K.1    Kleist, R.2    Hardt, J.3    Witzke, G.4
  • 29
    • 84926205053 scopus 로고    scopus 로고
    • Plasma contact system activation drives anaphylaxis in severe mast cell-mediated allergic reactions
    • Sala-Cunill A, et al. Plasma contact system activation drives anaphylaxis in severe mast cell-mediated allergic reactions. J Allergy Clin Immunol. 2015;135(4):1031-1043.
    • (2015) J Allergy Clin Immunol. , vol.135 , Issue.4 , pp. 1031-1043
    • Sala-Cunill, A.1
  • 30
    • 50549190821 scopus 로고
    • A Biochemical Abnormality in Herediatry Angioneurotic Edema: Absence of Serum Inhibitor of C' 1-Esterase
    • Donaldson VH, Evans RR. A Biochemical Abnormality in Herediatry Angioneurotic Edema: Absence of Serum Inhibitor of C' 1-Esterase. Am J Med. 1963;35:37-44.
    • (1963) Am J Med. , vol.35 , pp. 37-44
    • Donaldson, V.H.1    Evans, R.R.2
  • 31
    • 84856654320 scopus 로고    scopus 로고
    • Hereditary angio-oedema
    • Longhurst H, Cicardi M. Hereditary angio-oedema. Lancet. 2012;379(9814):474-481.
    • (2012) Lancet. , vol.379 , Issue.9814 , pp. 474-481
    • Longhurst, H.1    Cicardi, M.2
  • 33
    • 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, Nothen MM, Cichon S, Drouet C. 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. J Allergy Clin Immunol. 2007;120(4):975-977.
    • (2007) J Allergy Clin Immunol. , vol.120 , Issue.4 , pp. 975-977
    • Martin, L.1    Raison-Peyron, N.2    Nothen, M.M.3    Cichon, S.4    Drouet, C.5
  • 34
    • 84908497917 scopus 로고    scopus 로고
    • Structural and molecular changes caused by mutations Thr328Lys and Thr328Arg in FXII associated with hereditary angioedema with normal C1 inhibitor
    • Moreno AS, Arcuri H, Palma M, Arruda LKP. Structural and molecular changes caused by mutations Thr328Lys and Thr328Arg in FXII associated with hereditary angioedema with normal C1 inhibitor. J Allergy Clin Immunol. 2014;133(2):39.
    • (2014) J Allergy Clin Immunol. , vol.133 , Issue.2 , pp. 39
    • Moreno, A.S.1    Arcuri, H.2    Palma, M.3    Arruda, L.K.P.4
  • 35
    • 0021997366 scopus 로고
    • Assessment of Hageman factor activation in human plasma: Quantification of activated Hageman factor-C1 inactivator complexes by an enzyme-linked differential antibody immunosorbent assay
    • Kaplan AP, Gruber B, Harpel PC. Assessment of Hageman factor activation in human plasma: quantification of activated Hageman factor-C1 inactivator complexes by an enzyme-linked differential antibody immunosorbent assay. Blood. 1985;66(3):636-641.
    • (1985) Blood. , vol.66 , Issue.3 , pp. 636-641
    • Kaplan, A.P.1    Gruber, B.2    Harpel, P.C.3
  • 36
    • 67649227073 scopus 로고    scopus 로고
    • Hereditary angioedema caused by missense mutations in the factor XII gene: Clinical features, trigger factors, and therapy
    • Bork K, Wulff K, Hardt J, Witzke G, Staubach P. Hereditary angioedema caused by missense mutations in the factor XII gene: clinical features, trigger factors, and therapy. J Allergy Clin Immunol. 2009;124(1):129-134.
    • (2009) J Allergy Clin Immunol. , vol.124 , Issue.1 , pp. 129-134
    • Bork, K.1    Wulff, K.2    Hardt, J.3    Witzke, G.4    Staubach, P.5
  • 37
    • 84926123023 scopus 로고    scopus 로고
    • Coagulation factor XII protease domain crystal structure
    • Pathak M, et al. Coagulation factor XII protease domain crystal structure. J Thromb Haemost. 2015;13(4):580-591.
    • (2015) J Thromb Haemost. , vol.13 , Issue.4 , pp. 580-591
    • Pathak, M.1
  • 38
    • 0030175373 scopus 로고    scopus 로고
    • Activation of factor XII and cleavage of high molecular weight kininogen during acute attacks in hereditary and acquired C1-inhibitor deficiencies
    • Cugno M, Cicardi M, Coppola R, Agostoni A. Activation of factor XII and cleavage of high molecular weight kininogen during acute attacks in hereditary and acquired C1-inhibitor deficiencies. Immunopharmacol. 1996;33(1-3):361-364.
    • (1996) Immunopharmacol. , vol.33 , Issue.1-3 , pp. 361-364
    • Cugno, M.1    Cicardi, M.2    Coppola, R.3    Agostoni, A.4
  • 40
    • 84911374174 scopus 로고    scopus 로고
    • High-molecular-weight kininogen cleavage correlates with disease states in the bradykinin-mediated angioedema due to hereditary C1-inhibitor deficiency
    • Suffritti C, Zanichelli A, Maggioni L, Bonanni E, Cugno M, Cicardi M. High-molecular-weight kininogen cleavage correlates with disease states in the bradykinin-mediated angioedema due to hereditary C1-inhibitor deficiency. Clin Exp Allergy. 2014;44(12):1503-1514.
    • (2014) Clin Exp Allergy. , vol.44 , Issue.12 , pp. 1503-1514
    • Suffritti, C.1    Zanichelli, A.2    Maggioni, L.3    Bonanni, E.4    Cugno, M.5    Cicardi, M.6
  • 41
    • 84921467982 scopus 로고    scopus 로고
    • -/- mice is mediated by increased Mas receptor, prostacyclin, Sirt1, and KLF4 and decreased tissue factor
    • -/- mice is mediated by increased Mas receptor, prostacyclin, Sirt1, and KLF4 and decreased tissue factor. Blood. 2015;125(4):710-719.
    • (2015) Blood. , vol.125 , Issue.4 , pp. 710-719
    • Stavrou, E.X.1
  • 42
    • 38949099750 scopus 로고    scopus 로고
    • Deletion of murine kininogen gene 1 (mKng1) causes loss of plasma kininogen and delays thrombosis
    • Merkulov S, et al. Deletion of murine kininogen gene 1 (mKng1) causes loss of plasma kininogen and delays thrombosis. Blood. 2008;111(3):1274-1281.
    • (2008) Blood. , vol.111 , Issue.3 , pp. 1274-1281
    • Merkulov, S.1
  • 43
    • 33745320535 scopus 로고    scopus 로고
    • Plasma levels of bradykinin are suppressed in factor XII-deficient mice
    • Iwaki T, Castellino FJ. Plasma levels of bradykinin are suppressed in factor XII-deficient mice. Thromb Haemost. 2006;95(6):1003-1010.
    • (2006) Thromb Haemost. , vol.95 , Issue.6 , pp. 1003-1010
    • Iwaki, T.1    Castellino, F.J.2
  • 44
    • 41549140461 scopus 로고    scopus 로고
    • Cleavage of high-molecular-weight kininogen by elastase and tryptase is inhibited by ferritin
    • Coffman LG, et al. Cleavage of high-molecular-weight kininogen by elastase and tryptase is inhibited by ferritin. Am J Physiol Lung Cell Mol Physiol. 2008;294(3):L505-L515.
    • (2008) Am J Physiol Lung Cell Mol Physiol. , vol.294 , Issue.3 , pp. L505-L515
    • Coffman, L.G.1
  • 45
    • 67649218762 scopus 로고    scopus 로고
    • Factor XII-independent cleavage of high-molecular-weight kininogen by prekallikrein and inhibition by C1 inhibitor
    • Joseph K, Tholanikunnel BG, Kaplan AP. Factor XII-independent cleavage of high-molecular-weight kininogen by prekallikrein and inhibition by C1 inhibitor. J Allergy Clin Immunol. 2009;124(1):143-149.
    • (2009) J Allergy Clin Immunol. , vol.124 , Issue.1 , pp. 143-149
    • Joseph, K.1    Tholanikunnel, B.G.2    Kaplan, A.P.3
  • 46
    • 0029978763 scopus 로고    scopus 로고
    • Selective kallikrein-kinin system activation in inbred rats differentially susceptible to granulomatous enterocolitis
    • Sartor RB, et al. Selective kallikrein-kinin system activation in inbred rats differentially susceptible to granulomatous enterocolitis. Gastroenterology. 1996;110(5):1467-1481.
    • (1996) Gastroenterology. , vol.110 , Issue.5 , pp. 1467-1481
    • Sartor, R.B.1
  • 47
    • 0035076062 scopus 로고    scopus 로고
    • Bradykinin receptor antagonists type 2 attenuate the inflammatory changes in peptidoglycan-induced acute arthritis in the Lewis rat
    • Uknis AB, DeLa Cadena RA, Janardham R, Sartor RB, Whalley ET, Colman RW. Bradykinin receptor antagonists type 2 attenuate the inflammatory changes in peptidoglycan-induced acute arthritis in the Lewis rat. Inflamm Res. 2001;50(3):149-155.
    • (2001) Inflamm Res. , vol.50 , Issue.3 , pp. 149-155
    • Uknis, A.B.1    DeLa Cadena, R.A.2    Janardham, R.3    Sartor, R.B.4    Whalley, E.T.5    Colman, R.W.6
  • 48
    • 0141923904 scopus 로고    scopus 로고
    • The mutation Ser511Asn leads to N-glycosylation and increases the cleavage of high molecular weight kininogen in rats genetically susceptible to inflammation
    • Isordia-Salas I, et al. The mutation Ser511Asn leads to N-glycosylation and increases the cleavage of high molecular weight kininogen in rats genetically susceptible to inflammation. Blood. 2003;102(8):2835-2842.
    • (2003) Blood. , vol.102 , Issue.8 , pp. 2835-2842
    • Isordia-Salas, I.1
  • 49
    • 80053130267 scopus 로고    scopus 로고
    • A novel mutation in the coagulation factor 12 gene in subjects with hereditary angioedema and normal C1-inhibitor
    • Bork K, Wulff K, Meinke P, Wagner N, Hardt J, Witzke G. A novel mutation in the coagulation factor 12 gene in subjects with hereditary angioedema and normal C1-inhibitor. Clin Immunol. 2011;141(1):31-35.
    • (2011) Clin Immunol. , vol.141 , Issue.1 , pp. 31-35
    • Bork, K.1    Wulff, K.2    Meinke, P.3    Wagner, N.4    Hardt, J.5    Witzke, G.6
  • 50
    • 84939241709 scopus 로고    scopus 로고
    • A deletion in the factor 12 gene analysed in two Turkish families with hereditary angioedema with normal C1 inhibitor (HAE type III): A Turkish F12 mutant
    • Bork K, Wulff K, Hardt J, Witzke G. A deletion in the factor 12 gene analysed in two Turkish families with hereditary angioedema with normal C1 inhibitor (HAE type III): a Turkish F12 mutant. Allergy. 2013;68:15.
    • (2013) Allergy. , vol.68 , pp. 15
    • Bork, K.1    Wulff, K.2    Hardt, J.3    Witzke, G.4
  • 51
    • 84884374545 scopus 로고    scopus 로고
    • Novel duplication in the F12 gene in a patient with recurrent angioedema
    • Kiss N, et al. Novel duplication in the F12 gene in a patient with recurrent angioedema. Clin Immunol. 2013;149(1):142-145.
    • (2013) Clin Immunol. , vol.149 , Issue.1 , pp. 142-145
    • Kiss, N.1
  • 52
    • 0030812723 scopus 로고    scopus 로고
    • Mutations in the human factor XII gene
    • Schloesser M, et al. Mutations in the human factor XII gene. Blood. 1997;90(10):3967-3977.
    • (1997) Blood. , vol.90 , Issue.10 , pp. 3967-3977
    • Schloesser, M.1
  • 53
    • 0028017572 scopus 로고
    • Coagulation factor XII Locarno: The functional defect is caused by the amino acid substitution Arg 353-->Pro leading to loss of a kallikrein cleavage site
    • Hovinga JK, Schaller J, Stricker H, Wuillemin WA, Furlan M, Lammle B. Coagulation factor XII Locarno: the functional defect is caused by the amino acid substitution Arg 353-->Pro leading to loss of a kallikrein cleavage site. Blood. 1994;84(4):1173-1181.
    • (1994) Blood. , vol.84 , Issue.4 , pp. 1173-1181
    • Hovinga, J.K.1    Schaller, J.2    Stricker, H.3    Wuillemin, W.A.4    Furlan, M.5    Lammle, B.6
  • 55
    • 84883216057 scopus 로고    scopus 로고
    • Plasma kallikrein: The bradykinin-producing enzyme
    • Bjorkqvist J, Jamsa A, Renne T. Plasma kallikrein: the bradykinin-producing enzyme. Thromb Haemost. 2013;110(3):399-407.
    • (2013) Thromb Haemost. , vol.110 , Issue.3 , pp. 399-407
    • Bjorkqvist, J.1    Jamsa, A.2    Renne, T.3
  • 56
    • 0021235057 scopus 로고
    • In vitro activation of the contact (Hageman factor) system of plasma by heparin and chondroitin sulfate E
    • Hojima Y, Cochrane CG, Wiggins RC, Austen KF, Stevens RL. In vitro activation of the contact (Hageman factor) system of plasma by heparin and chondroitin sulfate E. Blood. 1984;63(6):1453-1459.
    • (1984) Blood. , vol.63 , Issue.6 , pp. 1453-1459
    • Hojima, Y.1    Cochrane, C.G.2    Wiggins, R.C.3    Austen, K.F.4    Stevens, R.L.5
  • 57
    • 0030851598 scopus 로고    scopus 로고
    • Mast cell derived heparin activates the contact system: A link to kinin generation in allergic reactions
    • Brunnee T, Reddigari SR, Shibayama Y, Kaplan AP, Silverberg M. Mast cell derived heparin activates the contact system: a link to kinin generation in allergic reactions. Clin Exp Allergy. 1997;27(6):653-663.
    • (1997) Clin Exp Allergy. , vol.27 , Issue.6 , pp. 653-663
    • Brunnee, T.1    Reddigari, S.R.2    Shibayama, Y.3    Kaplan, A.P.4    Silverberg, M.5
  • 58
    • 80155138033 scopus 로고    scopus 로고
    • Bleeding diathesis in patients with mast cell activation disease
    • Seidel H, et al. Bleeding diathesis in patients with mast cell activation disease. Thromb Haemost. 2011;106(5):987-989.
    • (2011) Thromb Haemost. , vol.106 , Issue.5 , pp. 987-989
    • Seidel, H.1
  • 59
    • 0035851273 scopus 로고    scopus 로고
    • Hereditary angioedema: A broad review for clinicians
    • Nzeako UC, Frigas E, Tremaine WJ. Hereditary angioedema: a broad review for clinicians. Arch Intern Med. 2001;161(20):2417-2429.
    • (2001) Arch Intern Med. , vol.161 , Issue.20 , pp. 2417-2429
    • Nzeako, U.C.1    Frigas, E.2    Tremaine, W.J.3
  • 60
    • 51349160073 scopus 로고    scopus 로고
    • Misfolded proteins activate factor XII in humans, leading to kallikrein formation without initiating coagulation
    • Maas C, et al. Misfolded proteins activate factor XII in humans, leading to kallikrein formation without initiating coagulation. J Clin Invest. 2008;118(9):3208-3218.
    • (2008) J Clin Invest. , vol.118 , Issue.9 , pp. 3208-3218
    • Maas, C.1
  • 61
    • 44849115945 scopus 로고    scopus 로고
    • Contaminated heparin associated with adverse clinical events and activation of the contact system
    • Kishimoto TK, et al. Contaminated heparin associated with adverse clinical events and activation of the contact system. N Engl J Med. 2008;358(23):2457-2467.
    • (2008) N Engl J Med. , vol.358 , Issue.23 , pp. 2457-2467
    • Kishimoto, T.K.1
  • 62
    • 0028589888 scopus 로고
    • Dextran sulfate activates contact system and mediates arterial hypotension via B2 kinin receptors
    • Siebeck M, et al. Dextran sulfate activates contact system and mediates arterial hypotension via B2 kinin receptors. J Appl Physiol. 1994;77(6):2675-2680.
    • (1994) J Appl Physiol. , vol.77 , Issue.6 , pp. 2675-2680
    • Siebeck, M.1
  • 63
    • 71149116751 scopus 로고    scopus 로고
    • Platelet polyphosphates are proinflammatory and procoagulant mediators in vivo
    • Muller F, et al. Platelet polyphosphates are proinflammatory and procoagulant mediators in vivo. Cell. 2009;139(6):1143-1156.
    • (2009) Cell. , vol.139 , Issue.6 , pp. 1143-1156
    • Muller, F.1
  • 64
    • 51349169451 scopus 로고    scopus 로고
    • The elusive physiologic role of Factor XII
    • Schmaier AH. The elusive physiologic role of Factor XII. J Clin Invest. 2008;118(9):3006-3009.
    • (2008) J Clin Invest. , vol.118 , Issue.9 , pp. 3006-3009
    • Schmaier, A.H.1
  • 65
    • 84897538637 scopus 로고    scopus 로고
    • Factor XII inhibition reduces thrombus formation in a primate thrombosis model
    • Matafonov A, et al. Factor XII inhibition reduces thrombus formation in a primate thrombosis model. Blood. 2014;123(11):1739-1746.
    • (2014) Blood. , vol.123 , Issue.11 , pp. 1739-1746
    • Matafonov, A.1
  • 66
    • 0025710581 scopus 로고
    • Designer and catalytic antibodies
    • Mayforth RD, Quintans J. Designer and catalytic antibodies. N Engl J Med. 1990;323(3):173-178.
    • (1990) N Engl J Med. , vol.323 , Issue.3 , pp. 173-178
    • Mayforth, R.D.1    Quintans, J.2
  • 67
    • 84908478697 scopus 로고    scopus 로고
    • A phase 1 study investigating DX-2930 in healthy subjects
    • Chyung Y, et al. A phase 1 study investigating DX-2930 in healthy subjects. Ann Allergy Asthma Immunol. 2014;113(4):460-466.
    • (2014) Ann Allergy Asthma Immunol. , vol.113 , Issue.4 , pp. 460-466
    • Chyung, Y.1
  • 68
    • 84878243943 scopus 로고    scopus 로고
    • Inhibition of vascular permeability by antisense-mediated inhibition of plasma kallikrein and coagulation factor 12
    • Bhattacharjee G, et al. Inhibition of vascular permeability by antisense-mediated inhibition of plasma kallikrein and coagulation factor 12. Nucleic Acid Ther. 2013;23(3):175-187.
    • (2013) Nucleic Acid Ther. , vol.23 , Issue.3 , pp. 175-187
    • Bhattacharjee, G.1
  • 69
    • 81155133305 scopus 로고    scopus 로고
    • Selective depletion of plasma prekallikrein or coagulation factor XII inhibits thrombosis in mice without increased risk of bleeding
    • Revenko AS, et al. Selective depletion of plasma prekallikrein or coagulation factor XII inhibits thrombosis in mice without increased risk of bleeding. Blood. 2011;118(19):5302-5311.
    • (2011) Blood. , vol.118 , Issue.19 , pp. 5302-5311
    • Revenko, A.S.1
  • 70
    • 36349019291 scopus 로고    scopus 로고
    • Enhanced N-glycosylation site analysis of sialoglycopeptides by strong cation exchange prefractionation applied to platelet plasma membranes
    • Lewandrowski U, Zahedi RP, Moebius J, Walter U, Sickmann A. Enhanced N-glycosylation site analysis of sialoglycopeptides by strong cation exchange prefractionation applied to platelet plasma membranes. Mol Cell Proteomics. 2007;6(11):1933-1941.
    • (2007) Mol Cell Proteomics. , vol.6 , Issue.11 , pp. 1933-1941
    • Lewandrowski, U.1    Zahedi, R.P.2    Moebius, J.3    Walter, U.4    Sickmann, A.5
  • 71
    • 0034721787 scopus 로고    scopus 로고
    • High molecular weight kininogen utilizes heparan sulfate proteoglycans for accumulation on endothelial cells
    • Renne T, Dedio J, David G, Muller-Esterl W. High molecular weight kininogen utilizes heparan sulfate proteoglycans for accumulation on endothelial cells. J Biol Chem. 2000;275(43):33688-33696.
    • (2000) J Biol Chem. , vol.275 , Issue.43 , pp. 33688-33696
    • Renne, T.1    Dedio, J.2    David, G.3    Muller-Esterl, W.4
  • 72
    • 0033520434 scopus 로고    scopus 로고
    • Mapping of the discontinuous H-kininogen binding site of plasma prekallikrein. Evidence for a critical role of apple domain-2
    • Renne T, Dedio J, Meijers JC, Chung D, Muller-Esterl W. Mapping of the discontinuous H-kininogen binding site of plasma prekallikrein. Evidence for a critical role of apple domain-2. J Biol Chem. 1999;274(36):25777-25784.
    • (1999) J Biol Chem. , vol.274 , Issue.36 , pp. 25777-25784
    • Renne, T.1    Dedio, J.2    Meijers, J.C.3    Chung, D.4    Muller-Esterl, W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.