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Volumn 11, Issue SUPPL.1, 2013, Pages 306-315

Insights into thrombin activatable fibrinolysis inhibitor function and regulation

Author keywords

Blood coagulation; Carboxypeptidase U; Fibrinolysis; Inflammation; Thrombin activatable fibrinolysis inhibitor

Indexed keywords

THROMBIN ACTIVATABLE FIBRINOLYSIS INHIBITOR;

EID: 84880643902     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1111/jth.12216     Document Type: Review
Times cited : (80)

References (114)
  • 1
    • 84945736607 scopus 로고
    • Characterisation of a carboxypeptidase in human serum distinct from carboxypeptidase N
    • Hendriks D, Scharpé S, van Sande M, Lommaert MP. Characterisation of a carboxypeptidase in human serum distinct from carboxypeptidase N. J Clin Chem Clin Biochem 1989; 27: 277-85.
    • (1989) J Clin Chem Clin Biochem , vol.27 , pp. 277-285
    • Hendriks, D.1    Scharpé, S.2    van Sande, M.3    Lommaert, M.P.4
  • 2
    • 0024412863 scopus 로고
    • An arginine specific carboxypeptidase generated in blood during coagulation or inflammation which is unrelated to carboxypeptidase N or its subunits
    • Campbell W, Okada H. An arginine specific carboxypeptidase generated in blood during coagulation or inflammation which is unrelated to carboxypeptidase N or its subunits. Biochem Biophys Res Commun 1989; 162: 933-9.
    • (1989) Biochem Biophys Res Commun , vol.162 , pp. 933-939
    • Campbell, W.1    Okada, H.2
  • 3
    • 0025748556 scopus 로고
    • Isolation, molecular-cloning, and partial characterization of a novel carboxypeptidase-B from human plasma
    • Eaton DL, Malloy BE, Tsai SP, Henzel W, Drayna D. Isolation, molecular-cloning, and partial characterization of a novel carboxypeptidase-B from human plasma. J Biol Chem 1991; 266: 21833-8.
    • (1991) J Biol Chem , vol.266 , pp. 21833-21838
    • Eaton, D.L.1    Malloy, B.E.2    Tsai, S.P.3    Henzel, W.4    Drayna, D.5
  • 4
    • 0029044322 scopus 로고
    • Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor
    • Bajzar L, Manuel R, Nesheim ME. Purification and characterization of TAFI, a thrombin-activable fibrinolysis inhibitor. J Biol Chem 1995; 270: 14477-84.
    • (1995) J Biol Chem , vol.270 , pp. 14477-14484
    • Bajzar, L.1    Manuel, R.2    Nesheim, M.E.3
  • 5
    • 0028222563 scopus 로고
    • Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen
    • Wang W, Hendriks DF, Scharpé SS. Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen. J Biol Chem 1994; 269: 15937-44.
    • (1994) J Biol Chem , vol.269 , pp. 15937-15944
    • Wang, W.1    Hendriks, D.F.2    Scharpé, S.S.3
  • 6
    • 0030589619 scopus 로고    scopus 로고
    • The gene for human carboxypeptidase U (CPU)-a proposed novel regulator of plasminogen activation-maps to 13q14.11
    • Vanhoof G, Wauters J, Schatteman K, Hendriks D, Goossens F, Bossuyt P, Scharpé S. The gene for human carboxypeptidase U (CPU)-a proposed novel regulator of plasminogen activation-maps to 13q14.11. Genomics 1996; 38: 454-5.
    • (1996) Genomics , vol.38 , pp. 454-455
    • Vanhoof, G.1    Wauters, J.2    Schatteman, K.3    Hendriks, D.4    Goossens, F.5    Bossuyt, P.6    Scharpé, S.7
  • 7
    • 0033580640 scopus 로고    scopus 로고
    • Characterization of the gene encoding human TAFI (thrombin-activable fibrinolysis inhibitor; plasma procarboxypeptidase B)
    • Boffa MB, Reid TS, Joo E, Nesheim ME, Koschinsky ML. Characterization of the gene encoding human TAFI (thrombin-activable fibrinolysis inhibitor; plasma procarboxypeptidase B). Biochemistry 1999; 38: 6547-58.
    • (1999) Biochemistry , vol.38 , pp. 6547-6558
    • Boffa, M.B.1    Reid, T.S.2    Joo, E.3    Nesheim, M.E.4    Koschinsky, M.L.5
  • 8
    • 0031766583 scopus 로고    scopus 로고
    • Identification and characterization of two thrombin-activatable fibrinolysis inhibitor isoforms
    • Zhao L, Morser J, Bajzar L, Nesheim M, Nagashima M. Identification and characterization of two thrombin-activatable fibrinolysis inhibitor isoforms. Thromb Haemost 1998; 80: 949-55.
    • (1998) Thromb Haemost , vol.80 , pp. 949-955
    • Zhao, L.1    Morser, J.2    Bajzar, L.3    Nesheim, M.4    Nagashima, M.5
  • 10
    • 0038454527 scopus 로고    scopus 로고
    • Identification of thrombin activatable fibrinolysis inhibitor (TAFI) in human platelets
    • Mosnier LO, Buijtenhuijs P, Marx PF, Meijers JCM, Bouma BN. Identification of thrombin activatable fibrinolysis inhibitor (TAFI) in human platelets. Blood 2003; 101: 4844-6.
    • (2003) Blood , vol.101 , pp. 4844-4846
    • Mosnier, L.O.1    Buijtenhuijs, P.2    Marx, P.F.3    Meijers, J.C.M.4    Bouma, B.N.5
  • 11
    • 78149277497 scopus 로고    scopus 로고
    • Secretion and antifibrinolytic function of thrombin-activatable fibrinolysis inhibitor from human platelets
    • Schadinger SL, Lin JH, Garand M, Boffa MB. Secretion and antifibrinolytic function of thrombin-activatable fibrinolysis inhibitor from human platelets. J Thromb Haemost 2010; 8: 2523-9.
    • (2010) J Thromb Haemost , vol.8 , pp. 2523-2529
    • Schadinger, S.L.1    Lin, J.H.2    Garand, M.3    Boffa, M.B.4
  • 12
    • 53449101060 scopus 로고    scopus 로고
    • Crystal structures of TAFI elucidate the inactivation mechanism of activated TAFI: a novel mechanism for enzyme autoregulation
    • Marx PF, Brondijk THC, Plug T, Romijn RA, Hemrika W, Meijers JCM, Huizinga EG. Crystal structures of TAFI elucidate the inactivation mechanism of activated TAFI: a novel mechanism for enzyme autoregulation. Blood 2008; 112: 2803-9.
    • (2008) Blood , vol.112 , pp. 2803-2809
    • Marx, P.F.1    Brondijk, T.H.C.2    Plug, T.3    Romijn, R.A.4    Hemrika, W.5    Meijers, J.C.M.6    Huizinga, E.G.7
  • 13
    • 0029793068 scopus 로고    scopus 로고
    • The profibrinolytic effect of activated protein C in clots formed from plasma is TAFI-dependent
    • Bajzar L, Nesheim ME, Tracy PB. The profibrinolytic effect of activated protein C in clots formed from plasma is TAFI-dependent. Blood 1996; 88: 2093-100.
    • (1996) Blood , vol.88 , pp. 2093-2100
    • Bajzar, L.1    Nesheim, M.E.2    Tracy, P.B.3
  • 14
    • 0031775510 scopus 로고    scopus 로고
    • Plasma TAFI levels influence the clot lysis time in healthy individuals in the presence of an intact intrinsic pathway of coagulation
    • Mosnier LO, von dem Borne PAK, Meijers JCM, Bouma BN. Plasma TAFI levels influence the clot lysis time in healthy individuals in the presence of an intact intrinsic pathway of coagulation. Thromb Haemost 1998; 80: 829-35.
    • (1998) Thromb Haemost , vol.80 , pp. 829-835
    • Mosnier, L.O.1    von dem Borne, P.A.K.2    Meijers, J.C.M.3    Bouma, B.N.4
  • 17
    • 33947585401 scopus 로고    scopus 로고
    • Curiouser and curiouser: recent advances in measurement of thrombin-activatable fibrinolysis inhibitor (TAFI) and in understanding its molecular genetics, gene regulation, and biological roles
    • Boffa MB, Koschinsky ML. Curiouser and curiouser: recent advances in measurement of thrombin-activatable fibrinolysis inhibitor (TAFI) and in understanding its molecular genetics, gene regulation, and biological roles. Clin Biochem 2007; 40: 431-42.
    • (2007) Clin Biochem , vol.40 , pp. 431-442
    • Boffa, M.B.1    Koschinsky, M.L.2
  • 18
    • 32244438306 scopus 로고    scopus 로고
    • Post-translational modifications of human thrombin-activatable fibrinolysis inhibitor (TAFI): evidence for a large shift in the isoelectric point and reduced solubility upon activation
    • Valnickova Z, Christensen T, Skottrup P, Thogersen IB, Hojrup P, Enghild JJ. Post-translational modifications of human thrombin-activatable fibrinolysis inhibitor (TAFI): evidence for a large shift in the isoelectric point and reduced solubility upon activation. Biochemistry 2006; 45: 1525-35.
    • (2006) Biochemistry , vol.45 , pp. 1525-1535
    • Valnickova, Z.1    Christensen, T.2    Skottrup, P.3    Thogersen, I.B.4    Hojrup, P.5    Enghild, J.J.6
  • 19
    • 44049087406 scopus 로고    scopus 로고
    • Thrombin-activable fibrinolysis inhibitor zymogen does not play a significant role in the attenuation of fibrinolysis
    • Foley JH, Kim P, Nesheim ME. Thrombin-activable fibrinolysis inhibitor zymogen does not play a significant role in the attenuation of fibrinolysis. J Biol Chem 2008; 283: 8863-7.
    • (2008) J Biol Chem , vol.283 , pp. 8863-8867
    • Foley, J.H.1    Kim, P.2    Nesheim, M.E.3
  • 20
    • 0029895009 scopus 로고    scopus 로고
    • TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex
    • Bajzar L, Morser J, Nesheim M. TAFI, or plasma procarboxypeptidase B, couples the coagulation and fibrinolytic cascades through the thrombin-thrombomodulin complex. J Biol Chem 1996; 271: 16603-8.
    • (1996) J Biol Chem , vol.271 , pp. 16603-16608
    • Bajzar, L.1    Morser, J.2    Nesheim, M.3
  • 21
    • 0032579276 scopus 로고    scopus 로고
    • Both cellular and soluble forms of thrombomodulin inhibit fibrinolysis by potentiating the activation of thrombin-activable fibrinolysis inhibitor
    • Bajzar L, Nesheim M, Morser J, Tracy PB. Both cellular and soluble forms of thrombomodulin inhibit fibrinolysis by potentiating the activation of thrombin-activable fibrinolysis inhibitor. J Biol Chem 1998; 273: 2792-8.
    • (1998) J Biol Chem , vol.273 , pp. 2792-2798
    • Bajzar, L.1    Nesheim, M.2    Morser, J.3    Tracy, P.B.4
  • 22
    • 0000650903 scopus 로고
    • Identification of an endothelial cell cofactor for thrombin-catalyzed activation of protein C
    • Esmon CT, Owen WG. Identification of an endothelial cell cofactor for thrombin-catalyzed activation of protein C. Proc Natl Acad Sci U S A 1981; 78: 2249-52.
    • (1981) Proc Natl Acad Sci U S A , vol.78 , pp. 2249-2252
    • Esmon, C.T.1    Owen, W.G.2
  • 23
    • 0020063793 scopus 로고
    • Isolation of a membrane-bound cofactor for thrombin-catalyzed activation of protein C
    • Esmon NL, Owen WG, Esmon CT. Isolation of a membrane-bound cofactor for thrombin-catalyzed activation of protein C. J Biol Chem 1982; 257: 859-64.
    • (1982) J Biol Chem , vol.257 , pp. 859-864
    • Esmon, N.L.1    Owen, W.G.2    Esmon, C.T.3
  • 24
    • 79957611298 scopus 로고    scopus 로고
    • Kinetics of activated thrombin-activatable fibrinolysis inhibitor (TAFIa)-catalyzed cleavage of C-terminal lysine residues of fibrin degradation products and removal of plasminogen-binding sites
    • Foley JH, Cook PF, Nesheim ME. Kinetics of activated thrombin-activatable fibrinolysis inhibitor (TAFIa)-catalyzed cleavage of C-terminal lysine residues of fibrin degradation products and removal of plasminogen-binding sites. J Biol Chem 2011; 286: 19280-6.
    • (2011) J Biol Chem , vol.286 , pp. 19280-19286
    • Foley, J.H.1    Cook, P.F.2    Nesheim, M.E.3
  • 25
    • 0033521034 scopus 로고    scopus 로고
    • Characterization of plasmin-mediated activation of plasma procarboxypeptidase B. Modulation by glycosaminoglycans
    • Mao SS, Cooper CM, Wood T, Shafer JA, Gardell SJ. Characterization of plasmin-mediated activation of plasma procarboxypeptidase B. Modulation by glycosaminoglycans. J Biol Chem 1999; 274: 35046-52.
    • (1999) J Biol Chem , vol.274 , pp. 35046-35052
    • Mao, S.S.1    Cooper, C.M.2    Wood, T.3    Shafer, J.A.4    Gardell, S.J.5
  • 26
    • 0037188376 scopus 로고    scopus 로고
    • Plasmin-mediated activation and inactivation of thrombin-activatable fibrinolysis inhibitor
    • Marx PF, Dawson PE, Bouma BN, Meijers JC. Plasmin-mediated activation and inactivation of thrombin-activatable fibrinolysis inhibitor. Biochemistry 2002; 41: 6688-96.
    • (2002) Biochemistry , vol.41 , pp. 6688-6696
    • Marx, P.F.1    Dawson, P.E.2    Bouma, B.N.3    Meijers, J.C.4
  • 27
    • 79960069147 scopus 로고    scopus 로고
    • Identification and characterisation of monoclonal antibodies that impair the activation of human thrombin activatable fibrinolysis inhibitor through different mechanisms
    • Mishra N, Vercauteren E, Develter J, Bammens R, Declerck PJ, Gils A. Identification and characterisation of monoclonal antibodies that impair the activation of human thrombin activatable fibrinolysis inhibitor through different mechanisms. Thromb Haemost 2011; 106: 90-101.
    • (2011) Thromb Haemost , vol.106 , pp. 90-101
    • Mishra, N.1    Vercauteren, E.2    Develter, J.3    Bammens, R.4    Declerck, P.J.5    Gils, A.6
  • 28
    • 84873034640 scopus 로고    scopus 로고
    • Plasmin and the thrombin-thrombomodulin complex both contribute to TAFI activation in whole blood model thrombi
    • Vercauteren E, Mutch NJ, Declerck PJ, Gils A. Plasmin and the thrombin-thrombomodulin complex both contribute to TAFI activation in whole blood model thrombi. J Thromb Haemost 2013; 11: 190-2.
    • (2013) J Thromb Haemost , vol.11 , pp. 190-192
    • Vercauteren, E.1    Mutch, N.J.2    Declerck, P.J.3    Gils, A.4
  • 29
    • 79955960414 scopus 로고    scopus 로고
    • Evaluation of the profibrinolytic properties of an anti-TAFI monoclonal antibody in a mouse thromboembolism model
    • Vercauteren E, Emmerechts J, Peeters M, Hoylaerts MF, Declerck PJ, Gils A. Evaluation of the profibrinolytic properties of an anti-TAFI monoclonal antibody in a mouse thromboembolism model. Blood 2011; 117: 4615-22.
    • (2011) Blood , vol.117 , pp. 4615-4622
    • Vercauteren, E.1    Emmerechts, J.2    Peeters, M.3    Hoylaerts, M.F.4    Declerck, P.J.5    Gils, A.6
  • 30
    • 0034725120 scopus 로고    scopus 로고
    • Roles of thermal instability and proteolytic cleavage in regulation of activated thrombin-activable fibrinolysis inhibitor
    • Boffa MB, Bell R, Stevens WK, Nesheim ME. Roles of thermal instability and proteolytic cleavage in regulation of activated thrombin-activable fibrinolysis inhibitor. J Biol Chem 2000; 275: 12868-78.
    • (2000) J Biol Chem , vol.275 , pp. 12868-12878
    • Boffa, M.B.1    Bell, R.2    Stevens, W.K.3    Nesheim, M.E.4
  • 31
    • 0037059828 scopus 로고    scopus 로고
    • Two naturally occurring variants of TAFI (Thr-325 and Ile-325) differ substantially with respect to thermal stability and antifibrinolytic activity of the enzyme
    • Schneider M, Boffa M, Stewart R, Rahman M, Koschinsky M, Nesheim M. Two naturally occurring variants of TAFI (Thr-325 and Ile-325) differ substantially with respect to thermal stability and antifibrinolytic activity of the enzyme. J Biol Chem 2002; 277: 1021-30.
    • (2002) J Biol Chem , vol.277 , pp. 1021-1030
    • Schneider, M.1    Boffa, M.2    Stewart, R.3    Rahman, M.4    Koschinsky, M.5    Nesheim, M.6
  • 33
    • 33846444017 scopus 로고    scopus 로고
    • Announcing a TAFIa mutant with a 180-fold increased half-life and concomitantly a strongly increased antifibrinolytic potential
    • Ceresa E, Peeters M, Declerck PJ, Gils A. Announcing a TAFIa mutant with a 180-fold increased half-life and concomitantly a strongly increased antifibrinolytic potential. J Thromb Haemost 2007; 5: 418-20.
    • (2007) J Thromb Haemost , vol.5 , pp. 418-420
    • Ceresa, E.1    Peeters, M.2    Declerck, P.J.3    Gils, A.4
  • 34
  • 35
    • 77952018180 scopus 로고    scopus 로고
    • Association between the Thr325Ile polymorphism of the thrombin-activatable fibrinolysis inhibitor and stroke in the Ludwigshafen Risk and Cardiovascular Health Study
    • Kozian DH, Lorenz M, März W, Cousin E, Mace S, Deleuze JF. Association between the Thr325Ile polymorphism of the thrombin-activatable fibrinolysis inhibitor and stroke in the Ludwigshafen Risk and Cardiovascular Health Study. Thromb Haemost 2010; 103: 976-83.
    • (2010) Thromb Haemost , vol.103 , pp. 976-983
    • Kozian, D.H.1    Lorenz, M.2    März, W.3    Cousin, E.4    Mace, S.5    Deleuze, J.F.6
  • 37
    • 33750079554 scopus 로고    scopus 로고
    • Characterization of rat thrombin-activatable fibrinolysis inhibitor (TAFI) - a comparative study assessing the biological equivalence of rat, murine and human TAFI
    • Hillmayer K, Macovei A, Pauwels D, Compernolle G, Declerck PJ, Gils A. Characterization of rat thrombin-activatable fibrinolysis inhibitor (TAFI) - a comparative study assessing the biological equivalence of rat, murine and human TAFI. J Thromb Haemost 2006; 4: 2470-7.
    • (2006) J Thromb Haemost , vol.4 , pp. 2470-2477
    • Hillmayer, K.1    Macovei, A.2    Pauwels, D.3    Compernolle, G.4    Declerck, P.J.5    Gils, A.6
  • 38
    • 47649114003 scopus 로고    scopus 로고
    • Conformational (in)stability of rat vs. human activated thrombin activatable fibrinolysis inhibitor
    • Hillmayer K, Ceresa E, Vancraenenbroeck R, Declerck PJ, Gils A. Conformational (in)stability of rat vs. human activated thrombin activatable fibrinolysis inhibitor. J Thromb Haemost 2008; 6: 1426-8.
    • (2008) J Thromb Haemost , vol.6 , pp. 1426-1428
    • Hillmayer, K.1    Ceresa, E.2    Vancraenenbroeck, R.3    Declerck, P.J.4    Gils, A.5
  • 39
    • 29744453508 scopus 로고    scopus 로고
    • Measurement of procarboxypeptidase U (TAFI) in human plasma: a laboratory challenge
    • Willemse JL, Hendriks DF. Measurement of procarboxypeptidase U (TAFI) in human plasma: a laboratory challenge. Clin Chem 2006; 52: 30-6.
    • (2006) Clin Chem , vol.52 , pp. 30-36
    • Willemse, J.L.1    Hendriks, D.F.2
  • 41
    • 79959852935 scopus 로고    scopus 로고
    • Comparative study of commercially available procarboxypeptidase U (thrombin-activatable fibrinolysis inhibitor) assays
    • Heylen E, Willemse JL, Hendriks DF. Comparative study of commercially available procarboxypeptidase U (thrombin-activatable fibrinolysis inhibitor) assays. J Thromb Haemost 2011; 9: 1407-9.
    • (2011) J Thromb Haemost , vol.9 , pp. 1407-1409
    • Heylen, E.1    Willemse, J.L.2    Hendriks, D.F.3
  • 42
    • 37549034248 scopus 로고    scopus 로고
    • Development of sandwich-type ELISAs for the quantification of rat and murine thrombin activatable fibrinolysis inhibitor in plasma
    • Hillmayer K, Brouwers E, León-Tamariz F, Meijers JC, Marx PF, Declerck PJ, Gils A. Development of sandwich-type ELISAs for the quantification of rat and murine thrombin activatable fibrinolysis inhibitor in plasma. J Thromb Haemost 2008; 6: 132-8.
    • (2008) J Thromb Haemost , vol.6 , pp. 132-138
    • Hillmayer, K.1    Brouwers, E.2    León-Tamariz, F.3    Meijers, J.C.4    Marx, P.F.5    Declerck, P.J.6    Gils, A.7
  • 43
    • 77953355876 scopus 로고    scopus 로고
    • Measurement of carboxypeptidase U (active thrombin-activatable fibrinolysis inhibitor) in plasma: challenges overcome by a novel selective assay
    • Heylen E, van Goethem S, Augustyns K, Hendriks D. Measurement of carboxypeptidase U (active thrombin-activatable fibrinolysis inhibitor) in plasma: challenges overcome by a novel selective assay. Anal Biochem 2010; 403: 114-6.
    • (2010) Anal Biochem , vol.403 , pp. 114-116
    • Heylen, E.1    van Goethem, S.2    Augustyns, K.3    Hendriks, D.4
  • 44
    • 78650926093 scopus 로고    scopus 로고
    • The role of thrombin activatable fibrinolysis inhibitor and factor XI in platelet-mediated fibrinolysis resistance: a thromboelastographic study in whole blood
    • Carrieri C, Galasso R, Semeraro F, Ammollo CT, Semeraro N, Colucci M. The role of thrombin activatable fibrinolysis inhibitor and factor XI in platelet-mediated fibrinolysis resistance: a thromboelastographic study in whole blood. J Thromb Haemost 2011; 9: 154-62.
    • (2011) J Thromb Haemost , vol.9 , pp. 154-162
    • Carrieri, C.1    Galasso, R.2    Semeraro, F.3    Ammollo, C.T.4    Semeraro, N.5    Colucci, M.6
  • 45
    • 36048964941 scopus 로고    scopus 로고
    • An assay for measuring functional activated thrombin-activatable fibrinolysis inhibitor in plasma
    • Kim PY, Foley J, Hsu G, Kim PY, Nesheim ME. An assay for measuring functional activated thrombin-activatable fibrinolysis inhibitor in plasma. Anal Biochem 2008; 372: 32-40.
    • (2008) Anal Biochem , vol.372 , pp. 32-40
    • Kim, P.Y.1    Foley, J.2    Hsu, G.3    Kim, P.Y.4    Nesheim, M.E.5
  • 46
    • 0031018008 scopus 로고    scopus 로고
    • Production and characterization of recombinant human plasminogen (S741C-fluorescein). A novel approach to study zymogen activation without generation of active protease
    • Horrevoets AJ, Pannekoek H, Nesheim ME. Production and characterization of recombinant human plasminogen (S741C-fluorescein). A novel approach to study zymogen activation without generation of active protease. J Biol Chem 1997; 272: 2176-82.
    • (1997) J Biol Chem , vol.272 , pp. 2176-2182
    • Horrevoets, A.J.1    Pannekoek, H.2    Nesheim, M.E.3
  • 48
    • 24944454291 scopus 로고    scopus 로고
    • Carboxypeptidase U (TAFla): a metallocarboxypeptidase with a distinct role in haemostasis and a possible risk factor for thrombotic disease
    • Leurs J, Hendriks D. Carboxypeptidase U (TAFla): a metallocarboxypeptidase with a distinct role in haemostasis and a possible risk factor for thrombotic disease. Thromb Haemost 2005; 94: 471-87.
    • (2005) Thromb Haemost , vol.94 , pp. 471-487
    • Leurs, J.1    Hendriks, D.2
  • 49
    • 77449151896 scopus 로고    scopus 로고
    • Carboxypeptidase U (TAFIa): a new drug target for fibrinolytic therapy?
    • Willemse JL, Heylen E, Nesheim ME, Hendriks DF. Carboxypeptidase U (TAFIa): a new drug target for fibrinolytic therapy? J Thromb Haemost 2009; 7: 1962-71.
    • (2009) J Thromb Haemost , vol.7 , pp. 1962-1971
    • Willemse, J.L.1    Heylen, E.2    Nesheim, M.E.3    Hendriks, D.F.4
  • 50
    • 84866327170 scopus 로고    scopus 로고
    • Design and characterization of a selenium-containing inhibitor of activated thrombin-activatable fibrinolysis inhibitor (TAFIa), a zinc-containing metalloprotease
    • Yoshimoto N, Sasaki T, Sugimoto K, Ishii H, Yamamoto K. Design and characterization of a selenium-containing inhibitor of activated thrombin-activatable fibrinolysis inhibitor (TAFIa), a zinc-containing metalloprotease. J Med Chem 2012; 55: 7696-705.
    • (2012) J Med Chem , vol.55 , pp. 7696-7705
    • Yoshimoto, N.1    Sasaki, T.2    Sugimoto, K.3    Ishii, H.4    Yamamoto, K.5
  • 51
    • 0028815556 scopus 로고
    • Plasma carboxypeptidases as regulators of the plasminogen system
    • Redlitz A, Tan AK, Eaton DL, Plow EF. Plasma carboxypeptidases as regulators of the plasminogen system. J Clin Invest 1995; 96: 2534-8.
    • (1995) J Clin Invest , vol.96 , pp. 2534-2538
    • Redlitz, A.1    Tan, A.K.2    Eaton, D.L.3    Plow, E.F.4
  • 52
    • 0032484025 scopus 로고    scopus 로고
    • A carboxypeptidase inhibitor from the medical leech Hirudo medicinalis - isolation, sequence analysis, cDNA cloning, recombinant expression, and characterization
    • Reverter D, Vendrell J, Canals F, Horstmann J, Aviles FX, Fritz H, Sommerhoff CP. A carboxypeptidase inhibitor from the medical leech Hirudo medicinalis - isolation, sequence analysis, cDNA cloning, recombinant expression, and characterization. J Biol Chem 1998; 273: 32927-33.
    • (1998) J Biol Chem , vol.273 , pp. 32927-32933
    • Reverter, D.1    Vendrell, J.2    Canals, F.3    Horstmann, J.4    Aviles, F.X.5    Fritz, H.6    Sommerhoff, C.P.7
  • 54
    • 0141484363 scopus 로고    scopus 로고
    • Reversible inhibitors of TAFIa can both promote and inhibit fibrinolysis
    • Schneider M, Nesheim M. Reversible inhibitors of TAFIa can both promote and inhibit fibrinolysis. J Thromb Haemost 2003; 1: 147-54.
    • (2003) J Thromb Haemost , vol.1 , pp. 147-154
    • Schneider, M.1    Nesheim, M.2
  • 56
    • 0037646413 scopus 로고    scopus 로고
    • Stabilization versus inhibition of TAFIa by competitive inhibitors in vitro
    • Walker JB, Hughes B, James I, Haddock P, Kluft C, Bajzar L. Stabilization versus inhibition of TAFIa by competitive inhibitors in vitro. J Biol Chem 2003; 278: 8913-21.
    • (2003) J Biol Chem , vol.278 , pp. 8913-8921
    • Walker, J.B.1    Hughes, B.2    James, I.3    Haddock, P.4    Kluft, C.5    Bajzar, L.6
  • 58
    • 54149105360 scopus 로고    scopus 로고
    • Discovery of novel mechanisms and molecular targets for the inhibition of activated thrombin activatable fibrinolysis inhibitor
    • Hillmayer K, Vancraenenbroeck R, De Maeyer M, Compernolle G, Declerck PJ, Gils A. Discovery of novel mechanisms and molecular targets for the inhibition of activated thrombin activatable fibrinolysis inhibitor. J Thromb Haemost 2008; 6: 1892-9.
    • (2008) J Thromb Haemost , vol.6 , pp. 1892-1899
    • Hillmayer, K.1    Vancraenenbroeck, R.2    De Maeyer, M.3    Compernolle, G.4    Declerck, P.J.5    Gils, A.6
  • 59
    • 77954477917 scopus 로고    scopus 로고
    • Generation and characterization of inhibitory nanobodies towards thrombin activatable fibrinolysis inhibitor
    • Buelens K, Hassanzadeh-Ghassabeh G, Muyldermans S, Gils A, Declerck PJ. Generation and characterization of inhibitory nanobodies towards thrombin activatable fibrinolysis inhibitor. J Thromb Haemost 2010; 8: 1302-12.
    • (2010) J Thromb Haemost , vol.8 , pp. 1302-1312
    • Buelens, K.1    Hassanzadeh-Ghassabeh, G.2    Muyldermans, S.3    Gils, A.4    Declerck, P.J.5
  • 60
    • 36148996511 scopus 로고    scopus 로고
    • Thrombin-thrombomodulin connects coagulation and fibrinolysis: more than an in vitro phenomenon
    • Binette TM, Taylor FB, Peer G, Bajzar L. Thrombin-thrombomodulin connects coagulation and fibrinolysis: more than an in vitro phenomenon. Blood 2007; 110: 3168-75.
    • (2007) Blood , vol.110 , pp. 3168-3175
    • Binette, T.M.1    Taylor, F.B.2    Peer, G.3    Bajzar, L.4
  • 61
    • 0032877624 scopus 로고    scopus 로고
    • A novel approach to arterial thrombolysis
    • Klement P, Liao P, Bajzar L. A novel approach to arterial thrombolysis. Blood 1999; 94: 2735-43.
    • (1999) Blood , vol.94 , pp. 2735-2743
    • Klement, P.1    Liao, P.2    Bajzar, L.3
  • 62
    • 0034657826 scopus 로고    scopus 로고
    • An inhibitor of activated thrombin-activatable fibrinolysis inhibitor potentiates tissue-type plasminogen activator-induced thrombolysis in a rabbit jugular vein thrombolysis model
    • Nagashima M, Werner M, Wang M, Zhao L, Light DR, Pagila R, Morser J, Verhallen P. An inhibitor of activated thrombin-activatable fibrinolysis inhibitor potentiates tissue-type plasminogen activator-induced thrombolysis in a rabbit jugular vein thrombolysis model. Thromb Res 2000; 98: 333-42.
    • (2000) Thromb Res , vol.98 , pp. 333-342
    • Nagashima, M.1    Werner, M.2    Wang, M.3    Zhao, L.4    Light, D.R.5    Pagila, R.6    Morser, J.7    Verhallen, P.8
  • 64
    • 0037436061 scopus 로고    scopus 로고
    • Carboxypeptidase B inhibitors reduce tissue factor-induced renal microthrombi in rats
    • Muto Y, Suzuki K, Sato E, Ishii H. Carboxypeptidase B inhibitors reduce tissue factor-induced renal microthrombi in rats. Eur J Pharmacol 2003; 461: 181-9.
    • (2003) Eur J Pharmacol , vol.461 , pp. 181-189
    • Muto, Y.1    Suzuki, K.2    Sato, E.3    Ishii, H.4
  • 65
    • 11144356646 scopus 로고    scopus 로고
    • Enhancement of fibrinolysis by EF6265[(S)-7-amino-2-[[[(R)-2-methyl-1-(3-phenylpropanoylamino)propyl]hydroxyphosphinoyl]methyl]heptanoic acid], a specific inhibitor of plasma carboxypeptidase B
    • Suzuki K, Muto Y, Fushihara K, Kanemoto K, Iida H, Sato E, Kikuchi C, Matsushima T, Kato E, Nomoto M, Yoshioka S, Ishii H. Enhancement of fibrinolysis by EF6265[(S)-7-amino-2-[[[(R)-2-methyl-1-(3-phenylpropanoylamino)propyl]hydroxyphosphinoyl]methyl]heptanoic acid], a specific inhibitor of plasma carboxypeptidase B. J Pharmacol Exp Ther 2004; 309: 607-15.
    • (2004) J Pharmacol Exp Ther , vol.309 , pp. 607-615
    • Suzuki, K.1    Muto, Y.2    Fushihara, K.3    Kanemoto, K.4    Iida, H.5    Sato, E.6    Kikuchi, C.7    Matsushima, T.8    Kato, E.9    Nomoto, M.10    Yoshioka, S.11    Ishii, H.12
  • 66
    • 0036147681 scopus 로고    scopus 로고
    • Enhancement of endogenous plasminogen activator-induced thrombolysis by argatroban and APC and its control by TAFl, measured in an arterial thrombolysis model in vivo using rat mesenteric arterioles
    • Hashimoto M, Yamashita T, Oiwa T, Watanabe S, Giddings JC, Yamamoto J. Enhancement of endogenous plasminogen activator-induced thrombolysis by argatroban and APC and its control by TAFl, measured in an arterial thrombolysis model in vivo using rat mesenteric arterioles. Thromb Haemost 2002; 87: 110-3.
    • (2002) Thromb Haemost , vol.87 , pp. 110-113
    • Hashimoto, M.1    Yamashita, T.2    Oiwa, T.3    Watanabe, S.4    Giddings, J.C.5    Yamamoto, J.6
  • 67
    • 67650470216 scopus 로고    scopus 로고
    • EF6265, a novel inhibitor of activated thrombin-activatable fibrinolysis inhibitor, protects against sepsis-induced organ dysfunction in rats
    • Muto Y, Suzuki K, Iida H, Sakakibara S, Kato E, Itoh F, Kakui N, Ishii H. EF6265, a novel inhibitor of activated thrombin-activatable fibrinolysis inhibitor, protects against sepsis-induced organ dysfunction in rats. Crit Care Med 2009; 37: 1744-9.
    • (2009) Crit Care Med , vol.37 , pp. 1744-1749
    • Muto, Y.1    Suzuki, K.2    Iida, H.3    Sakakibara, S.4    Kato, E.5    Itoh, F.6    Kakui, N.7    Ishii, H.8
  • 68
    • 84866263980 scopus 로고    scopus 로고
    • Intravenous and oral administration of DD2 [7-Amino-2-(sulfanylmethyl)heptanoic acid] produce thrombolysis through inhibition of plasma TAFIa in rats with tissue factor-induced microthrombosis
    • Sasaki T, Yoshimoto N, Sugimoto K, Takada K, Murayama N, Yamazaki H, Yamamoto K, Ishii H. Intravenous and oral administration of DD2 [7-Amino-2-(sulfanylmethyl)heptanoic acid] produce thrombolysis through inhibition of plasma TAFIa in rats with tissue factor-induced microthrombosis. Thromb Res 2012; 130: e222-8.
    • (2012) Thromb Res , vol.130
    • Sasaki, T.1    Yoshimoto, N.2    Sugimoto, K.3    Takada, K.4    Murayama, N.5    Yamazaki, H.6    Yamamoto, K.7    Ishii, H.8
  • 70
    • 33645563991 scopus 로고    scopus 로고
    • Murine model of ferric chloride-induced vena cava thrombosis: evidence for effect of potato carboxypeptidase inhibitor
    • Wang X, Smith PL, Hsu MY, Ogletree ML, Schumacher WA. Murine model of ferric chloride-induced vena cava thrombosis: evidence for effect of potato carboxypeptidase inhibitor. J Thromb Haemost 2006; 4: 403-10.
    • (2006) J Thromb Haemost , vol.4 , pp. 403-410
    • Wang, X.1    Smith, P.L.2    Hsu, M.Y.3    Ogletree, M.L.4    Schumacher, W.A.5
  • 71
    • 78149358940 scopus 로고    scopus 로고
    • Progress in metallocarboxypeptidases and their small molecular weight inhibitors
    • Fernandez D, Pallares I, Vendrell J, Aviles FX. Progress in metallocarboxypeptidases and their small molecular weight inhibitors. Biochimie 2010; 92: 1484-500.
    • (2010) Biochimie , vol.92 , pp. 1484-1500
    • Fernandez, D.1    Pallares, I.2    Vendrell, J.3    Aviles, F.X.4
  • 73
    • 46749103227 scopus 로고    scopus 로고
    • TAFla inhibitors in the treatment of thrombosis
    • Bunnage ME, Owen DR. TAFla inhibitors in the treatment of thrombosis. Curr Opin Drug Discov Devel 2008; 11: 480-6.
    • (2008) Curr Opin Drug Discov Devel , vol.11 , pp. 480-486
    • Bunnage, M.E.1    Owen, D.R.2
  • 75
    • 0025142701 scopus 로고
    • Evolutionary assembly of blood coagulation proteins
    • Patthy L. Evolutionary assembly of blood coagulation proteins. Semin Thromb Hemost 1990; 16: 245-59.
    • (1990) Semin Thromb Hemost , vol.16 , pp. 245-259
    • Patthy, L.1
  • 76
    • 0018774402 scopus 로고
    • On the specific interaction between the lysine-binding sites in plasmin and complementary sites in alpha2-antiplasmin and in fibrinogen
    • Wiman B, Lijnen HR, Collen D. On the specific interaction between the lysine-binding sites in plasmin and complementary sites in alpha2-antiplasmin and in fibrinogen. Biochim Biophys Acta 1979; 579: 142-54.
    • (1979) Biochim Biophys Acta , vol.579 , pp. 142-154
    • Wiman, B.1    Lijnen, H.R.2    Collen, D.3
  • 77
    • 3142584783 scopus 로고    scopus 로고
    • Carboxypeptidase U (TAFIa) prevents lysis from proceeding into the propagation phase through a threshold-dependent mechanism
    • Leurs J, Nerme V, Sim Y, Hendriks D. Carboxypeptidase U (TAFIa) prevents lysis from proceeding into the propagation phase through a threshold-dependent mechanism. J Thromb Haemost 2004; 2: 416-23.
    • (2004) J Thromb Haemost , vol.2 , pp. 416-423
    • Leurs, J.1    Nerme, V.2    Sim, Y.3    Hendriks, D.4
  • 78
    • 3142579973 scopus 로고    scopus 로고
    • The intrinsic threshold of the fibrinolytic system is modulated by basic carboxypeptidases, but the magnitude of the antifibrinolytic effect of activated thrombin-activable fibrinolysis inhibitor is masked by its instability
    • Walker JB, Bajzar L. The intrinsic threshold of the fibrinolytic system is modulated by basic carboxypeptidases, but the magnitude of the antifibrinolytic effect of activated thrombin-activable fibrinolysis inhibitor is masked by its instability. J Biol Chem 2004; 279: 27896-904.
    • (2004) J Biol Chem , vol.279 , pp. 27896-27904
    • Walker, J.B.1    Bajzar, L.2
  • 79
    • 34047264612 scopus 로고    scopus 로고
    • Thrombin-activable fibrinolysis inhibitor (TAFI) zymogen is an active carboxypeptidase
    • Valnickova Z, Thogersen IB, Potempa J, Enghild JJ. Thrombin-activable fibrinolysis inhibitor (TAFI) zymogen is an active carboxypeptidase. J Biol Chem 2007; 282: 3066-76.
    • (2007) J Biol Chem , vol.282 , pp. 3066-3076
    • Valnickova, Z.1    Thogersen, I.B.2    Potempa, J.3    Enghild, J.J.4
  • 80
    • 34250206344 scopus 로고    scopus 로고
    • The intrinsic enzymatic activity of procarboxypeptidase U (TAFI) does not significantly influence the fibrinolytic rate: reply to a rebuttal
    • Valnickova Z, Thogersen IB, Potempa J, Enghild JJ. The intrinsic enzymatic activity of procarboxypeptidase U (TAFI) does not significantly influence the fibrinolytic rate: reply to a rebuttal. J Thromb Haemost 2007; 5: 1336-7.
    • (2007) J Thromb Haemost , vol.5 , pp. 1336-1337
    • Valnickova, Z.1    Thogersen, I.B.2    Potempa, J.3    Enghild, J.J.4
  • 81
    • 34250176224 scopus 로고    scopus 로고
    • The intrinsic enzymatic activity of procarboxypeptidase U (TAFI) does not significantly influence the fibrinolysis rate: a rebuttal
    • Willemse JL, Heylen E, Hendriks DF. The intrinsic enzymatic activity of procarboxypeptidase U (TAFI) does not significantly influence the fibrinolysis rate: a rebuttal. J Thromb Haemost 2007; 5: 1334-6.
    • (2007) J Thromb Haemost , vol.5 , pp. 1334-1336
    • Willemse, J.L.1    Heylen, E.2    Hendriks, D.F.3
  • 83
    • 0034192129 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor and the risk for deep vein thrombosis
    • van Tilburg NH, Rosendaal FR, Bertina RM. Thrombin activatable fibrinolysis inhibitor and the risk for deep vein thrombosis. Blood 2000; 95: 2855-9.
    • (2000) Blood , vol.95 , pp. 2855-2859
    • van Tilburg, N.H.1    Rosendaal, F.R.2    Bertina, R.M.3
  • 84
    • 0036797501 scopus 로고    scopus 로고
    • Co-segregation of thrombophilic disorders in factor V Leiden carriers; the contributions of factor VIII, factor XI, thrombin activatable fibrinolysis inhibitor and lipoprotein(a) to the absolute risk of venous thromboembolism
    • Libourel EJ, Bank I, Meinardi JR, Balje-Volkers CP, Hamulyak K, Middeldorp S, Koopman MM, van Pampus EC, Prins MH, Büller HR, van der Meer J. Co-segregation of thrombophilic disorders in factor V Leiden carriers; the contributions of factor VIII, factor XI, thrombin activatable fibrinolysis inhibitor and lipoprotein(a) to the absolute risk of venous thromboembolism. Haematologica 2002; 87: 1068-73.
    • (2002) Haematologica , vol.87 , pp. 1068-1073
    • Libourel, E.J.1    Bank, I.2    Meinardi, J.R.3    Balje-Volkers, C.P.4    Hamulyak, K.5    Middeldorp, S.6    Koopman, M.M.7    van Pampus, E.C.8    Prins, M.H.9    Büller, H.R.10    van der Meer, J.11
  • 85
    • 79959539564 scopus 로고    scopus 로고
    • An update on the role of carboxypeptidase U (TAFIa) in fibrinolysis
    • Heylen E, Willemse J, Hendriks D. An update on the role of carboxypeptidase U (TAFIa) in fibrinolysis. Front Biosci 2011; 16: 2427-50.
    • (2011) Front Biosci , vol.16 , pp. 2427-2450
    • Heylen, E.1    Willemse, J.2    Hendriks, D.3
  • 86
    • 1542297149 scopus 로고    scopus 로고
    • Very high TAFI antigen levels are associated with a lower risk of hard coronary events: the PRIME Study
    • Juhan-Vague I, Morange PE. Very high TAFI antigen levels are associated with a lower risk of hard coronary events: the PRIME Study. J Thromb Haemost 2003; 1: 2243-4.
    • (2003) J Thromb Haemost , vol.1 , pp. 2243-2244
    • Juhan-Vague, I.1    Morange, P.E.2
  • 88
    • 66749125298 scopus 로고    scopus 로고
    • Low thrombin activatable fibrinolysis inhibitor activity levels are associated with an increased risk of a first myocardial infarction in men
    • Meltzer ME, Doggen CJ, de Groot PG, Meijers JC, Rosendaal FR, Lisman T. Low thrombin activatable fibrinolysis inhibitor activity levels are associated with an increased risk of a first myocardial infarction in men. Haematologica 2009; 94: 811-8.
    • (2009) Haematologica , vol.94 , pp. 811-818
    • Meltzer, M.E.1    Doggen, C.J.2    de Groot, P.G.3    Meijers, J.C.4    Rosendaal, F.R.5    Lisman, T.6
  • 89
    • 34247275973 scopus 로고    scopus 로고
    • Thrombin activatable fibrinolysis inhibitor activation peptide shows association with all major subtypes of ischemic stroke and with TAFI gene variation
    • Ladenvall C, Gils A, Jood K, Blomstrand C, Declerck PJ, Jern C. Thrombin activatable fibrinolysis inhibitor activation peptide shows association with all major subtypes of ischemic stroke and with TAFI gene variation. Arterioscler Thromb Vasc Biol 2007; 27: 955-62.
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 955-962
    • Ladenvall, C.1    Gils, A.2    Jood, K.3    Blomstrand, C.4    Declerck, P.J.5    Jern, C.6
  • 91
    • 84859181545 scopus 로고    scopus 로고
    • Convalescent plasma levels of TAFI activation peptide predict death and recurrent vascular events in ischemic stroke survivors
    • Jood K, Redfors P, Gils A, Blomstrand C, Declerck PJ, Jern C. Convalescent plasma levels of TAFI activation peptide predict death and recurrent vascular events in ischemic stroke survivors. J Thromb Haemost 2012; 10: 725-7.
    • (2012) J Thromb Haemost , vol.10 , pp. 725-727
    • Jood, K.1    Redfors, P.2    Gils, A.3    Blomstrand, C.4    Declerck, P.J.5    Jern, C.6
  • 93
    • 77955874727 scopus 로고    scopus 로고
    • Venous thrombosis risk associated with plasma hypofibrinolysis is explained by elevated plasma levels of TAFI and PAI-1
    • Meltzer ME, Lisman T, de Groot PG, Meijers JC, le Cessie S, Doggen CJ, Rosendaal FR. Venous thrombosis risk associated with plasma hypofibrinolysis is explained by elevated plasma levels of TAFI and PAI-1. Blood 2010; 116: 113-21.
    • (2010) Blood , vol.116 , pp. 113-121
    • Meltzer, M.E.1    Lisman, T.2    de Groot, P.G.3    Meijers, J.C.4    le Cessie, S.5    Doggen, C.J.6    Rosendaal, F.R.7
  • 97
    • 0036843274 scopus 로고    scopus 로고
    • In vivo regulation of plasminogen function by plasma carboxypeptidase B
    • Swaisgood CM, Schmitt D, Eaton D, Plow EF. In vivo regulation of plasminogen function by plasma carboxypeptidase B. J Clin Invest 2002; 110: 1275-82.
    • (2002) J Clin Invest , vol.110 , pp. 1275-1282
    • Swaisgood, C.M.1    Schmitt, D.2    Eaton, D.3    Plow, E.F.4
  • 100
    • 33846951195 scopus 로고    scopus 로고
    • Deficiency in thrombin-activatable fibrinolysis inhibitor (TAFI) protected mice from ferric chloride-induced vena cava thrombosis
    • Wang XK, Smith PL, Hsu MY, Tamasi JA, Bird E, Schumacher WA. Deficiency in thrombin-activatable fibrinolysis inhibitor (TAFI) protected mice from ferric chloride-induced vena cava thrombosis. J Thromb Thrombolysis 2007; 23: 41-9.
    • (2007) J Thromb Thrombolysis , vol.23 , pp. 41-49
    • Wang, X.K.1    Smith, P.L.2    Hsu, M.Y.3    Tamasi, J.A.4    Bird, E.5    Schumacher, W.A.6
  • 101
    • 84871057895 scopus 로고    scopus 로고
    • The hyperfibrinolytic state of mice with combined TAFI and PAI-1 gene deficiency is critically dependent on TAFI deficiency
    • Vercauteren E, Peeters M, Hoylaerts MF, Lijnen HR, Meijers JC, Declerck PJ, Gils A. The hyperfibrinolytic state of mice with combined TAFI and PAI-1 gene deficiency is critically dependent on TAFI deficiency. J Thromb Haemost 2012; 10: 2555-62.
    • (2012) J Thromb Haemost , vol.10 , pp. 2555-2562
    • Vercauteren, E.1    Peeters, M.2    Hoylaerts, M.F.3    Lijnen, H.R.4    Meijers, J.C.5    Declerck, P.J.6    Gils, A.7
  • 102
    • 0036191244 scopus 로고    scopus 로고
    • Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N
    • Campbell WD, Lazoura E, Okada N, Okada H. Inactivation of C3a and C5a octapeptides by carboxypeptidase R and carboxypeptidase N. Microbiol Immunol 2002; 46: 131-4.
    • (2002) Microbiol Immunol , vol.46 , pp. 131-134
    • Campbell, W.D.1    Lazoura, E.2    Okada, N.3    Okada, H.4
  • 105
    • 0021952732 scopus 로고
    • Chemotactic responses of human peripheral blood monocytes to the complement-derived peptides C5a and C5a des Arg
    • Marder SR, Chenoweth DE, Goldstein IM, Perez HD. Chemotactic responses of human peripheral blood monocytes to the complement-derived peptides C5a and C5a des Arg. J Immunol 1985; 134: 3325-31.
    • (1985) J Immunol , vol.134 , pp. 3325-3331
    • Marder, S.R.1    Chenoweth, D.E.2    Goldstein, I.M.3    Perez, H.D.4
  • 106
    • 0036721025 scopus 로고    scopus 로고
    • Essential role of the C5a receptor in E coli-induced oxidative burst and phagocytosis revealed by a novel lepirudin-based human whole blood model of inflammation
    • Mollnes TE, Brekke OL, Fung M, Fure H, Christiansen D, Bergseth G, Videm V, Lappegård KT, Köhl J, Lambris JD. Essential role of the C5a receptor in E coli-induced oxidative burst and phagocytosis revealed by a novel lepirudin-based human whole blood model of inflammation. Blood 2002; 100: 1869-77.
    • (2002) Blood , vol.100 , pp. 1869-1877
    • Mollnes, T.E.1    Brekke, O.L.2    Fung, M.3    Fure, H.4    Christiansen, D.5    Bergseth, G.6    Videm, V.7    Lappegård, K.T.8    Köhl, J.9    Lambris, J.D.10
  • 107
    • 0020539765 scopus 로고
    • Direct effect of complement factor C5a on the contractile state of isolated smooth muscle cells
    • Scheid CR, Webster RO, Henson PM, Findlay SR. Direct effect of complement factor C5a on the contractile state of isolated smooth muscle cells. J Immunol 1983; 130: 1997-9.
    • (1983) J Immunol , vol.130 , pp. 1997-1999
    • Scheid, C.R.1    Webster, R.O.2    Henson, P.M.3    Findlay, S.R.4
  • 108
    • 0035253577 scopus 로고    scopus 로고
    • Expression of the complement anaphylatoxin C3a and C5a receptors on bronchial epithelial and smooth muscle cells in models of sepsis and asthma
    • Drouin SM, Kildsgaard J, Haviland J, Zabner J, Jia HP, McCray PB, Tack BF, Wetsel RA. Expression of the complement anaphylatoxin C3a and C5a receptors on bronchial epithelial and smooth muscle cells in models of sepsis and asthma. J Immunol 2001; 166: 2025-32.
    • (2001) J Immunol , vol.166 , pp. 2025-2032
    • Drouin, S.M.1    Kildsgaard, J.2    Haviland, J.3    Zabner, J.4    Jia, H.P.5    McCray, P.B.6    Tack, B.F.7    Wetsel, R.A.8
  • 110
    • 76949088249 scopus 로고    scopus 로고
    • Silencing of C5a receptor gene with siRNA for protection from Gram-negative bacterial lipopolysaccharide-induced vascular permeability
    • Liu ZM, Zhu SM, Qin XJ, Cheng ZD, Liu MY, Zhang HM, Liu DX. Silencing of C5a receptor gene with siRNA for protection from Gram-negative bacterial lipopolysaccharide-induced vascular permeability. Mol Immunol 2010; 47: 1325-33.
    • (2010) Mol Immunol , vol.47 , pp. 1325-1333
    • Liu, Z.M.1    Zhu, S.M.2    Qin, X.J.3    Cheng, Z.D.4    Liu, M.Y.5    Zhang, H.M.6    Liu, D.X.7
  • 111
    • 0036155204 scopus 로고    scopus 로고
    • A role for C5a in augmenting IgG-dependent histamine release from basophils in chronic urticaria
    • Kikuchi Y, Kaplan AP. A role for C5a in augmenting IgG-dependent histamine release from basophils in chronic urticaria. J Allergy Clin Immunol 2002; 109: 114-8.
    • (2002) J Allergy Clin Immunol , vol.109 , pp. 114-118
    • Kikuchi, Y.1    Kaplan, A.P.2
  • 112
    • 0028265789 scopus 로고
    • Complement peptides C3a- and C5a-induced mediator release from dissociated human skin mast cells
    • el-Lati SG, Dahinden CA, Church MK. Complement peptides C3a- and C5a-induced mediator release from dissociated human skin mast cells. J Invest Dermatol 1994; 102: 803-6.
    • (1994) J Invest Dermatol , vol.102 , pp. 803-806
    • el-Lati, S.G.1    Dahinden, C.A.2    Church, M.K.3
  • 114
    • 77953779759 scopus 로고    scopus 로고
    • What has been learnt from the thrombin-activatable fibrinolysis inhibitor-deficient mouse?
    • Morser J, Gabazza EC, Myles T, Leung LL. What has been learnt from the thrombin-activatable fibrinolysis inhibitor-deficient mouse? J Thromb Haemost 2010; 8: 868-76.
    • (2010) J Thromb Haemost , vol.8 , pp. 868-876
    • Morser, J.1    Gabazza, E.C.2    Myles, T.3    Leung, L.L.4


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