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  • 1
    Rivera J, Vannakambadi G, Hook M, Speziale P. Fibrinogen-binding proteins of Gram-positive bacteria. Thromb Haemost 2007; 98: 50311.
  • 2
    Johnson LL, Berggren KN, Szaba FM, Chen W, Smiley ST. Fibrin-mediated protection against infection-stimulated immunopathology. J Exp Med 2003; 197: 8016.
  • 3
    Bergmann S, Hammerschmidt S. Fibrinolysis and host response in bacterial infections. Thromb Haemost 2007; 98: 51220.
  • 4
    Lähteenmäki K, Kyllönen P, Partanen L, Korhonen TK. Antiprotease inactivation by Salmonella enterica released from infected macrophages. Cell Microbiol 2005; 7: 52938.
  • 5
    Degen JL, Bugge TH, Goguen JD. Fibrin and fibrinolysis in infection and host defense. J Thromb Haemost 2007; 5 (Suppl 1): 2431.
  • 6
    Sun H. The interaction between pathogens and the host coagulation system. Physiology (Bethesda) 2006; 21: 2818.
  • 7
    Beaufort N, Wojciechowski P, Sommerhoff CP, Szmyd G, Dubin G, Eick S, Kellermann J, Schmitt M, Potempa J, Magdolen V. The human fibrinolytic system is a target for the staphylococcal metalloprotease aureolysin. Biochem J 2008; 410: 15765.
  • 8
    Haiko J, Kukkonen M, Ravantti JJ, Westerlund-Wikström B, Korhonen TK. The single substitution I259T, conserved in the plasminogen activator Pla of pandemic Yersinia pestis branches, enhances fibrinolytic activity. J Bacteriol 2009; 191: 475866.
  • 9
    Yun TH, Cott JE, Tapping RI, Slauch JM, Morrissey JH. Proteolytic inactivation of tissue factor pathway inhibitor by bacterial omptins. Blood 2009; 113: 113948.
  • 10
    Lathem WW, Price PA, Miller VL, Goldman WE. A plasminogen-activating protease specifically controls the development of primary pneumonic plague. Science 2007; 315: 50913.
  • 11
    Sebbane F, Jarrett CO, Gardner D, Long D, Hinnebusch BJ. Role of the Yersinia pestis plasminogen activator in the incidence of distinct septicemic and bubonic forms of flea-borne plague. Proc Natl Acad Sci USA 2006; 103: 552630.
  • 12
    Sodeinde OA, Subrahmanyam YV, Stark K, Quan T, Bao Y, Goguen JD. A surface protease and the invasive character of plague. Science 1992; 258: 10047.
  • 13
    Kukkonen M, Lähteenmäki K, Suomalainen M, Kalkkinen N, Emody L, Lang H, Korhonen TK. Protein regions important for plasminogen activation and inactivation of alpha2-antiplasmin in the surface protease Pla of Yersinia pestis. Mol Microbiol 2001; 40: 1097111.
  • 14
    Sebbane F, Lemaitre N, Sturdevant DE, Rebeil R, Virtaneva K, Porcella SF, Hinnebusch BJ. Adaptive response of Yersinia pestis to extracellular effectors of innate immunity during bubonic plague. Proc Natl Acad Sci USA 2006; 103: 1176671.
  • 15
    Rawlings ND, Morton FR, Kok CY, Kong J, Barrett AJ. MEROPS: the peptidase database. Nucleic Acids Res 2008; 36: D3205.
  • 16
    Haiko J, Suomalainen M, Ojala T, Lähteenmäki K, Korhonen TK. Invited review: breaking barriers--attack on innate immune defences by omptin surface proteases of enterobacterial pathogens. Innate Immun 2009; 15: 6780.
  • 17
    Hritonenko V, Stathopoulos C. Omptin proteins: an expanding family of outer membrane proteases in Gram-negative Enterobacteriaceae. Mol Membr Biol 2007; 24: 395406.
  • 18
    Ramu P, Lobo LA, Kukkonen M, Bjur E, Suomalainen M, Raukola H, Miettinen M, Julkunen I, Holst O, Rhen M, Korhonen TK, Lähteenmäki K. Activation of pro-matrix metalloproteinase-9 and degradation of gelatin by the surface protease PgtE of Salmonella enterica serovar Typhimurium. Int J Med Microbiol 2008; 298: 26378.
  • 19
    Handley SA, Miller VL. General and specific host responses to bacterial infection in Peyer’s patches: a role for stromelysin-1 (matrix metalloproteinase-3) during Salmonella enterica infection. Mol Microbiol 2007; 64: 94110.
  • 20
    Marx PF, Dawson PE, Bouma BN, Meijers JC. Plasmin-mediated activation and inactivation of thrombin-activatable fibrinolysis inhibitor. Biochemistry 2002; 41: 668896.
  • 21
    Kawamura T, Okada N, Okada H. Elastase from activated human neutrophils activates procarboxypeptidase R. Microbiol Immunol 2002; 46: 22530.
  • 22
    >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: 218338.
  • 23
    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: 166038.
  • 24
    Marx PF, Brondijk TH, Plug T, Romijn RA, Hemrika W, Meijers JC, Huizinga EG. Crystal structures of TAFI elucidate the inactivation mechanism of activated TAFI: a novel mechanism for enzyme autoregulation. Blood 2008; 112: 28039.
  • 25
    Marx PF, Hackeng TM, Dawson PE, Griffin JH, Meijers JC, Bouma BN. Inactivation of active thrombin-activable fibrinolysis inhibitor takes place by a process that involves conformational instability rather than proteolytic cleavage. J Biol Chem 2000; 275: 124105.
  • 26
    Mosnier LO, Von Dem Borne PA, Meijers JC, 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: 82935.
  • 27
    Sangrar W, Gabel BR, Boffa MB, Walker JB, Hancock MA, Marcovina SM, Horrevoets AJ, Nesheim ME, Koschinsky ML. The solution phase interaction between apolipoprotein(a) and plasminogen inhibits the binding of plasminogen to a plasmin-modified fibrinogen surface. Biochemistry 1997; 36: 1035363.
  • 28
    Kukkonen M, Suomalainen M, Kyllönen P, Lähteenmäki K, Lang H, Virkola R, Helander IM, Holst O, Korhonen TK. Lack of O-antigen is essential for plasminogen activation by Yersinia pestis and Salmonella enterica. Mol Microbiol 2004; 51: 21525.
  • 29
    Marx PF, Wagenaar GT, Reijerkerk A, Tiekstra MJ, Van Rossum AG, Gebbink MF, Meijers JC. Characterization of mouse thrombin-activatable fibrinolysis inhibitor. Thromb Haemost 2000; 83: 297303.
  • 30
    Willemse J, Leurs J, Verkerk R, Hendriks D. Development of a fast kinetic method for the determination of carboxypeptidase U (TAFIa) using C-terminal arginine containing peptides as substrate. Anal Biochem 2005; 340: 10612.
  • 31
    Guimaraes AH, Barrett-Bergshoeff MM, Gils A, Declerck PJ, Rijken DC. Migration of the activation peptide of thrombin-activatable fibrinolysis inhibitor (TAFI) during SDS-polyacrylamide gel electrophoresis. J Thromb Haemost 2004; 2: 7804.
  • 32
    Boffa MB, Wang W, Bajzar L, Nesheim ME. Plasma and recombinant thrombin-activable fibrinolysis inhibitor (TAFI) and activated TAFI compared with respect to glycosylation, thrombin/thrombomodulin-dependent activation, thermal stability, and enzymatic properties. J Biol Chem 1998; 273: 212735.
  • 33
    Wang W, Boffa MB, Bajzar L, Walker JB, Nesheim ME. A study of the mechanism of inhibition of fibrinolysis by activated thrombin-activable fibrinolysis inhibitor. J Biol Chem 1998; 273: 2717681.
  • 34
    Wang W, Hendriks DF, Scharpe SS. Carboxypeptidase U, a plasma carboxypeptidase with high affinity for plasminogen. J Biol Chem 1994; 269: 1593744.
  • 35
    Mao SS, Colussi D, Bailey CM, Bosserman M, Burlein C, Gardell SJ, Carroll SS. Electrochemiluminescence assay for basic carboxypeptidases: inhibition of basic carboxypeptidases and activation of thrombin-activatable fibrinolysis inhibitor. Anal Biochem 2003; 319: 15970.
  • 36
    Wang YX, Da Cunha V, Vincelette J, Zhao L, Nagashima M, Kawai K, Yuan S, Emayan K, Islam I, Hosoya J, Sullivan ME, Dole WP, Morser J, Buckman BO, Vergona R. A novel inhibitor of activated thrombin activatable fibrinolysis inhibitor (TAFIa) - part II: enhancement of both exogenous and endogenous fibrinolysis in animal models of thrombosis. Thromb Haemost 2007; 97: 5461.
  • 37
    Lazoura E, Campbell W, Yamaguchi Y, Kato K, Okada N, Okada H. Rational structure-based design of a novel carboxypeptidase R inhibitor. Chem Biol 2002; 9: 112939.
  • 38
    Barrow JC, Nantermet PG, Stauffer SR, Ngo PL, Steinbeiser MA, Mao SS, Carroll SS, Bailey C, Colussi D, Bosserman M, Burlein C, Cook JJ, Sitko G, Tiller PR, Miller-Stein CM, Rose M, McMasters DR, Vacca JP, Selnick HG. Synthesis and evaluation of imidazole acetic acid inhibitors of activated thrombin-activatable fibrinolysis inhibitor as novel antithrombotics. J Med Chem 2003; 46: 52947.
  • 39
    Polla MO, Tottie L, Norden C, Linschoten M, Musil D, Trumpp-Kallmeyer S, Aukrust IR, Ringom R, Holm KH, Neset SM, Sandberg M, Thurmond J, Yu P, Hategan G, Anderson H. Design and synthesis of potent, orally active, inhibitors of carboxypeptidase U (TAFIa). Bioorg Med Chem 2004; 12: 115175.
  • 40
    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]hydroxypho sphinoyl] methyl]heptanoic acid], a specific inhibitor of plasma carboxypeptidase B. J Pharmacol Exp Ther 2004; 309: 60715.
  • 41
    Bunnage ME, Blagg J, Steele J, Owen DR, Allerton C, McElroy AB, Miller D, Ringer T, Butcher K, Beaumont K, Evans K, Gray AJ, Holland SJ, Feeder N, Moore RS, Brown DG. Discovery of potent & selective inhibitors of activated thrombin-activatable fibrinolysis inhibitor for the treatment of thrombosis. J Med Chem 2007; 50: 6095103.
  • 42
    Gils A, Ceresa E, Macovei AM, Marx PF, Peeters M, Compernolle G, Declerck PJ. Modulation of TAFI function through different pathways--implications for the development of TAFI inhibitors. J Thromb Haemost 2005; 3: 274553.
  • 43
    Bajzar L, Nesheim ME, Tracy PB. The profibrinolytic effect of activated protein C in clots formed from plasma is TAFI-dependent. Blood 1996; 88: 2093100.
  • 44
    Hillmayer K, Vancraenenbroeck R, De MM, 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: 18929.
  • 45
    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; 6: 130212.
  • 46
    Ramu P, Tanskanen R, Holmberg M, Lähteenmäki K, Korhonen TK, Meri S. The surface protease PgtE of Salmonella enterica affects complement activity by proteolytically cleaving C3b, C4b and C5. FEBS Lett 2007; 581: 171620.
  • 47
    Haiko J, Laakkonen L, Juuti K, Kalkkinen N, Korhonen TK. The omptins of Yersinia pestis and Salmonella enterica cleave the reactive center loop of plasminogen activator inhibitor 1. J Bacteriol 2010. Doi 10.1128/JB.00458-10.
  • 48
    Dekker N, Cox RC, Kramer RA, Egmond MR. Substrate specificity of the integral membrane protease OmpT determined by spatially addressed peptide libraries. Biochemistry 2001; 40: 1694701.
  • 49
    Wiman B. On the reaction of plasmin or plasmin-streptokinase complex with aprotinin or alpha 2-antiplasmin. Thromb Res 1980; 17: 14352.
  • 50
    Pahlman LI, Marx PF, Morgelin M, Lukomski S, Meijers JC, Herwald H. Thrombin-activatable fibrinolysis inhibitor binds to Streptococcus pyogenes by interacting with collagen-like proteins A and B. J Biol Chem 2007; 282: 2487381.
  • 51
    Bengtson SH, Sanden C, Morgelin M, Marx PF, Olin AI, Leeb-Lundberg LM, Meijers JC, Herwald H. Activation of TAFI on the surface of Streptococcus pyogenes evokes inflammatory reactions by modulating the kallikrein/kinin system. J Innate Immun 2008; 1: 1828.
  • 52
    Finegold MJ, Petery JJ, Berendt RF, Adams HR. Studies on the pathogenesis of plague. Blood coagulation and tissue responses of Macaca mulatta following exposure to aerosols of Pasteurella pestis. Am J Pathol 1968; 53: 99114.
  • 53
    Une T, Brubaker RR. In vivo comparison of avirulent Vwa- and Pgm- or Pstr phenotypes of yersiniae. Infect Immun 1984; 43: 895900.
  • 54
    Wick MJ, Harding CV, Normark SJ, Pfeifer JD. Parameters that influence the efficiency of processing antigenic epitopes expressed in Salmonella typhimurium. Infect Immun 1994; 62: 45428.