Comparative study of inhibitory antibody derivatives towards thrombin activatable fibrinolysis inhibitor

Thrombosis and Haemostasis

Volumn 102, Issue 1, 2009, Pages 69-75

  Develter, Jan ^a   Dewilde, Maarten ^a   Gils, Ann ^a   Declerck, Paul J ^a  

^a UNIVERSITY OF LEUVEN   (Belgium)

Author keywords

Antibody; Drug design; Fibrinolysis; Single chain Fv; Thrombin activatable fibrinolysis inhibitor (TAFI) carboxypeptidases

Indexed keywords

IMMUNOGLOBULIN F(AB) FRAGMENT; MONOCLONAL ANTIBODY; PAPAIN; PLASMIN; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; THROMBIN; THROMBIN ACTIVATABLE FIBRINOLYSIS INHIBITOR; THROMBOMODULIN;

ARTICLE; BLOOD CLOT LYSIS; COMPARATIVE STUDY; CONTROLLED STUDY; DRUG ACTIVITY; DRUG TARGETING; ENZYME INHIBITION; HUMAN; MOLECULAR CLONING; PRIORITY JOURNAL; PROTEIN EXPRESSION;

AMINO ACID SEQUENCE; ANTIBODIES, MONOCLONAL; CARBOXYPEPTIDASE U; CLONING, MOLECULAR; DOSE-RESPONSE RELATIONSHIP, IMMUNOLOGIC; DRUG DESIGN; FIBRINOLYSIS; IMMUNOGLOBULIN FAB FRAGMENTS; IMMUNOGLOBULIN VARIABLE REGION; MOLECULAR SEQUENCE DATA; RECOMBINANT PROTEINS;

EID: 67749145269     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH08-09-0834     Document Type: Article

References (38)

1. Fleury V, Angles-Cano E. Characterization of the binding of plasminogen to fibrin surfaces: the role of carboxy-terminal lysines. Biochemistry 1991; 30: 7630-7638.
2. Wang W, Boffa MB, Bajzar L, et al. A study of the mechanism of inhibition of fibrinolysis by activated thrombin-activable fibrinolysis inhibitor. J Biol Chem 1998; 273: 27176-27181.
3. te Velde EA, Wagenaar GTM, Reijerkerk A, et al. Impaired healing of cutaneous wounds and colonic anastomoses in mice lacking thrombin-activatable fibrinolysis inhibitor. J Thromb Haemost 2003; 1: 2087-2096.
4. Myles T, Nishimura T, Yun TH, et al. Thrombin activatable fibrinolysis inhibitor, a potential regulator of vascular inflammation. J Biol Chem 2003; 278: 51059-51067.
5. Asai S, Sato T, Tada T, et al. Absence of procarboxypeptidase R induces complement-mediated lethal inflammation in lipopolysaccharide-primed mice. J Immunol 2004; 173: 4669-4674.
6. 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: 431-442.
7. 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: 16603-16608.
8. Boffa MB, Wang W, Bajzar L, et al. 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: 2127-2135.
9. Boffa MB, Bell R, Stevens WK, et al. Roles of thermal instability and proteolytic cleavage in regulation of activated thrombin-activable fibrinolysis inhibitor. J Biol Chem 2000; 275: 12868-12878.
10. Marx PF, Hackeng TM, Dawson PE, et al. 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: 12410-12415.
11. Silveira A, Schatteman K, Goossens F, et al. Plasma procarboxypeptidase U in men with symptomatic coronary artery disease. Thromb Haemost 2000; 84: 364-368.
12. van-Tilburg NH, Rosendaal FR, Bertina RM. Thrombin activatable fibrinolysis inhibitor and the risk for deep vein thrombosis. Blood 2000; 95: 2855-2859.
13. Redlitz A, Nicolini FA, Malycky JL, et al. Inducible carboxypeptidase activity. A role in clot lysis in vivo. Circulation 1996; 93: 1328-1330.
14. Minnema MC, Friederich PW, Levi M, et al. Enhancement of rabbit jugular vein thrombolysis by neutralization of factor XI. In vivo evidence for a role of factor XI as an anti-fibrinolytic factor. J Clin Invest 1998; 101: 10-14.
15. Klement P, Liao P, Bajzar L. A novel approach to arterial thrombolysis. Blood 1999; 94: 2735-2743.
16. Nagashima M, Werner M, Wang M, et al. 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: 333-342.
17. Wang YX, da Cunha V, Vincelette J, et al. 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: 54-61.
18. Leurs J, Hendriks D. Carboxypeptidase U (TAFIa): a metallocarboxypeptidase with a distinct role in haemostasis and a possible risk factor for thrombotic disease. Thromb Haemost 2005; 94: 471-487.
19. Vendrell J, Querol E, Aviles FX. Metallocarboxypeptidases and their protein inhibitors. Structure, function and biomedical properties. Biochim Biophys Acta 2000; 1477: 284-298.
20. Gils A, Ceresa E, Macovei AM, et al. Modulation of TAFI function through different pathways-implications for the development of TAFI inhibitors. J Thromb Haemost 2005; 3: 2745-2753.
21. Lonberg N. Human antibodies from transgenic animals. Nat Biotechnol 2005; 23: 1117-1125.
22. Gils A, Alessi MC, Brouwers E, et al. Development of a genotype 325-specific proCPU/TAFI ELISA. Arterioscler Thromb Vasc Biol 2003; 23: 1122-1127.
23. Develter J, Booth NA, Declerck PJ, et al. Bispecific targeting of thrombin activatable fibrinolysis inhibitor and plasminogen activator inhibitor-1 by a heterodimer diabody. J Thromb Haemost 2008; 6: 1884-1891.
24. Mosnier LO, von-dem-Borne PA, Meijers JC, et al. 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: 829-835.
25. Mutch NJ, Thomas L, Moore NR, et al. TAFIa, PAI-1 and alpha-antiplasmin: complementary roles in regulating lysis of thrombi and plasma clots. J Thromb Haemost 2007; 5: 812-817.
26. Kipriyanov SM, Moldenhauer G, Martin AC, et al. Two amino acid mutations in an anti-human CD3 single chain Fv antibody fragment that affect the yield on bacterial secretion but not the affinity. Protein Eng 1997; 10: 445-453.
27. Polla MO, Tottie L, Norden C, et al. Design and synthesis of potent, orally active, inhibitors of carboxypeptidase U (TAFIa). Bioorg Med Chem 2004; 12: 1151-1175.
28. Wang YX, Zhao L, Nagashima M, et al. A novel inhibitor of activated thrombin-activatable fibrinolysis inhibitor (TAFIa) - part I: pharmacological characterization. Thromb Haemost 2007; 97: 45-53.
29. Reichert JM, Rosensweig CJ, Faden LB, et al. Monoclonal antibody successes in the clinic. Nat Biotechnol 2005; 23: 1073-1078.
30. Wang W, Wang EQ, Balthasar JP. Monoclonal antibody pharmacokinetics and pharmacodynamics. Clin Pharmacol Ther 2008; 84: 548-558.
31. Hagemeyer CE, Schwarz M, Peter K. Single-chain antibodies as new antithrombotic drugs. Semin Thromb Hemost 2007; 33: 185-195.
32. Hagemeyer CE, Tomic I, Jaminet P, et al. Fibrin-targeted direct factor Xa inhibition: construction and characterization of a recombinant factor Xa inhibitor composed of an anti-fibrin single-chain antibody and tick anticoagulant peptide. Thromb Haemost 2004; 92: 47-53.
33. Schwarz M, Meade G, Stoll P, et al. Conformation-specific blockade of the integrin GPIIb/IIIa: a novel antiplatelet strategy that selectively targets activated platelets. Circ Res 2006; 99: 25-33.
34. Binette TM, Taylor FB, Jr., Peer G, et al. Thrombin-thrombomodulin connects coagulation and fibrinolysis: more than an in vitro phenomenon. Blood 2007; 110: 3168-3175.
35. Honegger A, Pluckthun A. The influence of the buried glutamine or glutamate residue in position 6 on the structure of immunoglobulin variable domains. J Mol Biol 2001; 309: 687-699.
36. Bothmann H, Pluckthun A. Selection for a periplasmic factor improving phage display and functional periplasmic expression. Nat Biotechnol 1998; 16: 376-380.
37. Fairlie DP, West ML, Wong AK. Towards protein surface mimetics. Curr Med Chem 1998; 5: 29-62.
38. Eichler J. Rational and random strategies for the mimicry of discontinuous protein binding sites. Protein Pept Lett 2004; 11: 281-290.