Elucidation of the epitope of a latency-inducing antibody: Identification of a new molecular target for PAI-1 inhibition

Thrombosis and Haemostasis

Volumn 90, Issue 1, 2003, Pages 52-58

  Naessens, Dominik ^a   Gils, Ann ^a   Compernolle, Griet ^a   Declerck, Paul J ^a  

^a UNIVERSITY OF LEUVEN   (Belgium)

Author keywords

Epitope mapping; Fibrinolysis; Monoclonal antibody; PAI 1

Indexed keywords

ASPARTIC ACID; EPITOPE; HISTIDINE; LYSINE; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY MA 33B8; PLASMINOGEN ACTIVATOR INHIBITOR 1; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO ACID SEQUENCE; ANTIBODY AFFINITY; ARTICLE; BINDING SITE; CHIMERA; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DNA STRAND; EPITOPE MAPPING; FIBRINOLYSIS; HUMAN; HYDROGEN BOND; MOLECULAR DYNAMICS; PRIORITY JOURNAL; PROTEIN TARGETING; RAT; SEQUENCE ALIGNMENT;

EID: 0037623683     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0037-1613598     Document Type: Article

References (43)

1. Declerck PJ, De Mol M, Vaughan DE, Collen D. Identification of a conformationally distinct form of plasminogen activator inhibitor-1, acting as a noninhibitory substrate for tissue-type plasminogen activator. J Biol Chem 1992; 267(17):11693-6.
2. Hekman CM, Loskutoff DJ. Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants. J Biol Chem 1985; 260(21):11581-7.
3. Urano T, Strandberg L, Johansson LB, Ny T. A substrate-like form of plasminogen-activator-inhibitor type 1. Conversions between different forms by sodium dodecyl sulphate. Eur J Biochem 1992; 209(3):985-92.
4. Munch M, Heegaard CW, Andreasen PA Interconversions between active, inert and substrate forms of denatured/refolded type-1 plasminogen activator inhibitor. Biochim Biophys Acta 1993; 1202(1):29-37.
5. Sharp AM, Stein PE, Pannu NS, Carrell RW, Berkenpas MB, Ginsburg D et al. The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion. Structure Fold Des 1999; 7(2):111-8.
6. Nar H, Bauer M, Stassen JM, Lang D, Gils A, Declerck PJ Plasminogen activator inhibitor 1. Structure of the native serpin, comparison to its other conformers and implications for serpin inactivation. J Mol Biol 2000; 297(3):683-95.
7. Mottonen J, Strand A, Symersky J, et al. Structural basis of latency in plasminogen activator inhibitor-1. Nature 1992; 355(6357):270-3.
8. Collen D. The plasminogen (fibrinolytic) system. Thromb Haemost 1999; 82(2):259-70.
9. Wiman B, Chmielewska J, Ranby M. Inactivation of tissue plasminogen activator in plasma. Demonstration of a complex with a new rapid inhibitor. J Biol Chem 1984; 259(6):3644-7.
10. Loskutoff DJ, Sawdey M, Mimuro J. Type 1 plasminogen activator inhibitor. Prog Hemost Thromb 1989; 9:87-115.
11. Declerck PJ. Plasminogen activator inhibitor-1 (PAI-1) antigen. In: Laboratory Techniques in Thrombosis: A Manual. Jespersen J, Bertina RM, Haverkate F, editors. Dordrecht: Kluwer Academic Publishers, 1999: 239-45.
12. Declerck PJ, Juhan Vague I, Felez J, Wiman B. Pathophysiology of fibrinolysis. J Intern Med 1994; 236(4):425-32.
13. Rocha E, Paramo JA. The relationship between impaired fibrinolysis and coronary heart disease: A role for PAI-1. Fibrinolysis 1994; 8:294-303.
14. Juhan-Vague I, Alessi MC, Morange PE. Hypofibrinolysis and increased PAI-1 are linked to atherothrombosis via insulin resistance and obesity. Ann Med 2000; 32 Suppl. 1:78-84.
15. Folsom AR, Aleksik N, Park E, Salomaa V, Juneja H, Wu KK. Prospective study of fibrinolytic factors and incident coronary heart disease - The Atherosclerosis Risk in Communities (ARIC) Study. Arterioscler Thromb Vasc Biol 2001; 21(4):611-7.
16. Levi M, Biemond BJ, Van Zonneveld AJ, Pannekoek H. Inhibition of plasminogen activator inhibitor-1 activity results in promotion of endogenous thrombolysis and inhibition of thrombus extension in models of experimental thrombosis [see comments]. Circulation 1992; 85(1):305-12.
17. Debrock S, Declerck PJ. Neutralization of plasminogen activator inhibitor-1 inhibitory properties: Identification of two different mechanisms. Biochim Biophys Acta 1997; 1337(2):257-66.
18. Ngo TH, Debrock S, Declerck PJ. Identification of functional synergism between monoclonal antibodies. Application to the enhancement of plasminogen activator inhibitor-1 neutralizing effects. FEBS Lett 1997; 416(3):373-6.
19. Abrahamson T, Nerme V, Stromqvist M, et al. Anti-thrombotic effect of a PAI-1 inhibitor in rats given endotoxin. Thromb Haemost 1996; 75(1):118-26.
20. Van Giezen JJ, Wahlund G, Nerme, Abrahamson T. The Fab-fragment of a PAI-1 inhibiting antibody reduces thrombus size and restores blood flow in a rat model of arterial thrombosis. Thromb Haemost 1997; 77(5):964-9.
21. Debrock S, Sironi L, Declerck PJ. Cloning of a single-chain variable fragment (scFv) switching active plasminogen activator inhibitor-1 to substrate. Gene 1997; 189(1):83-8.
22. Vleugels N, Gils A, Mannaerts S, Knockaert I, Declerck PJ. Evaluation of the mechanism of inactivation of plasminogen activator inhibitor-1 by monoclonal antibodies using a stable variant. Fibrinolysis & Proteolysis 1998; 12(5):277-82.
23. Verhamme I, Kvassman JO, Day DE, et al. Accelerated conversion of human plasminogen activator inhibitor-1 to its latent form by antibody binding. J Biol Chem 1999; 274(25):17511-7.
24. Ngo TH, Zhou Y, Stassen JM, Declerck PJ. Importance of N-terminal residues in plasminogen activator inhibitor 1 on its antibody induced latency transition. Thromb Haemost 2002; 88(2):288-93.
25. Montes R, Declerck PJ, Calvo A, et al. Prevention of renal fibrin deposition in endotoxin-induced DIC through inhibition of PAI-1. Thromb Haemost 2000; 84:65-70.
26. Gils A, Knockaert I, Declerck PJ. Substrate behavior of plasminogen activator inhibitor-1 is not associated with a lack of insertion of the reactive site loop. Biochemistry 1996; 35(23):7474-81.
27. Bijnens AP, Gils A, Knockaert I, Stassen JM, Declerck PJ. Importance of the hinge region between α-helix F and the main part of serpins, based upon identification of the epitope of plasminogen activator inhibitor type 1 neuratralizing antibodies. J Biol Chem 2000; 275:6375-80.
28. Gils A, Declerck PJ. Modulation of plasminogen activator inhibitor 1 by Triton X-100 - Identification of two consecutive conformational transitions. Thromb Haemost 1998; 80:286-91.
29. Gils A, Knockaert I, Brouwers E, Declerck PJ. Glycosylation dependent conformational transitions in plasminogen activator inhibitor-1: Evidence for the presence of two active conformations. Fibrinolysis & Proteolysis 2000; 14(1):58-64.
30. Bijnens AP, Gils A, Stassen JM, et al. The distal hinge of the reactive site loop and its proximity: A target to modulate plasminogen activator inhibito-1 activity. J Biol Chem 2001; 276(48):44912-8.
31. Bijnens AP, Ngo TH, Gils A, et al. Elucidation of the binding regions of PAI-1 neutralizing antibodies using chimeric variants of human and rat PAI-1. Thromb Haemost 2001; 85(5):866-74.
32. Greenspan NS, Di CE. Defining epitopes: It's not as easy as it seems. Nat Biotechnol 1999; 17(10):936-7.
33. Aertgeerts K, De Bondt HL, De Ranter CJ, Declerck PJ. Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1. Nat Struct Biol 1995; 2(10):891-7.
34. Kruger P, Verheyden S, Declerck PJ, Engelborghs Y. Extending the capabilities of targeted molecular dynamics: Simulation of a large conformational transition in plasminogen activator inhibitor 1. Protein Sci 2001; 10(4):798-808.
35. Sui GC, Wiman B. The Bβ-sheet in the PAI-1 molecule plays an important role for its stability. Thromb Haemost 2000; 83:896-901.
36. Lawrence DA, Berkenpas MB, Palaniappan S, Ginsburg D. Localization of vitronectin binding domain in plasminogen activator inhibitor-1. J Biol Chem 1994; 269(21):15223-8.
37. Padmanabhan J, Sane DC. Localization of a vitronectin binding region of plasminogen activator inhibitor-1. Thromb Haemost 1995; 73(5):829-34.
38. Jensen JK, Wind T, Andreasen PA. The vitronectin binding area of plasminogen activator inhibitor-1, mapped by mutagenesis and protection against in inactivating organochemical ligand. FEBS Lett 2002; 521(1-3):91-4.
39. Ehrlich HJ, Gebbink RK, Keijer J, Pannekoek H. Elucidation of structural requirements on plasminogen activator inhibitor 1 for binding to heparin. J Biol Chem 1992; 267(16):11606-11.
40. Edelberg JM, Reilly CF, Pizzo SV. The inhibition of tissue type plasminogen activator by plasminogen activator inhibitor-1. The effects of fibrinogen, heparin, vitronectin, and lipoprotein(a). J Biol Chem 1991; 266(12):7488-93.
41. Stoop AA, Jespers L, Lasters I, Eldering E, Pannekoek H. High-density mutagenesis by combined DMA shuffling and phage display to assign essential amino acid residues in protein-protein interactions: Application to study structure-function of plasminogen activation inhibitor 1 (PAI-I). J Mol Biol 2000; 301(5):1135-47.
42. Wind T, Jensen MA, Andreasen PA. Epitope mapping for four monoclonal antibodies against human plasminogen activator inhibitor type-1 - Implications for antibody-mediated PAI-1-neutralization and vitronectin-binding. Eur J Biochem 2001; 268(4):1095-106.
43. Gorlatova NV, Elokdah H, Fan K, Crandall DL, Lawrence DA. Mapping of a conformational epitope on Plasminogen Activator Inhibitor-1 by random mutagenesis: Implications for serpin function. J Biol Chem 2003; in press.