Purification of recombinant plasminogen activator inhibitor-1 in the active conformation by refolding from inclusion bodies

Protein Expression and Purification

Volumn 31, Issue 1, 2003, Pages 99-107

  Lee, Hak Joo ^a   Im, Hana ^a  

^a Sejong University   (South Korea)

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI; EUKARYOTA; PROKARYOTA;

EID: 0141539503     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1046-5928(03)00160-8     Document Type: Article

References (39)

1. M.C. Alessi, P.J. Declerck, M. De Mol, L. Nelles, D. Collen, Purification and characterisation of natural and recombinant human plasminogen activator inhibitor 1 (PAI-1), Eur. J. Biochem. 175 (1988) 531-540.
2. F. Blasi, N. Behrendt, M.V. Cubellis, V. Ellis, L.R. Lund, M.T. Masucci, L.B. Moller, D.P. Olson, N. Pedersen, M. Ploug, E. Ronne, K. Dano, The urokinase receptor and regulation of cell surface plasminogen activation, Cell Differ. Dev. 32(1990) 247-254.
3. K.A. Hajjar, The endothelial cell t-PA receptor, J. Biol. Chem. 266 (1991) 21962-21970.
4. T.M. Reilly, R. Seetharam, J.L. Duke, G.L. Davis, S.K. Pierce, H.L. Walton, D. Kingsley, W.P. Sisk, Purification and characterization of recombinant plasminogen activator inhibitor-1 from Esherichia coli, J. Biol. Chem. 265 (1990) 9570-9574.
5. W. Fay, A. Shapiro, J. Shih, R.R. Schleef, D. Ginsburg, A frameshift mutation resulting in complete plasminogen activator inhibitor-1 (PAI-1) deficiency, N. Eng. J. Med. 327 (1992) 1729-1733.
6. R.R. Schleef, D.L. Higgins, E. Pillemer, L.J. Levitt, Bleeding diathesis due to decreased functional activity of type 1 plasminogen-activator inhibitor, J. Clin. Invest. 83 (1989) 1747-1752.
7. D.J. Loskutoff, M. Sawdey, J. Mimuro, Type 1 plasminogen activator inhibitor, Prog. Hemost. Thromb. 9 (1989) 87-115.
8. I. Juhan-Vague, J. Valadier, M.C. Alessi, M.F. Aillaud, J. Ansaldi, C. Philip-Joet, P. Holvoet, A. Serradimigni, D. Collen, Deficient t-PA release and elevated PA inhibitor levels in patients with spontaneous or recurrent deep venous thrombosis, Thromb. Haemost. 57 (1987) 67-72.
9. G. Deng, S.A. Curriden, S. Wang, S. Rosenberg, D.J. Loskutoff, Is plasminogen activator inhibitor-1 the molecular switch that governs urokinase receptor-mediated cell adhesion and release?, J. Cell Biol. 134 (1996) 1563-1571.
10. 8 binding to vitronectin, Nature 383 (1996) 441-443.
11. 1-antitrypsin for structure and function of serpins, Biochemistry 28 (1989) 8951-8966.
12. T. Ny, M. Sawdey, D. Lawrence, J.L. Millan, D.J. Loskutoff, Cloning and sequence of a cDNA coding for the human β-migrating endothelial-cell-type plasminogen activator inhibitor, Proc. Natl. Acad. Sci. USA 83 (1986) 6776-6780.
13. H. Pannekoek, H. Veerman, H. Lambers, P. Diergaarde, C.L. Verweij, A.J. van Zonneveld, J.A. van Mourik, Endothelial plasminogen activator inhibitor (PAI): a new member of the Serpin gene family, EMBO J. 5 (1986) 2539-2544.
14. C.B. Anfinsen, Principles that govern the folding of protein chains, Science 181 (1973) 223-230.
15. D.C. Wiley, J.J. Skehel, The structure and function of the hemagglutinin membrane glycoprotein of influenza virus, Annu. Rev. Biochem. 56 (1987) 365-394.
16. P.E. Stein, R.W. Carrell, What do dysfunctional serpins tell us about molecular mobility and disease?, Nat. Struct. Biol. 2 (1995) 96-113.
17. C.M. Carr, C. Chaudhry, P.S. Kim, Influenza hemagglutinin is spring-loaded by a metastable native conformation, Proc. Natl. Acad. Sci. USA 94 (1997) 14306-14313.
18. 1-antitrypsin, J. Biol. Chem. 274 (1999) 11072-11077.
19. C. Lee, S.-H. Park, M.-Y. Lee, M-H. Yu, Regulation of protein function by native stability, Proc. Natl. Acad. Sci. USA 97 (2000) 7727-7731.
20. H.T. Wright, J.N. Scarsdale, Structural basis for serpin inhibitor activity, Proteins Struct. Funct. Genet. 22 (1995) 210-225.
21. R.A. Engh, R. Huber, W. Bode, A.J. Schulze, Divining the serpin inhibition mechanism: a suicide substrate "spring"?, Trends Biotechnol. 13 (1995) 503-510.
22. J.A. Huntington, R.J. Read, R.W. Carrell, Structure of a serpin-protease complex shows inhibition by deformation, Nature 407 (2000) 923-926.
23. J. Mottonen, A. Strand, J. Symersky, R.M. Sweet, D.E. Danley, K.F. Geoghegan, R.D. Gerard, E.J. Goldsmith, Structural basis of latency in plasminogen activator-1, Nature 355 (1992) 270-273.
24. C.M. Hekman, D.J. Loskutoff, Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants, J. Biol. Chem. 260 (1985) 11581-11587.
25. R.W. Carrell, J.A. Huntington, A. Mushunje, A. Zhou, The conformational basis of thrombosis, Thromb. Haemost. 86 (2001) 14-22.
26. 1-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational disease, Proc. Natl. Acad. Sci. 97 (2000) 67-72.
27. 1-antichymotrypsin, J. Biol. Chem. 173 (1998) 3695-3701.
28. A.M. Sharp, P.E. Stein, N.S. Pannu, R.W. Carrell, M.B. Berkenpas, D. Ginsburg. D.A. Lawrence, R.J. Read, The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion, Struct. Fold. Des. 7 (1999) 111-118.
29. N.A. Booth, I.R. MacGregor, N.R. Hunter, B. Bennett, Plasminogen activator inhibitor from human endothelial cells. Purification and partial characterization, Eur. J. Biochem. 165 (1987) 595-600.
30. P.A. Andreassen, A. Riccio, K.G. Welinder, R. Douglas, R. Sartorio, L.S. Nielsen, C. Oppenheimer, F. Blasi, K. Danø, Plasminogen activator inhibitor type-1. Reactive center and amino-terminal heterogeneity determined by protein and cDNA sequencing, FEBS Lett. 209 (1986) 213-218.
31. A. Gils, P.J. Declerck, Proteinase specificity and functional diversity in point mutants of plasminogen activator inhibitor-1, J. Biol. Chem. 272 (1997) 12662-12666.
32. P.J. Declerck, M. De Mol, D.E. Vaughan, D. Collen, Identification of a conformationally distinct form of plasminogen activator inhibitor-1, acting as a noninhibitory substrate for tissue-type plasminogen activator, J. Biol. Chem. 267 (1992) 11693-11696.
33. Z. Wang, J. Mottonen, E.J. Goldsmith, Kinetically controlled folding of the serpin plasminogen activator inhibitor 1, Biochemistry 35 (1996) 16443-16448.
34. 1-antitrypsin expressed as inclusion bodies in Esherichia coli: characterization of aggregation, Biochim. Biophys. Acta 1247 (1995) 179-184.
35. H. Im, M.-H. Yu, Role of Lys335 in the metastability and function of inhibitory serpins, Protein Sci. 9 (2000) 934-941.
36. T.M. Jovin, Multiphasic zone electrophoresis, IV. Design and analysis of discontinuous buffer systems with a digital computer, Ann. N. Y. Acad. Sci. 209 (1973) 477-496.
37. E. Sancho, D.W. Tonge, R.C. Hockney, N.A. Booth, Purification and characterization of active and stable recombinant plasminogen-activator inhibitor accumulated at high levels in Esherichia coli, Eur. J. Biochem. 224 (1994) 125-134.
38. A. Zhou, R. Faint, P. Charlton, T.R. Dafforn, R.W. Carrell, Polymerization of plasminogen activator inhibitor-1, J. Biol. Chem. 276 (2001) 9115-9122.
39. A. Gils, I. Knockaert, P.J. Declerck, Substrate behavior of plasminogen activator inhibitor-1 is not associated with a lack of insertion of the reactive site loop, Biochemistry 35 (1996) 7474-7481.