Glycosylation dependent conformational transitions in plasminogen activator inhibitor-1: Evidence for the presence of two active conformations

Fibrinolysis and Proteolysis

Volumn 14, Issue 1, 2000, Pages 58-64

  Gils, A ^a   Knockaert, I ^a   Brouwers, E ^a   Declerck, P J ^a  

^a UNIVERSITY OF LEUVEN   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

PLASMINOGEN ACTIVATOR INHIBITOR 1; SERINE PROTEINASE INHIBITOR; TRITON X 100;

ARTICLE; CHO CELL; CONFORMATIONAL TRANSITION; GLYCOSYLATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; TEMPERATURE DEPENDENCE;

EID: 0034040240     PISSN: 13690191     EISSN: None     Source Type: Journal    
DOI: 10.1054/fipr.2000.0062     Document Type: Article

References (31)

1. Sprengers ED, Kluft C. Plasminogen activator inhibitors. Blood 1987; 69: 381-387.
2. Loskutoff DJ, Sawdey M, Mimuro J. Type 1 plasminogen activator inhibitor. Prog Hemost Thromb 1989; 9: 87-115.
3. Alessi MC, Declerck PJ, De Mol M et al. Purification and characterization of natural and recombinant human plasminogen activator inhibitor-1 (PAI-1). Eur J Biochem 1988; 175: 531-540.
4. Lawrence D, Strandberg L, Grundstrom T et al. Purification of active human plasminogen activator inhibitor 1 from Escherichia coli. Comparison with natural and recombinant forms purified from eucaryotic cells. Eur J Biochem 1989; 186: 523-533.
5. Hekman CM, Loskutoff DJ. Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants. J Biol Chem 1985; 260: 11581-11587.
6. Declerck PJ, De Mol M, Vaughan DE et al. 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: 11693-11696.
7. Mottonen J, Strand A, Symersky J et al. Structural basis of latency in plasminogen activator inhibitor-1. Nature 1992; 355: 270-273.
8. Seetharam R, Dwivedi AM, Duke JL et al. Purification and characterization of active and latent forms of recombinant plasminogen activator inhibitor 1 produced in Escherichia coli. Biochemistry 1992; 31: 9877-9882.
9. Vaughan DE, Declerck PJ, Reilly TM et al. Dynamic structural and functional relationship in recombinant plasminogen activator inhibitor-1 (rPAI-1). Biochim Biophys Acta 1993; 1202: 221-229.
10. Sancho E, Declerck PJ, Price NC et al. Conformational studies on plasminogen activator inhibitor (PAI-1) in active, latent, substrate, and cleaved forms. Biochemistry 1995; 34: 1064-1069.
11. Schulze AJ, Quarzago D, Andreasen PA. A spectroscopic study of the structures of latent, active and reactive center cleaved type 1 plasminogen activator inhibitor. Eur J Biochem 1996; 240: 550-555.
12. Sancho E, Tonge DW, Hockney RC et al. Purification and characterization of active and stable recombinant plasminogen-activator inhibitor accumulated at high levels in Escherichia coli. Eur J Biochem 1994; 224: 125-134.
13. Declerck PJ, De Mol M, Alessi MC et al. Purification and characterization of a plasminogen activator inhibitor I binding protein from human plasma. Identification as a multimeric form of S protein (vitronectin). J Biol Chem 1988; 263: 15454-15461.
14. Wiman B, Almquist A, Sigurdardottir O, et al. Plasminogen activator inhibitor 1 (PAI) is bound to vitronectin in plasma. FEBS Lett 1988; 242: 125-128.
15. Mimuro J, Sawdey M, Hattori M, et al. cDNA for bovine type I plasminogen activator inhibitor (PAI-1). Nucleic Acids Res 1989; 17: 8872-8872.
16. Urano T, Strandberg L, Johansson LB, et al. A substrate-like form of plasminogen-activator- inhibitor type I. Conversions between different forms by sodium dodecyl sulphate. Eur J Biochem 1992; 209: 985-992.
17. 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: 29-37.
18. van Mourik JA, Lawrence DA, Loskutoff DJ. Purification of an inhibitor of plasminogen activator (antiactivator) synthesized by endothelial cells. J Biol Chem 1984; 259: 14914-14921.
19. Wagner OF, Vetterlein M, Binder BR. Purification of an active plasminogen activator inhibitor immunologically related to the endothelial type plasminogen activator inhibitor from the conditioned media of a human melanoma cell line. J Biol Chem 1986; 261: 14474-14481.
20. Booth NA, MacGregor IR, Hunter NR et al. Plasminogen activator inhibitor from human endothelial cells. Purification and partial characterization. Eur J Biochem 1987; 165: 595-600.
21. Nielsen LS, Andreasen PA, Grondahl Hansen J et al. Monoclonal antibodies to human 54,000 molecular weight plasminogen activator inhibitor from fibrosarcoma cells-inhibitor neutralization and one-step affinity purification. Thromb Haemost 1986; 55: 206-212.
22. Chmielewska J, Carlsson T, Urden G et al. On the relationship between different molecular forms of the fast inhibitor of tissue plasminogen activator. Fibrinolysis 1987; 1: 67-73.
23. Andreasen PA, Nielsen LS, Kristensen P et al. Plasminogen activator inhibitor from human fibrosarcoma cells binds urokinase-type plasminogen activator, but not its proenzyme. J Biol Chem 1986; 261: 7644-7651.
24. 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: 7474-7481.
25. Kjoller L, Martensen PM, Sottrup-Jensen L et al. Conformational changes of the reactive centre loop and beta strand 5a accompany temperature dependent inhibitor substrate transition of plasminogen activator inhibitor 1. Eur J Biochem 1996; 241: 38-46.
26. Rodenburg KW, Kjoller L, Petersen HH, Andreasen PA. Binding of urokinase-type plasminogen activator plasminogen activator inhibitor-1 complex to the endocytosis receptors alpha(2)-macroglobulin receptor/low-density lipoprotein receptor-related protein and very-low- density lipoprotein receptor involves basic residues in the inhibitor. Biochemical Journal 1998; 329 Part 1: 55-63.
27. Stromqvist M, Andersson JO, Bostrom S et al. Separation of active and inactive forms of recombinant human plasminogen activator inhibitor type 1 (PAI-1) expressed in Chinese hamster ovary cells: comparison with native human PAI-1. Protein Expr Purif 1994; 5: 309-316.
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: 286-291.
29. Ehnebom J, Bjorquist P, Andersson JO et al. Detergent tween 80 modifies the specific activity of PAI-1. Fibrinolysis & Proteolysis 1997; 11: 165-170.
30. Andreasen PA, Egelund R, Jensen S et al. Solvent effects on activity and conformation of plasminogen activator inhibitor-1. Thromb Haemostas 1999; 81: 407-414.
31. Declerck PJ, Collen D. Measurement of plasminogen activator inhibitor 1 (PAI-1) in plasma with various monoclonal antibody-based enzyme-linked immunosorbent assays. Thromb Res Suppl 1990; 10: 3-9