Conformational changes of the reactive-centre loop and β-strand 5A accompany temperature-dependent inhibitor-substrate transition of plasminogen-activator inhibitor 1

European Journal of Biochemistry

Volumn 241, Issue 1, 1996, Pages 38-46

  Kjøller, Lars ^a   Martensen, Pia M ^a   Sottrup Jensen, Lars ^a   Justesen, Just ^a   Rodenburg, Kees W ^a   Andreasen, Peter A ^a  

^a AARHUS UNIVERSITY   (Denmark)

Author keywords

Conformation; Plasminogen activator inhibitor; Proteolysis; Reactive centre loop; Serpin

Indexed keywords

PLASMINOGEN ACTIVATOR INHIBITOR 1; PROTEINASE;

ARTICLE; CONFORMATIONAL TRANSITION; ENZYME BINDING; ENZYME INHIBITION; HUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; TEMPERATURE;

EID: 0029828508     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1996.0038t.x     Document Type: Article

References (52)

1. Aertgeerts, K., De Bondt, H. L., De Ranter, C. J. & Deelerck, P. J. (1995) Mechanisms contributing to the conformational and functional flexibility of plasminogen activator inhibitor-1. Nature Struct. Biol. 2, 891-897.
2. Andreasen, P. A., Riceio, A., Welinder, K. G., Douglas, R., Sartorio, R., Nielsen, L. S., Oppenheimer, C., Blasi, E. & Dano, K. (1986a) Plasminogen activator inhibitor type-1: reactive center and aminoterminal heterogeneity determined by protein and cDNA sequencing, FEBS Lett, 209, 213-218.
3. Andreasen, P. A., Nielsen, L. S., Kristensen, P., Grøndahl-Hansen, J., Skriver, L. & Danø, K. (1986b) Plasminogen activator inhibitor from human fibrosarcoma cells hinds urokinase-type plasminogen activator, but not its proenzyme, J. Biol. Chem. 261, 7644-7651.
4. Andreasen, P. A., Georg, B., Lund, L. R., Riccio A. & Stacey, S. (1990) Plasminogen activator inhibitors: hormonally regulated serpins. Mol. Cell. Endocrinol. 68, 1-19.
5. Andreasen, P. A., Sottrup-Jensen, L., Kjøller, L., Nykjær, A., Moestrup, S. K., Munch Petersen, C. & Gliemann, J. (1994) Receptor-mediated endocytosis of plasminogen activators and activator/inhibitor complexes, FEBS Lett. 338, 239-245.
6. Audenaert, A.-M., Knockaert, I., Collen, D. & Declerck, P. J. (1994) Conversion of plasminogen activator inhibitor-1 from inhibitor to substrate by point mutations in the reactive-site loop, J. Biol. Chem. 269, 19559-19564.
7. Berkenpas, M. B., Lawrence, D. A. & Ginsberg, D. (1995) Molecular evolution of plasminogen activator inhibitor-1 functional stability. EMBO J. 14, 2969-2977.
8. 14 region of the putative reactive bond loop of the inhibitor, J. Biol. Chem. 267, 1976-1982.
9. Bode, W. & Huber, R. (1992) Natural protein proteinase inhibitors and their interaction with proteinases. Eur. J. Biochem. 204, 433-451.
10. Carrell, R. W. & Evans, D. L. I. (1992) Serpins: mobile conformations in a family of proteinase inhibitors, Curr. Opin. Struct. Biol. 2, 438-446.
11. Carrell, R. W., Evans, D. L. & Stein, P. E. (1991) Mobile reactive centre of serpins and the control of thrombosis. Nature 353, 576-578.
12. Carrell, R. W., Stein, P. E., Fermi, G. & Wardell, M. R. (1994) Biological implications of a 3 Å structure of dimeric antithrombin, Structure 2, 257-270.
13. Caso, R., Lane, D. A., Thompson, E. A., Olds, R. J., Thein, S. L., Panico, M., Blench, I., Morris, H. R., Freyssinet, J. M. & Aiach, M. (1991) Antithrombin Vicenza. Ala 384 to Pro (GCA to CCA) mutation, transforming the inhibitor into a substrate, Br. J. Haematol. 77, 87-92.
14. Cooperman, B. S., Stavridi, E., Nickbarg, E., Rescorla, E., Schlechter, N. M. & Rubin, H. (1993) Antichymotrypsin interaction with chymotrypsin. J. Biol. Chem. 268, 23616-23625.
15. Declerck, P. J., De Mol, M., Vaughan, D. E. & Collen, D. (1992) Identification of a conformationally distinct form of plasminogen activator inhibitor-1, acting as a non-inhibitory substrate for tissue-type plasminogen activator, J. Biol. Chem. 267, 11693- 11696.
16. Dill, K. A. (1990) Dominant forces in protein folding, Biochemisty 29, 7133-7155.
17. Gettins, P. G. W., Patston, P. A. & Schapira, M. (1993) The role of conformational change in serpin structure and function. Bioessays 15, 461-467.
18. Heegaard, C. W., Wiborg Simonsen, A. C., Oka, K., Kjøller, L., Christensen, A., Madsen, B., Ellgaard, L., Chan. L. & Andreasen, P. A. (1995) Very low density lipoprotein receptor binds and mediates endocytosis of urokinase-type plasminogen activator-type-1 plasminogen activator inhibitor complex. J. Biol. Chem. 270, 20855-20861.
19. Hekman, C. M. & Loskutoff, D. J. (1985) Endothelial cells produce a latent inhibitor of plasminogen activators that can be activated by denaturants, J. Biol. Chem. 260, 11581-11587.
20. 1-antitrypsin for structure and function of serpins, Biochemistry 28, 8951-8965.
21. 1-proteinase inhibitor variant T345R. Influence of P14 residue on substrate and inhibitory pathways. Biochemistry 33, 8538-8547.
22. Hopkins, P. C. R., Carrell, R. W. & Stone. S. R. (1993) Effects of mutations in the hinge region of serpins, Biochemistry 32, 7650-7657.
23. Keijer, J., Linders, M., van Zonneveld, A.-J., Ehrlich, H., De Boer, J.-P. & Pannekoek, H. (1990) The interaction of plasminogen activator inhibitor type-1 with plasminogen activator (tissue-type and urokinase-type) and fibrin localization of interaction sites and physiological relevance. Blood 78, 401-409.
24. Kiso, U., Kaudewitz, H., Menschen, A., Åstedt, B., Kruithof, E. K. O. & Bachman, F. (1988) Determination of intermediates, products and cleavage site in the reaction between plasminogen activator inhibitor type-2 and urokinases, FEBS Lett. 230, 51-56.
25. 1-antitrypsin that confer enhancement in thermal stability, J. Biol. Chem. 269, 9627-9631.
26. Lawrence, D. A., Olson, S. T., Palaniappan, S. & Ginsburg, D. (1994) Serpin reactive center loop mobility is required for inhibitor function but not for enzyme recognition. J. Biol. Chem. 269, 27657-27662.
27. Levin, E. G. (1986) Quantitation and properties of the active and latent plasminogen activator inhibitors in cultures of human endothelial cells. Blood 67, 1309-1313.
28. Levin, E. G. & Santell, L. (1987) Conversion of the active to latent plasminogen inhibitor from human endothelial cells. Blood 70, 1090-1098.
29. Mottonen, J., Strand, A., Symersky, J., Sweet, R. M., Danley, D. E., Geoghegan, K. F., Gerard, R. D. & Goldsmith, E. J. (1992) Structural basis of latency in plasminogen activator inhibitor-1, Nature 355, 270-273.
30. Munch, M., Heegaard, C. W., Jensen, P. H. & Andreasen, P. A. (1991) Distinction between latent, activated and reactive centre-cleaved forms with thermal stability and monoclonal antibodies. FEBS Lett. 295, 102-106.
31. Munch, M., Heegaard, C. W. & Andreasen, P. A. (1993) Interconversions between active, inert and substrate forms of denatured/refolded type-1 plasminogen activator inhibitor, Biochim. Biophys. Acta 1202, 29-37.
32. Nielsen, L. S., Andreasen, P. A., Grondahl-Hansen, J., Skriver, L. & Danø, K. (1986a) Plasminogen activators catalyse conversion of inhibitor from fibrosarcoma cells to an inactive form with a lower apparent molecular mass. FEBS Lett. 196, 269-273.
33. Nielsen, L. S., Andreasen, P. A., Grøndahl-Hansen, J., Huang, J.-Y., Kristensen, P. & Danø, K. (1986b) Monoclonal antibodies to human 54000 molecular mass plasminogen activator inhibitor from fibrosarcoma cells, Thromb. Haemostas. 55, 206-212.
34. 2-macroglobulin receptor/low density lipoprotein receptor-related protein. J. Biol. Chem. 269, 25668-25676.
35. Olson, S. (1985) Heparin and ionic strength-dependent conversion of antithrombin III from an inhibitor to a substrate of α-thronihin, J. Biol. Chem. 260, 10153-10160.
36. Patston, P. A., Gettins, P., Beechem, J. & Schapira, M. (1991) Mechanism of serpin action: Evidence that C1 inhibitor functions as a suicide substrate. Biochemistry 30, 8876-8882.
37. Potempa, J., Korzus, E. & Travis, J. (1994) The serpin superfamily of proteinase inhibitors: Structure function and regulation. J. Biol. Chem. 269, 15957-15960.
38. Pöllänen, J., Stephens, R. W. & Vaheri, A. (1991) Directed plasminogen activation at the surface of normal and malignant cells. Adv. Cancer Res. 51, 273-328.
39. Preissner, K. T. & Jenne, D. (1991) Stucture of vitronectin and its biological role in haemostasis, Thromb. Haemostas. 66, 123-132.
40. Sanzo, M. A., Marasa, J. C., Wittwer, A. J., Siegel, N. R., Harakas, N. K. & Feder, J. (1987) Purification and characterization of a tissue plasminogen activator-inhibitor complex from human umbilical vein endothelial cell conditioned medium, Biochemistry 26, 7443-7449.
41. Schechter, I. & Berger, A. C. (1967) On the size of the active site in proteases. Biochem. Biophys. Res. Commun. 27, 157-162.
42. 1-antichymotrypsin, J. Biol. Chem. 268, 23626-23633.
43. Schreuder, H. A., de Boer, B., Dijkema, R., Mulders, J., Theunissen, H. J. M., Grootenhuis, P. D. J. & Hol, W. G. J. (1994) The intact and cleaved human antithrombin III as a model for serpin-proteinase interactions, Nat. Struct. Biol. I, 48-54.
44. 1-antitrypsin by a peptide sequentially similar to β-strand s4A, Eur. J. Biochem. 194, 51-56.
45. Schulze, A. J., Huber, R., Bode, W. & Engh, R. A. (1994) Structural aspects of serpin inhibition, FEBS Lett. 344, 117-124.
46. Skriver, K., Wikoff, W. R., Patston, P. A., Tausk, F., Schapira, M., Kaplan, A. P. & Bock, S. C. (1991) Substrate properties of C1 inhibitor Ma (Alanine 434 - glutamic acid), J. Biol. Chem. 266, 9216-9221.
47. Stein, P. E. & Carell, R. W. (1995) What do dysfunctional serpins tell us about molecular mobility and disease, Nat. Struct. Biol. 2, 96-113.
48. Stein, P. E. & Chothia, C. (1991) Serpin tertiary structure transformation. J. Mol. Biol. 221, 615-621.
49. Stein, P. E., Leslie, A. G. W., Finch, J. T., Turnell, W. G., McLaughlin, P. J. & Carrell, R. W. (1990) Crystal structure of ovalbumin as a model for the reactive centre of serpins, Nature 347, 99-102.
50. Urano, T., Strandberg, L., Johansson, L. B.-Å. & Ny, T. (1992) A substrate-like form of plasminogen-activator-inhibitor type 1, Eur. J. Biochem. 209, 985-992.
51. Wei, A., Rubin, H., Cooperman, B. S. & Christianson, D. W. (1994) Crystal structure of an uncleaved serpin reveals the conformation of an inhibitory reactive loop, Nat. Struct. Biol. 1, 251-257.
52. Wright, H. T., Qian, H. X. & Huber, R. (1990) Crystal structure of plakalbumin, a proteolytically nicked form of ovalbumin, J. Mol. Biol. 213, 513-528.