The length of the reactive center loop modulates the latency transition of plasminogen activator inhibitor-1

Protein Science

Volumn 14, Issue 1, 2005, Pages 55-63

  Na, Yu Ran ^a   Im, Hana ^a  

^a Sejong University   (South Korea)

Author keywords

Conformational transition; Kinetic trap; Latency transition; Loop length; Plasminogen activator inhibitor 1; Protein folding; Serpin

Indexed keywords

PLASMINOGEN ACTIVATOR INHIBITOR 1; SERINE PROTEINASE INHIBITOR;

ALPHA HELIX; ARTICLE; BETA SHEET; NONHUMAN; PHASE TRANSITION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FAMILY; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; PROTEIN TRANSPORT;

ESCHERICHIA COLI; HUMANS; PLASMINOGEN ACTIVATOR INHIBITOR 1; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS;

EID: 11144248956     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.041063705     Document Type: Article

References (53)

1. Anfinsen, C.B. 1973. Principles that govern the folding of protein chains. Science 181: 223-230.
2. Berkenpas, M.B., Lawrence, D.A., and Ginsburg, D. 1995. Molecular evolution of plasminogen activator inhibitor-1 functional stability. EMBO J. 14: 2969-2977.
3. Carrell, R.W., Evans, D.L., and Stein, P.E. 1991. Mobile reactive centre of serpins and the control of thrombosis. Nature 353: 576-578.
4. Carrell, R.W., Stein, P.E., Fermi, G., and Wardell, M.R. 1994. Biological implication of a 3 Å structure of dimeric antithrombin. Structure 2: 257-270.
5. Carrell, R.W., Huntington, J.A., Mushunje, A., and Zhou, A. 2001. The conformational basis of thrombosis. Thromb. Haemost. 86: 14-22.
6. 1-antichymotrypsin in chronic bronchitis and emphysema. J. Biol. Chem. 273: 3695-3701.
7. Chen, J., Lee, K.H., Steinhauer, D.A., Stevens, D.J., Skehel, J.J., and Wiley, D.C. 1998. Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation, Cell 95: 409-417.
8. Deng, G., Curriden, S.A., Wang, S., Rosenberg, S., and Loskutoff, D.J. 1996. Is plasminogen activator inhibitor-1 the molecular switch that governs urokinase receptor-mediated cell adhesion and release? J. Cell Biol. 134: 1563-1571.
9. Egelund, R., Schousboe, S.L., Sottrup-Jensen, L., Rodenburg, K.W., and Andreasen, P.A. 1997. Type-1 plasminogen-activator inhibitor: Conformational differences between latent, active, reactive-centre-cleaved and plasminogen-activator-complexed forms, as probed by proteolytic susceptibility. Eur. J. Biochem. 248: 775-785.
10. 1-antitrypsin. Nat. Struct. Biol. 3: 676-681.
11. Gallagher, T., Gilliland, G., Wang, L., and Bryan, P. 1995. The prosegment-subtilisin BPN′ complex: Crystal structure of a specific 'foldase.' Structure 3: 907-914.
12. Gils, A. and Declerck, P.J. 1997. Proteinase specificity and functional diversity in point mutants of plasminogen activator inhibitor-1. J. Biol. Chem. 272: 12662-12666.
13. Gils, A., Knockaert, I., and Declerck, P.J. 1996. Substrate behavior of plasminogen activator inhibitor-1 is not associated with a lack of insertion of the reactive site loop. Biochemistry 35: 7474-7481.
14. Goldenberg, D.P. 1989. Analysis of protein conformation by gel electrophoresis. In Protein structure: A practical approach (ed. T.E. Creghton), pp. 225-250. IRL Press at Oxford University Press, Oxford, UK.
15. 1-antichymotrypsin indicates two-stage insertion of the reactive loop: Implications for inhibitory function and conformational disease. Proc. Natl. Acad. Sci. 97: 67-72.
16. Hansen, M., Busse, M.N., and Andreasen, P.A. 2001. Importance of the amino-acid composition of the shutter region of plasminogen activator inhibitor-1 for its transitions to latent and substrate forms. Eur. J. Biochem. 268: 6274-6283.
17. Heegaard, C.W., Simonsen, A.C., Oka, K., Kjoller, L., Christensen, A., Madsen, B., Ellgaard, L., Chan, L., and 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.
18. Hekman, C.M. and 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.
19. Holmes, W.E., Lijnen, H.R., Nelles, L., Kluft, C., Nieuwenhuis, H.K., Rijken, D.C., and Collen, D. 1987a. Alpha 2-antiplasmin Enschede: alanine insertion and abolition of plasmin inhibitory activity. Science 238: 209-211.
20. Holmes, W.E., Lijnen, H.R., and Collen, D. 1987b. Characterization of recombinant human 2-antiplasmin and of mutants obtained by site-directed mutagenesis of the reactive site. Biochemistry 26: 5133-5140.
21. 1-antitrypsin for structure and function of serpins. Biochemistry 28: 8951-8966.
22. Huntington, J.A., Read, R.J., and Carrell, R.W. 2000. Structure of a serpinprotease complex shows inhibition by deformation. Nature 407: 923-926.
23. Im, H. and Yu, M.-H. 2000. Conformational switch of the strained native serpin induced by chemical cleavage of the reactive center loop. J. Biochem. Mol. Biol. 33:379-384.
24. Im, H., Ahn, H.-Y., and Yu, M.-H. 2000. Bypassing the kinetic trap of serpin protein folding by loop extension. Protein Sci. 9: 1497-1502.
25. Im, H., Woo, M.S., Hwang, K.Y., and Yu, M.-H. 2002. Interactions causing the kinetic trap in serpin protein folding. J. Biol. Chem. 277: 46347-4654.
26. Jovin, T.M. 1973. Multiphasic zone electrophoresis, IV: Design and analysis of discontinuous buffer systems with a digital computer. Ann. N. Y. Acad. Sci. 209: 477-496.
27. Juhan-Vague, I. and Alessi, M.C. 1997. PAI-1, obesity, insulin resistance and risk of cardiovascular events. Thromb. Haemost. 78: 656-660.
28. Juhan-Vague, I., Valadier, J., Alessi, M.C., Aillaud, M.F., Ansaldi, J., Philip-Joet, C., Holvoet, P., Serradimigni, A., and Collen, D. 1987. Deficient t-PA release and elevated PA inhibitor levels in patients with spontaneous or recurrent deep venous thrombosis. Thromb. Haemost. 57: 67-72.
29. malton, undergoes a spontaneous conformational conversion into a latent form. J. Microbiol. 41: 335-339.
30. Kjøller, L., Martensen, P.M., Sottrup-Jensen, L., Justesen, J., Rodenburg, K.W., and Andreasen, P.A. 1996. Conformational changes of the reactive-centre loop and β-strand 5A accompany temperature-dependent inhibitor-substrate transition of plasminogen-activator inhibitor 1. Eur. J. Biochem. 241: 38-46.
31. Lawrence, D., Strandberg, L., Grundstrom, T., and Ny, T. 1989. Purification of active human plasminogen activator inhibitor-I from Escherichia coli. Comparison with natural and recombinant forms purified from eucaryotic cells. Eur. J. Biochem. 186: 523-533.
32. Lee, H.J. and Im, H. 2003. Purification of recombinant plasminogen activator inhibitor-1 in the active conformation by refolding from inclusion bodies. Protein Expr. Purif. 31: 99-107.
33. Levin, E.G. and Santell, L. 1987. Conversion of the active to latent plasminogen activator inhibitor from human endothelial cells. Blood 70: 1090-1098.
34. 1- antitrypsin. J. Biol. Chem. 270: 5282-5288.
35. Loskutoff, D.J., Sawdey, M., and Mimuro, J. 1989. Type 1 plasminogen activator inhibitor. Prog. Hemost. Thromb. 9: 87-115.
36. Mottonen, J., Strand, A., Symersky, J., Sweet, R.M., Danley, D.E., Geoghegan, K.F., and Goldsmith, E.J. 1992. Structural basis of latency in plasminogen activator inhibitor-1. Nature 355: 270-273.
37. Pace, C.N., Shirley, B.A., and Thomson, J.A. 1989. Measuring the conformational stability of a protein. In Protein structure: A practical approach (ed. T.E. Creghton), pp. 311-330. IRL Press at Oxford University Press, Oxford, UK.
38. Rodenburg, K.W., Kjoller, L., Petersen, H.H., and Andreasen, P.A. 1998. Binding of urokinase-type plasminogen activator-plasminogen activator inhibitor-1 complex to the endocytosis receptors α2-macroglobulin receptor/low-density lipoprotein receptor-related protein and very-low-density lipoprotein receptor involves basic residues in the inhibitor. Biochem. J. 329: 55-63.
39. Sauter, N.K., Mau, T., Rader, S.D., and Agard, D.A. 1998. Structure of a-lytic protease complexed with its pro region. Nature Struct. Biol. 5: 945-950.
40. Schneiderman, J., Sawdey, M.S., Keeton, M.R., Bordin, G.M., Bernstein, E.F., Dilley, R.B., and Loskutoff, D.J. 1992. Increased type 1 plasminogen activator inhibitor gene expression in atherosclerotic human arteries. Proc. Natl. Acad. Sci. 89: 6998-7002.
41. Sharp, A.M., Stein, P.E., Pannu, N.S., Carrell, R.W., Berkenpas, M.B., Ginsburg, D., Lawrence, D.A., and Read, R.J. 1999. The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion. Struct. Fold. Des. 7: 111-118.
42. Stefansson, S. and Lawrence, D.A. 1996. The serpin PAI-1 inhibits cell migration by blocking integrin α V β 3 binding to vitronectin. Nature 383: 441-443.
43. Stein, P.E. and Carrell, R.W. 1995. What do dysfunctional serpins tell us about molecular mobility and disease? Nature Struct. Biol. 2: 96-113.
44. Stoop, A.A., Jespers, L., Lasters, I., Eldering, E., and Pannekoek, H. 2000. Hihg-density mutagenesis by combined DNA 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-1). J. Mol. Biol. 301: 1135-1147.
45. Sui, G.C. and Wiman, B. 1998. Stability of plasminogen activator inhibitor-1: role of tyrosine 221. FEBS Lett. 423: 319-323.
46. Sui, G.C., Mangs, H., and Wiman, B. 1999. The role of His(143) for the pH-dependent stability of plasminogen activator inhibitor-1. Biochim. Biophys. Acta 1434: 58-63.
47. Tucker, H.M., Mottonen, J., Goldsmith, E.J., and Gerard, R.D. 1995. Engineering of plasminogen activator inhibitor-1 to reduce the rate of latency transition. Nat. Struct. Biol. 2: 442-445.
48. van Meijer, M. and Pannekoek, H. 1995. Structure of plasminogen activator inhibitor 1 (PAI-1) and its function in fibrinolysis: An update. Fibrinolysis 9: 263-276.
49. Vaughan, D.E. 1998. Plasminogen activator inhibitor-1: A common denominator in cardiovascular disease. J. Invest. Med. 46: 370-376.
50. Vleugels, N., Gils, A., Bijnens, A.P., Knockaert, I., and Declerck, P.J. 2000. The importance of helix F in plasminogen activator inhibitor-1. Biochim. Biophys. Acta 1476: 20-26.
51. Wang, Z., Mottonen, J., and Goldsmith, E.J. 1996. Kinetically controlled folding of the serpin plasminogen activator inhibitor 1. Biochemistry 35: 16443-16448.
52. Wind, T., Jensen, J.K., Dupont, D.M., Kulig, P., and Andreasen, P.A. 2003. Mutational analysis of plasminogen activator inhibitor-1: Interaction of α-helix F and its neighbouring structural elements regulates the activity and the rate of latency transition. Eur. J. Biochem. 270: 1680-1688.
53. Wright, H.T. and Scarsdale, J.N. 1995. Structural basis for serpin inhibitor activity. Proteins 22: 210-225.