Structural and functional basis of plasminogen activation by staphylokinase

Thrombosis and Haemostasis

Volumn 81, Issue 4, 1999, Pages 479-485

  Jespers, L ^a   Vanwetswinkel, S ^a   Lijnen, H R ^b   Van Herzeele, N ^a   Van Hoef, B ^b   Demarsin, E ^b   Collen, D ^a,b   De Maeyer, M ^a  

^a DEPARTMENT OF PLANT SYSTEMS BIOLOGY   (Belgium)

^b UNIVERSITY OF LEUVEN   (Belgium)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; BACTERIAL PROTEIN; EPITOPE; FIBRINOLYTIC AGENT; PLASMIN; PLASMINOGEN; PROTEINASE INHIBITOR; RECOMBINANT DNA; SERINE PROTEINASE; STAPHYLOKINASE;

ARTICLE; BINDING AFFINITY; COMPLEX FORMATION; CRYSTAL STRUCTURE; HUMAN; MUTAGENESIS; PHAGE DISPLAY; PLASMINOGEN ACTIVATION; PRIORITY JOURNAL; X RAY CRYSTALLOGRAPHY;

EID: 0032951134     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0037-1614509     Document Type: Article

References (38)

1. Collen D, Lijnen HR. Fibrinolysis and the Control of Hemostasis. In: The Molecular Basis of Blood Diseases. Stamatoyannopoulos G, Nienhuis AW, Majerus PW, Varmus H, ads. Philadelphia: W. B. Saunders Co 1994; p. 725-52.
2. Tiliatt WS, Garner RL. Fibrinolytic activity of hemolytic streptococci. J Exp Med 1933; 58: 485-502.
3. Milestone H. A factor in normal human blood which participates in streptococcal fibrinolysis, J Immunol 1941; 42:109-16.
4. Lack CH. Staphylokinase: an activator of plasma protease. Nature 1948; 161: 559-60.
5. Lewis JH, Ferguson JH. A proteolytic enzyme system of the blood. III. Activation of dog serum profibrinolysin by Staphylokinase. Am J Physiol 1951; 166: 594-603.
6. Collen D. Lijnen RH. Staphylokinase, a fibrin-specific plasminogen activator with therapeutic potential? Blood 1994; 84: 680-6.
7. Reddy KNN, Markus G. Mechanism of activation of human plasminogen by streptokinase. Presence of active center in streptokinase-plasminogen complex. J Biol Chem 1972; 247: 1683-91.
8. Summaria L, Wohl RC, Boreisha IG, Robbins KC. A virgin enzyme derived from human plasminogen. Specific cleavage of the arginyl-560-valyl peptide bond in the diisopropoxyphosphinyl virgin enzyme by plasminogen activators. Biochemistry 1982; 21: 2056-9.
9. Rabijns A, De Bondt H, De Ranter C. Three-dimensional structure of staphylokinase, a plasminogen activator with therapeutic potential. Nature Struct Biol 1997; 4: 357-60.
10. Silence K, Hartmann M, Gührs KH, Gase A, Schlott B, Collen D, Lijnen HR. Structure-function relationships in staphylokinase as revealed by "clustered charge to alanine" mutagenesis. J Biol Chem 1995; 270: 27192-8.
11. Schlott B, Gührs KH, Hartmann M, Röcker A, Collen D. NH2-terminal structural motifs in staphylokinase required for plasminogen activation. J Biol Chem 1997; 272: 6067-72.
12. Jespers L, Van Herzeele H, Lijnen HR. Van Hoef B, De Maeyer M, Collen D, Lasters I. Arginine 719 in human plasminogen mediates formation of the staphylokinase:plasmin activator complex. Biochemistry 1998; 37: 6380-6.
13. Lamba D, Bauer M, Huber R, Fischer S, Rudolph R, Kohnert U, Bode W. The 2.3 A crystal structure of the catalytic domain of recombinant two-chain human tissue-type plasminogen activator. J Mol Biol 1996; 258: 117-35.
14. Deutsch DG, Mertz ET. Plasminogen: purification from human plasma by affinity chromatography. Science 1970; 170: 1095-6.
15. Lijnen HR, Van Hoef B, Collen D. Comparative kinetic analysis of the activation of human plasminogen by natural and recombinant single-chain urokinase-type plasminogen activator. Biochim Biophys Acta 1986; 884: 402-8.
16. Lijnen HR, Van Hoef B, Nelles L, Collen D. Plasminogen activation with single-chain urokinase-type plasminogen activator (scu-PA). Studies with active site mutagenized plasminogen (Ser740 to Ala) and plasmin-resistant scu-PA (Lys158 to Glu). J Biol Chem 1990; 265: 5232-6.
17. Silence K, Collen D, Lijnen HR. Interaction between staphylokinase, plasmin(ogen), and alpha 2-antiplasmin. Recycling of staphylokinase after neutralization of the plasmin-staphylokinase complex by alpha 2-antiplasmin. J Biol Chem 1993; 268: 9811-6.
18. Lijnen HR, Lasters I, Verstreken M, Collen D, Jespers L. Screening panels of monoclonal antibodies using phage-displayed antigen. Anal Biochem 1997; 248: 211-5.
19. Claessens M, Van Cutsem E, Lasters I, Wodak S. Modeling the polypeptide backbone with 'spare parts' from known protein structures. Protein Eng 1989; 2: 335-45.
20. Desmet J, De Maeyer M, Hazes B, Lasters I. The dead-end elimination theorem and its use in protein side-chain positioning. Nature 1992; 356: 539-42.
21. Huber R, Kukla D, Bode W, Schwager P, Bartels K, Deisenhofer J, Steigemann W. Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. II. Crystallographic refinement at 1.9 A resolution. J Mol Biol 1974; 89: 73-101.
22. Read RJ, Fujinaga M, Sielecki AR, James MNG. Structure of the complex of Streptomyces griseus protease B and the third domain of the turkey ovomucoid inhibitor at 1.8-Å resolution. Biochemistry 1983; 22: 4420-33.
23. Horton RM, Hunt HD, Ho SN, Pullen JK, Pease LR. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 1989; 77: 61-8.
24. Collen D, De Cock F, Demarsin E, Jenné S, Lasters I, Laroche Y, Wannerdam P, Jespers L. Recombinant staphylokinase variants with altered immunoreactivity. III: Species variability of antibody binding patterns. Circulation 1997; 95: 455-62.
25. Jespers L, Jenné S, Lasters I, Collen D. Epitope mapping by negative selection of randomized antigen libraries displayed on filamentous phage. J Mol Biol 1997; 269: 704-18.
26. Marks JD, Hoogenboom HR, Bonnert TP, McCafferty J, Griffiths AD, Winter G. By-passing immunization. Human antibodies from V-gene libraries displayed on phage. J Mol Biol 1991; 222: 581-97.
27. Spraggon G, Phillips C, Nowak UK, Ponting CP, Saunders D, Dobson CM, Stuart DI, Jones EY. The crystal structure of the catalytic domain of human urokinase-type plasminogen activator. Structure 1995; 3: 681-91.
28. Renatus M, Stubbs MT, Huber R, Bringmann P, Donner P, Schleuning WD, Bode W. Catalytic domain structure of vampire bat plasminogen activator: a molecular paradigm for proteolysis without activation cleavage. Biochemistry 1997; 36: 13483-93.
29. Zhang Y, Wisner A, Maroun RC, Choumet V, Xiong Y, Bon C. Trimeresurus stejnegeri snake venom plasminogen activator. Site-directed mutagenesis and molecular modeling. J Biol Chem 1997; 272: 20531-7.
30. Wang X, Lin X, Loy JA, Tang J, Zhang X. Crystal structure of the catalytic domain of human plasmin complexed with streptokinase. Science 1998; 281: 1662-5.
31. Dawson KM, Marshall JM, Raper RH, Gilbert RJ, Ponting CP. Substitution of arginine 719 for glutamic acid in human plasminogen substantially reduces its affinity for streptokinase. Biochemistry 1994; 33: 12042-7.
32. Lijnen HR, De Cock F, Van Hoef B, Schlott B, Collen D. Characterization of the interaction between plasminogen and staphylokinase. Eur J Biochem 1994; 224: 143-9.
33. Shieh HS, Kurumbail RG, Stevens AM, Stegeman RA, Sturman EJ, Pak JY, Wittwer AJ, Palmier MO, Wiegand RC, Holwerda BC, Stallings WC. Three-dimensional structure of human cytomegalovirus protease. Nature 1996; 383: 279-82.
34. Jespers L, Vanwetswinkel S, Lijnen HR, Van Herzeele N, Collen D, De Maeyer M. Interface scanning and 3D model of the staphylokinase:plasmin activator complex. Fibrinol Proteol 1998; 12 (Suppl 1): 4 (abstract 5).
35. Parry MAA, Fernandez-Catalan C, Bergner A, Huber R, Hopfner KP, Schlott B, Gührs KH, Bode W. The ternary microplasmin-staphylokinase-microplasmin complex is a proteinase-cofactor-substrate complex in action. Nature Struct Biol 1998; 5: 917-23.
36. Nicholls A, Sharp KA, Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct Funct Genet 1991; 11: 281-96.
37. Koradi R, Billeter M, Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graphics 1996; 14: 51-5.
38. Kabsch W, Sander C. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983; 22: 2577-637.