Role of the 88-97 loop in plasminogen activation by streptokinase probed through site-specific mutagenesis

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1784, Issue 9, 2008, Pages 1310-1318

  Yadav, Suman ^a   Datt, Manish ^a   Singh, Balvinder ^a   Sahni, Girish ^a  

^a INSTITUTE OF MICROBIAL TECHNOLOGY   (India)

Author keywords

Enzyme substrate interaction; Human plasminogen activation; Plasminogen activator; Protein protein interaction; Streptokinase

Indexed keywords

PLASMIN; PLASMINOGEN; STREPTOKINASE; PRIMER DNA; RECOMBINANT PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; CATALYSIS; CONFORMATIONAL TRANSITION; DELETION MUTANT; ENZYME SPECIFICITY; ENZYME SUBSTRATE; KRINGLE DOMAIN; PLASMINOGEN ACTIVATION; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN METABOLISM; PROTEIN PROTEIN INTERACTION; SITE DIRECTED MUTAGENESIS; SURFACE PLASMON RESONANCE; WILD TYPE; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; GENE DELETION; GENETICS; HUMAN; IN VITRO STUDY; KINETICS; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PROTEIN TERTIARY STRUCTURE; THERMODYNAMICS;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BASE SEQUENCE; CATALYTIC DOMAIN; DNA PRIMERS; ENZYME ACTIVATION; HUMANS; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PLASMINOGEN; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; SEQUENCE DELETION; STREPTOKINASE; THERMODYNAMICS;

EID: 53149145987     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.05.013     Document Type: Article

References (41)

1. M.A. Parry, X.C. Zhang, I. Bode, Molecular mechanisms of plasminogen activation: bacterial cofactors provide clues, Trends Biochem. Sci. 25 (2000) 53-59.
2. H.R. Lijnen, Elements of the fibrinolytic system, Ann. N. Y. Acad. Sci. 36 (2001) 226-236.
3. P. Wallen, B. Wiman, Characterization of human plasminogen. I. On the relationship between different molecular forms of plasminogen demonstrated in plasma and found in purified preparations, Biochim. Biophys. Acta 221 (1970) 20-30.
4. D. Collen, Staphylokinase: a potent, uniquely fibrin-selective thrombolytic agent, Nat. Med 4 (1998) 279-284.
5. F.J. Castellino, Recent advances in the chemistry of the fibrinolytic system, Chem. Rev. 81 (1981) 431-446.
6. C.T. Esmon, T. Mather, Switching serine protease specificity, Nat. Struct. Biol. 5 (1998) 933-937.
7. ISIS-3 (Third International Study of Infarct Survival) Collaborative Group, A randomized comparison of streptokinase vs tissue plasminogen activator vs anistreplase and of aspirin plus heparin vs aspirin alone among 41229 cases of suspected acute myocardial infarction, Lancet 339 (1992) 753-770.
8. P.E. Battershill, P. Benfield, K.L. Goa, Streptokinase. A review of its pharmacology and therapeutic efficacy in acute myocardial infarction in older patients, Drugs Aging 4 (1994) 83-86.
9. V.J. Marder, Recombinant streptokinase: opportunity for an improved agent, Blood Coagul. Fibrinolysis 4 (1993) 1039-1040.
10. F. Conejero-Lara, J. Parrado, A.I. Azuaga, R.A. Smith, C.P. Ponting, C.M. Dobson, Thermal stability of the three domains of streptokinase studied by circular dichroism and nuclear magnetic resonance, Protein Sci. 5 (1996) 2583-2591.
11. J. Parrado, F. Conejero-Lara, R.A. Smith, J.M. Marshall, C.P. Ponting, C.M. Dobson, The domain organization of streptokinase: nuclear magnetic resonance, circular dichroism, and functional characterization of proteolytic fragments, Protein Sci. 5 (1996) 693-704.
12. G. Markus, W.C. Werkheiser, The interaction of streptokinase with plasminogen. Functional properties of the activated enzyme, J. Biol. Chem. 239 (1964) 2637-2643.
13. L. Summaria, B. Hsieh, K.C. Robbins, The specific mechanism of activation of human plasminogen to plasmin, J. Biol. Chem. 242 (1967) 4279-4283.
14. D. Nihalani, G. Sahni, Streptokinase contains two independent plasminogen-binding sites, Biochem. Biophys. Res. Commun. 217 (1995) 1245-1254.
15. G.Y. Shi, B.I. Change, D.H. Wu, Y.M. Ha, H.L. Wu, Activation of human and bovine plasminogens by the microplasmin and streptokinase complex, Thromb. Res. 58 (1990) 317-329.
16. X. Wang, X. Lin, J.A. Loy, J. Tang, X.C. Zhang, Crystal structure of the catalytic domain of human plasmin complexed with streptokinase, Science 281 (1998) 1662-1665.
17. J. Dhar, A.H. Pande, V. Sundram, J.S. Nanda, S.C. Mande, G. Sahni, Involvement of a nine-residue loop of streptokinase in the generation of macromolecular substrate specificity by the activator complex through interaction with substrate kringle domains, J. Biol. Chem. 277 (2002) 13257-13267.
18. D.G. Deutsch, E.T. Mertz, Plasminogen: purification from human plasma by affinity chromatography, Science 170 (1970) 1095-1096.
19. D. Nihalani, G.P.S. Raghava, G. Sahni, Mapping of the plasminogen binding site of streptokinase with short synthetic peptides, Protein Sci. 6 (1997) 1284-1292.
20. V. Sundram, Structure-function studies of streptokinase, PhD thesis, Jawaharlal Nehru University, New Delhi, India, 2002.
21. D.A. Case, T.A. Darden, T.E. Cheatham III, C.L. Simmerling, J. Wang, R.E. Duke, R. Luo, K.M. Merz, B. Wang, D.A. Pearlman, M. Crowley, S. Brozell, V. Tsui, H. Gohlke, J. Mongan, V. Hornak, G. Cui, P. Beroza, C. Schafmeister, J.W. Caldwell, W.S. Ross, P.A. Kollman, AMBER 8, University of California, San Francisco, 2004.
22. W.L. DeLano, The PyMOL Molecular Graphics System, DeLano Scientific, San Carlos, CA, USA. http://www.pymol.org, 2002.
23. G.D. Hawkins, C.J. Cramer, D.G. Truhlar, Pairwise solute descreening of solute charges from a dielectric medium, Chem. Phys. Lett. 246 (1995) 122-129.
24. W. Humphrey, A. Dalke, K. Schulten, VMD - visual molecular dynamics, J. Molec. Graphics 14 (1996) 33-38.
25. G.Y. Shi, H.L. Wu, Isolation and characterization of microplasminogen. A low molecular weight form of plasminogen, J. Biol. Chem. 263 (1988) 17071-17075.
26. K.W. Jackson, N. Esmon, J. Tang, Streptokinase and staphylokinase, Methods Enzymol. 80 (1981) 387-394.
27. R.C. Wohl, L. Summaria, K.C. Robbins, Kinetics of activation of human plasminogen by different activator species at pH 7.4 and 37 degrees C, J. Biol. Chem. 255 (1980) 2005-2013.
28. T. Chase Jr., E. Shaw, Comparison of the esterase activities of trypsin, plasmin, and thrombin on guanidinobenzoate esters, titration of the enzymes, Biochemistry 8 (1969) 2212-2224.
29. D.K. McClintock, P.H. Bell, The mechanism of activation of human plasminogen by streptokinase, Biochem. Biophys. Res. Commun. 43 (1971) 694-702.
30. R.C. Wohl, Interference of active site specific reagents in plasminogen-streptokinase active site formation, Biochemistry 23 (1984) 3799-3804.
31. R. Cush, J.M. Cronin, W.J. Stewart, C.H. Maule, J. Molloy, N.J. Goddard, The resonant mirror: a novel optical biosensor for direct sensing of biomolecular interactions. Part I: principle of operation and associated instrumentation, Biosensors & Bioelectronics 8 (1993) 347-354.
32. P.E. Buckle, R.J. Davies, T. Kinning, D. Yeung, P.R. Edwards, D. Pollard-Knight, C.R. Lowe, The resonant mirror: a novel optical biosensor for direct sensing of biomolecular interactions Part II: applications, Biosensors & Bioelectronics 8 (1993) 365-370.
33. F. Conejero-Lara, J. Parrado, A.I. Azuaga, C.M. Dobson, C.P. Ponting, Analysis of the interactions between streptokinase domains and human plasminogen, Protein Sci. 7 (1998) 2190-2199.
34. D.G. Myszka, Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors, Curr. Opin. Biotechnol. 8 (1997) 50-57.
35. T.A. Morton, D.G. Myszka, I.M. Chaiken, Interpreting complex binding kinetics from optical biosensors: a comparison of analysis by linearization, the integrated rate equation, and numerical integration, Anal. Biochem. 227 (1995) 176-185.
36. V. Sundram, J.S. Nanda, K. Rajagopal, J. Dhar, A. Chaudhary, G. Sahni, Domain truncation studies reveal that the streptokinase-plasmin activator complex utilizes long range protein-protein interactions with macromolecular substrate to maximize catalytic turnover, J. Biol. Chem. 278 (2003) 30569-30577.
37. L.F. Lin, A. Houng, G.L. Reed, Epsilon amino caproic acid inhibits streptokinase-plasminogen activator complex formation and substrate binding through kringle-dependent mechanisms, Biochemistry 39 (2000) 4740-4745.
38. P.Y. Chou, G.D. Fasman, Beta-turns in proteins, J. Mol. Biol. 115 (1977) 135-175.
39. J.A. Loy, X. Lin, M. Schenone, F.J. Castellino, X.C. Zhang, J. Tang, Domain interactions between streptokinase and human plasminogen, Biochemistry 40 (2001) 14686-14695.
40. R.C. Wohl, L. Arzadon, L. Summaria, K.C. Robbins, Comparison of the esterase and human plasminogen activator activities of various activated forms of human plasminogen and their equimolar streptokinase complexes, J. Biol. Chem. 252 (1977) 1141-1147.
41. M.A. Parry, C. Fernandez-Catalan, A. Bergner, R. Huber, K.P. Hopfner, B. Schlott, K.H. Guhrs, W. Bode, The ternary microplasmin-staphylokinase- microplasmin complex is a proteinase-cofactor-substrate complex in action, Nat. Struct. Biol. 5 (1998) 917-923.