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BioMed Research International
Volume 2013 (2013), Article ID 297305, 12 pages
http://dx.doi.org/10.1155/2013/297305
Research Article

In Vitro Characterization of a Multifunctional Staphylokinase Variant with Reduced Reocclusion, Produced from Salt Inducible E. coli GJ1158

1Centre for Bioseparation Technology, VIT University, Vellore 632014, Tamilnadu, India
2Department of Biotechnology, Acharya Nagarjuna University, Nagarjuna Nagar, Guntur 522510, Andhra Pradesh, India
3Interdisciplinary Graduate Program in Human Toxicology, University of Iowa, Iowa City, IA 52242, USA
4Department of Occupational and Environmental Health, The University of Iowa, College of Public Health, 100 Oakdale Campus No. 121 IREH, Iowa City, IA 52242-5000, USA

Received 22 April 2013; Revised 19 June 2013; Accepted 3 July 2013

Academic Editor: Eileen Hao Yu

Copyright © 2013 K. K. Pulicherla et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. M. Nichols, N. Townsend, P. Scarborough, et al., European Cardiovascular Disease Statistics 2012, European Heart Network, European Society of Cardiology, Brussels, Belgium, 2012.
  2. A. T. Cohen, G. Agnelli, F. A. Anderson et al., “Venous thromboembolism (VTE) in Europe—the number of VTE events and associated morbidity and mortality,” Thrombosis and Haemostasis, vol. 98, no. 4, pp. 756–764, 2007. View at Publisher · View at Google Scholar · View at Scopus
  3. H. J. Rapold, “Promotion of thrombin activity by thrombolytic therapy without simultaneous anticoagulation,” The Lancet, vol. 335, no. 8687, pp. 481–482, 1990. View at Scopus
  4. K. Serizawa, T. Urano, Y. Kozima, Y. Takada, and A. Takada, “The potential role of platelet PAI-1 in t-PA mediated clot lysis of platelet rich plasma,” Thrombosis Research, vol. 71, no. 4, pp. 289–300, 1993. View at Publisher · View at Google Scholar · View at Scopus
  5. K. Ghandehari, “Barriers of thrombolysis therapy in developing countries,” Stroke Research and Treatment, vol. 2011, Article ID 686797, 4 pages, 2011. View at Publisher · View at Google Scholar · View at Scopus
  6. M. I. Bokarewa, T. Jin, and A. Tarkowski, “Staphylococcus aureus: staphylokinase,” International Journal of Biochemistry and Cell Biology, vol. 38, no. 4, pp. 504–509, 2006. View at Publisher · View at Google Scholar · View at Scopus
  7. S. C. Wu, F. J. Castellino, and S. L. Wong, “A fast-acting, modular-structured staphylokinase fusion with Kringle-1 from human plasminogen as the fibrin-targeting domain offers improved clot lysis efficacy,” The Journal of Biological Chemistry, vol. 278, no. 20, pp. 18199–18206, 2003. View at Publisher · View at Google Scholar · View at Scopus
  8. S. J. Szarka, E. G. Sihota, H. R. Habibi, and S. Wong, “Staphylokinase as a plasminogen activator component in recombinant fusion proteins,” Applied and Environmental Microbiology, vol. 65, no. 2, pp. 506–513, 1999. View at Scopus
  9. R. G. Miele, M. Prorok, V. A. Costa, and F. J. Castellino, “Glycosylation of asparagine-28 of recombinant staphylokinase with high-mannose-type oligosaccharides results in a protein with highly attenuated plasminogen activator activity,” The Journal of Biological Chemistry, vol. 274, no. 12, pp. 7769–7776, 1999. View at Publisher · View at Google Scholar · View at Scopus
  10. D. V. Sakharov, H. R. Lijnen, and D. C. Rijken, “Interactions between staphylokinase, plasmin(ogen), and fibrin. Staphylokinase discriminates between free plasminogen and plasminogen bound to partially degraded fibrin,” The Journal of Biological Chemistry, vol. 271, no. 44, pp. 27912–27918, 1996. View at Publisher · View at Google Scholar · View at Scopus
  11. T. Yamada, Y. Shimada, and M. Kikuchi, “Integrin-specific tissue-type plasminogen activator engineered by introduction of the Arg-Gly-Asp sequence,” Biochemical and Biophysical Research Communications, vol. 228, no. 2, pp. 306–311, 1996. View at Publisher · View at Google Scholar · View at Scopus
  12. Y. Pal, J. C. Gupta, and K. J. Mukherjee, “Optimizing recombinant protein expression in the T7 system under the control of the proUp promoter,” Biotechnology Letters, vol. 23, no. 1, pp. 41–46, 2001. View at Publisher · View at Google Scholar · View at Scopus
  13. J. Gowrishankar and D. Manna, “How is osmotic regulation of transcription of the Escherichia coli proU operon achieved? A review and a model,” Genetica, vol. 97, no. 3, pp. 363–378, 1996. View at Scopus
  14. B. Choi, P. Bobrowicz, R. C. Davidson et al., “Use of combinatorial genetic libraries to humanize N-linked glycosylation in the yeast Pichia pastoris,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 9, pp. 5022–5027, 2003. View at Publisher · View at Google Scholar · View at Scopus
  15. J. M. Cregg, T. S. Vedvick, and W. C. Raschke, “Recent advances in the expression of foreign genes in Pichia pastoris,” Bio/Technology, vol. 11, no. 8, pp. 905–910, 1993. View at Publisher · View at Google Scholar · View at Scopus
  16. P. Bhandari and J. Gowrishankar, “An Escherichia coli host strain useful for efficient overproduction of cloned gene products with NaCl as the inducer,” Journal of Bacteriology, vol. 179, no. 13, pp. 4403–4406, 1997. View at Scopus
  17. J. Szemraj, B. Walkowiak, I. Kawecka et al., “A new recombinant thrombolytic and antithrombotic agent with higher fibrin affinity—a staphylokinase variant. I. In vitro study,” Journal of Thrombosis and Haemostasis, vol. 3, no. 10, pp. 2156–2165, 2005. View at Publisher · View at Google Scholar · View at Scopus
  18. M. Kowalski, G. Brown, M. Bieniasz et al., “Cloning and expression of a new recombinant thrombolytic and anthithrombotic agent—a staphylokinase variant,” Acta Biochimica Polonica, vol. 56, no. 1, pp. 41–53, 2009. View at Scopus
  19. M. Wang, Y. Wang, J. Wang et al., “Construction and characterization of a novel staphylokinase variant with thrombin-inhibitory activity,” Biotechnology Letters, vol. 31, no. 12, pp. 1923–1927, 2009. View at Publisher · View at Google Scholar · View at Scopus
  20. N. V. Thrombogenics, 2012, http://www.thrombogenics.com/.
  21. K. K. Pulicherla, G. S. Gadupudi, V. P. B. Rekha, K. Seetharam, A. Kumar, and K. R. S. S. Rao, “Isolation, cloning and expression of mature staphylokinase from lysogenic Staphylococcus aureus collected from a local wound sample in a salt inducible E. coli expression host,” International Journal of Advanced Science and Technology, vol. 30, pp. 35–42, 2011.
  22. J. Sambrook and D. W. Russel, Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, New York, NY, USA, 2001.
  23. U. K. Laemmli, “Cleavage of structural proteins during the assembly of the head of bacteriophage T4,” Nature, vol. 227, no. 5259, pp. 680–685, 1970. View at Publisher · View at Google Scholar · View at Scopus
  24. O. H. Lowry, N. J. Rosebrough, A. L. Farr, and R. J. Randall, “Protein measurement with the Folin phenol reagent,” The Journal of Biological Chemistry, vol. 193, no. 1, pp. 265–275, 1951. View at Scopus
  25. L. A. Devriese and A. van de Kerckhove, “A comparison of methods used for testing staphylokinase (fibrinolysin) production in Staphylococcus strains,” Antonie van Leeuwenhoek, vol. 46, no. 5, pp. 457–465, 1980. View at Scopus
  26. T. Astrup and I. Stendorff, “A fibrinolytic system in human milk,” Proceedings of the Society for Experimental Biology and Medicine, vol. 84, no. 3, pp. 605–608, 1953. View at Scopus
  27. Q. Bi, X. Cen, Y. Huang, and S. Zhu, “Construction and characterization of trifunctional single-chain urokinase-type plasminogen activators. Trifunctional plasminogen activators,” European Journal of Biochemistry, vol. 269, no. 6, pp. 1708–1713, 2002. View at Publisher · View at Google Scholar · View at Scopus
  28. T. Trieu, D. Behnke, D. Gerlach, and J. Tang, “Activation of human plasminogen by recombinant staphylokinase,” Methods in Enzymology, vol. 223, pp. 156–167, 1993. View at Publisher · View at Google Scholar · View at Scopus
  29. K. W. Jackson, N. Esmon, and J. Tang, “Streptokinase and staphylokinase,” Methods in Enzymology, vol. 80, pp. 387–394, 1981. View at Publisher · View at Google Scholar · View at Scopus
  30. B. Schlott, K. H. Gührs, M. Hartmann, A. Röcker, and D. Collen, “Staphylokinase requires NH2-terminal proteolysis for plasminogen activation,” The Journal of Biological Chemistry, vol. 272, no. 9, pp. 6067–6072, 1997. View at Publisher · View at Google Scholar · View at Scopus
  31. D. Collen, B. Schlott, Y. Engelborghs et al., “On the mechanism of the activation of human plasminogen by recombinant staphylokinase,” The Journal of Biological Chemistry, vol. 268, no. 11, pp. 8284–8289, 1993. View at Scopus
  32. E. Lacoste, I. Martineau, and G. Gagnon, “Platelet concentrates: effects of calcium and thrombin on endothelial cell proliferation and growth factor release,” Journal of Periodontology, vol. 74, no. 10, pp. 1498–1507, 2003. View at Publisher · View at Google Scholar · View at Scopus
  33. L. Zhang, J. Wang, M. Yu, and B. Ru, “Functional properties of a recombinant chimeric plasminogen activator with platelet-targeted fibrinolytic and anticoagulant potential,” Molecular Genetics and Metabolism, vol. 82, no. 4, pp. 304–311, 2004. View at Publisher · View at Google Scholar · View at Scopus
  34. A. Challen, W. J. Branch, and J. H. Cummings, “Quantitation of platelet mass during aggregation in the electronic (wellcome) whole blood aggregometer,” Journal of Pharmacological Methods, vol. 8, no. 2, pp. 115–122, 1982. View at Scopus
  35. J. M. Maraganore and B. A. Adelman, “Hirulog: a direct thrombin inhibitor for management of acute coronary syndromes,” Coronary Artery Disease, vol. 7, no. 6, pp. 438–448, 1996. View at Scopus