Table of Contents Author Guidelines Submit a Manuscript
BioMed Research International
Volume 2017, Article ID 5130495, 10 pages
https://doi.org/10.1155/2017/5130495
Research Article

Structure and Function of Trypsin-Loaded Fibrinolytic Liposomes

1Department of Medical Biochemistry, Semmelweis University, Budapest, Hungary
2IMEC, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, Hungary

Correspondence should be addressed to Krasimir Kolev; uh.etos.koe@velok.rimisark

Received 3 February 2017; Revised 12 April 2017; Accepted 4 May 2017; Published 3 July 2017

Academic Editor: Zsuzsa Bagoly

Copyright © 2017 Anna Tanka-Salamon 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. H. P. Adams Jr., G. del Zoppo, M. J. Alberts et al., “Guidelines for the early management of adults with ischemic stroke: a guideline from the American Heart Association/American Stroke Association Stroke Council, Clinical Cardiology Council, Cardiovascular Radiology and Intervention Council, and the atherosclerotic peripheral vascular disease and quality of care outcomes in research interdisciplinary working groups: the American Academy of Neurology affirms the value of this guideline as an educational tool for neurologists,” Circulation, vol. 115, no. 20, pp. 478–534, 2007. View at Publisher · View at Google Scholar · View at Scopus
  2. P. W. Armstrong, A. H. Gershlick, P. Goldstein et al., “Fibrinolysis or primary PCI in ST-segment elevation myocardial infarction,” New England Journal of Medicine, vol. 368, no. 15, pp. 1379–1387, 2013. View at Publisher · View at Google Scholar · View at Scopus
  3. V. J. Marder and D. Stewart, “Towards safer thrombolytic therapy,” Seminars in Hematology, vol. 39, no. 3, pp. 206–216, 2002. View at Publisher · View at Google Scholar · View at Scopus
  4. V. J. Marder and V. Novokhatny, “Direct fibrinolytic agents: Biochemical attributes, preclinical foundation and clinical potential,” Journal of Thrombosis and Haemostasis, vol. 8, no. 3, pp. 433–444, 2010. View at Publisher · View at Google Scholar · View at Scopus
  5. R. Bashir, C. J. Zack, H. Zhao, A. J. Comerota, and A. A. Bove, “Comparative outcomes of catheter-directed thrombolysis plus anticoagulation vs anticoagulation alone to treat lower-extremity proximal deep vein thrombosis,” Journal of the American Medical Association Internal Medicine, vol. 174, no. 9, pp. 1494–1501, 2014. View at Publisher · View at Google Scholar · View at Scopus
  6. A. A. Manzoor, L. H. Lindner, C. D. Landon et al., “Overcoming limitations in nanoparticle drug delivery: triggered, intravascular release to improve drug penetration into tumors,” Cancer Research, vol. 72, no. 21, pp. 5566–5575, 2012. View at Publisher · View at Google Scholar · View at Scopus
  7. B. Kneidl, M. Peller, G. Winter, L. H. Lindner, and M. Hossann, “Thermosensitive liposomal drug delivery systems: state of the art review,” International Journal of Nanomedicine, vol. 16, no. 9, pp. 4387–4398, 2014. View at Publisher · View at Google Scholar · View at Scopus
  8. E. Komorowicz, K. Kolev, and R. Machovich, “Fibrinolysis with des-kringle derivatives of plasmin and its modulation by plasma protease inhibitors,” Biochemistry, vol. 37, no. 25, pp. 9112–9118, 1998. View at Publisher · View at Google Scholar · View at Scopus
  9. K. Kolev, I. Léránt, K. Tenekejiev, and R. Machovich, “Regulation of fibrinolytic activity of neutrophil leukocyte elastase, plasmin, and miniplasmin by plasma protease inhibitors,” Journal of Biological Chemistry, vol. 269, no. 25, pp. 17030–17034, 1994. View at Google Scholar · View at Scopus
  10. R. L. Lundblad, H. S. Kingdon, and K. G. Mann, “[14] Thrombin,” Methods in Enzymology, vol. 45, pp. 156–176, 1976. View at Publisher · View at Google Scholar · View at Scopus
  11. C. Longstaff, M.-Y. Wong, and P. J. Gaffney, “An international collaborative study to investigate standardisation of hirudin potency,” Thrombosis and Haemostasis, vol. 69, no. 5, pp. 430–435, 1993. View at Google Scholar · View at Scopus
  12. P. Jouanel, C. Motta, J. Delattre, and B. Dastugue, “A rapid and sensitive fluorometric assay of serum phospholipid,” Clinica Chimica Acta, vol. 105, no. 2, pp. 173–181, 1980. View at Publisher · View at Google Scholar · View at Scopus
  13. T. Sugo, H. Endo, M. Matsuda et al., “A classification of the fibrin network structures formed from the hereditary dysfibrinogens,” Journal of Thrombosis and Haemostasis, vol. 4, no. 8, pp. 1738–1746, 2006. View at Publisher · View at Google Scholar · View at Scopus
  14. A. Lorenzen and S. W. Kennedy, “A fluorescence-based protein assay for use with a microplate reader,” Analytical Biochemistry, vol. 214, no. 1, pp. 346–348, 1993. View at Publisher · View at Google Scholar · View at Scopus
  15. A. Wacha, Z. Varga, and A. Bóta, “CREDO: a new general-purpose laboratory instrument for small-angle X-ray scattering,” Journal of Applied Crystallography, vol. 47, no. 5, pp. 1749–1754, 2014. View at Publisher · View at Google Scholar · View at Scopus
  16. R. Deák, J. Mihály, I. C. Szigyártó, A. Wacha, G. Lelkes, and A. Bóta, “Physicochemical characterization of artificial nanoerythrosomes derived from erythrocyte ghost membranes,” Colloids and Surfaces B: Biointerfaces, vol. 135, pp. 225–234, 2015. View at Publisher · View at Google Scholar · View at Scopus
  17. O. Glatter and O. Kratky, Small Angle X-Ray Scattering, Academic Press, New York, NY, USA, 1982.
  18. L. A. Feigin and D. I. Svergun, Structure Analysis by Small-Angle X-Ray and Neutron Scattering, Plenum Press, New York, NY, USA, 1987.
  19. A. Guinier and G. Fournet, Small-Angle Scattering of X-Rays, John Wiley & Sons Inc, New York, NY, USA, 1955.
  20. A. Blicher, K. Wodzinska, M. Fidorra, M. Winterhalter, and T. Heimburg, “The temperature dependence of lipid membrane permeability, its quantized nature, and the influence of anesthetics,” Biophysical Journal, vol. 96, no. 11, pp. 4581–4591, 2009. View at Publisher · View at Google Scholar · View at Scopus
  21. B. Smith, I. Lyakhov, K. Loomis et al., “Hyperthermia-triggered intracellular delivery of anticancer agent to HER2+ cells by HER2-specific affibody (ZHER2-GS-Cys)-conjugated thermosensitive liposomes (HER2 + affisomes),” Journal of Controlled Release, vol. 153, no. 2, pp. 187–194, 2011. View at Publisher · View at Google Scholar · View at Scopus
  22. B. J. Wood, J. K. Locklin, A. Viswanathan et al., “Technologies for Guidance of Radiofrequency Ablation in the Multimodality Interventional Suite of the Future,” Journal of Vascular and Interventional Radiology, vol. 18, no. 1, pp. 9–24, 2007. View at Publisher · View at Google Scholar · View at Scopus
  23. V. Saxena, C. G. Johnson, A. H. Negussie, K. V. Sharma, M. R. Dreher, and B. J. Wood, “Temperature-sensitive liposome-mediated delivery of thrombolytic agents,” International Journal of Hyperthermia, vol. 31, no. 1, pp. 67–73, 2015. View at Publisher · View at Google Scholar · View at Scopus
  24. Y. F. Zhou, “High intensity focused ultrasound in clinical tumor ablation,” World Journal of Clinical Oncology, vol. 2, no. 1, pp. 8–27, 2011. View at Publisher · View at Google Scholar
  25. P. R. Stauffer, P. MacCarini, K. Arunachalam et al., “Conformal microwave array (CMA) applicators for hyperthermia of diffuse chest wall recurrence,” International Journal of Hyperthermia, vol. 26, no. 7, pp. 686–698, 2010. View at Publisher · View at Google Scholar · View at Scopus
  26. R. Gref, M. Lück, P. Quellec et al., “‘Stealth’ corona-core nanoparticles surface modified by polyethylene glycol (PEG): Influences of the corona (PEG chain length and surface density) and of the core composition on phagocytic uptake and plasma protein adsorption,” Colloids and Surfaces B: Biointerfaces, vol. 18, no. 3-4, pp. 301–313, 2000. View at Publisher · View at Google Scholar · View at Scopus
  27. J. M. M. Caaveiro, A. Molina, P. Rodríguez-Palenzuela, F. M. Goñi, and J. M. González-Mañas, “Interaction of wheat α-thionin with large unilamellar vesicles,” Protein Science, vol. 7, no. 12, pp. 2567–2577, 1998. View at Publisher · View at Google Scholar · View at Scopus
  28. R. D. Klausner, N. Kumar, J. N. Weinstein, R. Blumenthal, and M. Flavin, “Interaction of tubulin with phospholipid vesicles. I. Association with vesicles at the phase transition,” The Journal of Biological Chemistry, vol. 256, no. 11, pp. 5879–5885, 1981. View at Google Scholar
  29. S. Horkovics-Kovats and P. Traub, “A mathematical model for protein-induced lipid vesicle leakage: interaction of the intermediate filament protein vimentin and its isolated N-terminus with phosphatidylinositol vesicles,” Journal of Theoretical Biology, vol. 153, no. 1, pp. 89–110, 1991. View at Publisher · View at Google Scholar · View at Scopus
  30. N. V. Bogatcheva and N. B. Gusev, “Interaction of smooth muscle calponin with phospholipids,” FEBS Letters, vol. 371, no. 2, pp. 123–126, 1995. View at Publisher · View at Google Scholar · View at Scopus
  31. G. S. Retzinger, “Adsorption and coagulability of fibrinogen on atheromatous lipid surfaces,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 15, no. 6, pp. 786–792, 1995. View at Publisher · View at Google Scholar · View at Scopus
  32. M. T. Cunningham, B. A. Citron, and T. A. W. Koerner, “Evidence of a phospholipid binding species within human fibrinogen preparations,” Thrombosis Research, vol. 95, no. 6, pp. 325–334, 1999. View at Publisher · View at Google Scholar · View at Scopus
  33. S. Talens, J. J. M. C. Malfliet, P. T. W. van Hal, F. W. G. Leebeek, and D. C. Rijken, “Identification and characterization of α1-antitrypsin in fibrin clots,” Journal of Thrombosis and Haemostasis, vol. 11, no. 7, pp. 1319–1328, 2013. View at Publisher · View at Google Scholar · View at Scopus
  34. D. L. Sauls, M. Warren, and M. Hoffman, “Homocysteinylated fibrinogen forms disulfide-linked complexes with albumin,” Thrombosis Research, vol. 127, no. 6, pp. 576–581, 2011. View at Publisher · View at Google Scholar · View at Scopus
  35. Z. Rottenberger, E. Komorowicz, L. Szabó et al., “Lytic and mechanical stability of clots composed of fibrin and blood vessel wall components,” Journal of Thrombosis and Haemostasis, vol. 11, no. 3, pp. 529–538, 2013. View at Publisher · View at Google Scholar · View at Scopus
  36. I. Varjú, P. Sótonyi, R. Machovich et al., “Hindered dissolution of fibrin formed under mechanical stress,” Journal of Thrombosis and Haemostasis, vol. 9, no. 5, pp. 979–986, 2011. View at Publisher · View at Google Scholar · View at Scopus
  37. H. W. Meyer and W. Richter, “Freeze-fracture studies on lipids and membranes,” Micron, vol. 32, no. 6, pp. 615–644, 2001. View at Publisher · View at Google Scholar · View at Scopus
  38. S. J. Prestrelski, D. M. Byler, and M. N. Liebman, “Comparison of various molecular forms of bovine trypsin: correlation of infrared spectra with X-ray crystal structures,” Biochemistry, vol. 30, no. 1, pp. 133–143, 1991. View at Publisher · View at Google Scholar · View at Scopus
  39. R. N. A. H. Lewis and R. N. McElhaney, “Membrane lipid phase transitions and phase organization studied by Fourier transform infrared spectroscopy,” Biochimica et Biophysica Acta - Biomembranes, vol. 1828, no. 10, pp. 2347–2358, 2013. View at Publisher · View at Google Scholar · View at Scopus
  40. S. L. Diamond and S. Anand, “Inner clot diffusion and permeation during fibrinolysis,” Biophysical Journal, vol. 65, no. 6, pp. 2622–2643, 1993. View at Publisher · View at Google Scholar · View at Scopus
  41. S. Anand, J. Wu, and S. L. Diamond, “Enzyme‐mediated proteolysis of fibrous biopolymers: Dissolution front movement in fibrin or collagen under conditions of diffusive or convective transport,” Biotechnology and Bioengineering, vol. 48, no. 2, pp. 89–107, 1995. View at Publisher · View at Google Scholar · View at Scopus