Table of Contents Author Guidelines Submit a Manuscript
BioMed Research International
Volume 2014, Article ID 920942, 7 pages
http://dx.doi.org/10.1155/2014/920942
Research Article

Purification and Characterization of BmooAi: A New Toxin from Bothrops moojeni Snake Venom That Inhibits Platelet Aggregation

1Instituto de Genética e Bioquímica, Universidade Federal de Uberlândia, 38400-902 Uberlândia, MG, Brazil
2Instituto Nacional de Ciência e Tecnologia em Nano-Biofarmacêutica (N-Biofar), 31270-901 Belo Horizonte, MG, Brazil
3Instituto de Ciências Biomédicas, Universidade Federal de Uberlândia, 38400-902 Uberlândia, MG, Brazil
4Centro de Estudos de Biomoléculas Aplicadas à Saúde (CEBio), Fundação Oswaldo Cruz Rondônia (Fiocruz Rondônia) e Núcleo de Saúde, Universidade Federal de Rondônia (UNIR), 76812-245 Porto Velho, RO, Brazil

Received 1 March 2014; Revised 5 May 2014; Accepted 6 May 2014; Published 29 May 2014

Academic Editor: Phillip I. Bird

Copyright © 2014 Mayara Ribeiro de Queiroz 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. E. M. Singletary, A. S. Rochman, J. C. A. Bodmer, and C. P. Holstege, “Envenomations,” Medical Clinics of North America, vol. 89, no. 6, pp. 1195–1224, 2005. View at Publisher · View at Google Scholar · View at Scopus
  2. O. H. P. Ramos and H. S. Selistre-De-Araujo, “Snake venom metalloproteases—structure and function of catalytic and disintegrin domains,” Comparative Biochemistry and Physiology C, Toxicology and Pharmacology, vol. 142, no. 3-4, pp. 328–346, 2006. View at Publisher · View at Google Scholar · View at Scopus
  3. Y. Angulo and B. Lomonte, “Biochemistry and toxicology of toxins purified from the venom of the snake Bothrops asper,” Toxicon, vol. 54, no. 7, pp. 949–957, 2009. View at Publisher · View at Google Scholar · View at Scopus
  4. M. S. R. Gomes, M. M. Mendes, F. de Oliveira et al., “BthMP: a new weakly hemorrhagic metalloproteinase from Bothrops moojeni snake venom,” Toxicon, vol. 53, no. 1, pp. 24–32, 2009. View at Publisher · View at Google Scholar · View at Scopus
  5. J. D. O. Costa, K. C. Fonseca, M. S. Garrote-Filho et al., “Structural and functional comparison of proteolytic enzymes from plant latex and snake venoms,” Biochimie, vol. 92, no. 12, pp. 1760–1765, 2010. View at Publisher · View at Google Scholar · View at Scopus
  6. T. Sajevic, A. Leonardi, and I. Križaj, “Haemostatically active proteins in snake venoms,” Toxicon, vol. 57, no. 5, pp. 627–645, 2011. View at Publisher · View at Google Scholar · View at Scopus
  7. A. S. Kamiguti, “Platelets as targets of snake venom metalloproteinases,” Toxicon, vol. 45, no. 8, pp. 1041–1049, 2005. View at Publisher · View at Google Scholar · View at Scopus
  8. F. S. Markland, “Snake venoms and the hemostatic system,” Toxicon, vol. 36, no. 12, pp. 1749–1800, 1998. View at Publisher · View at Google Scholar · View at Scopus
  9. Q. Lu, J. M. Clemetson, and K. J. Clemetson, “Snake venoms and hemostasis,” Journal of Thrombosis and Haemostasis, vol. 3, no. 8, pp. 1791–1799, 2005. View at Publisher · View at Google Scholar · View at Scopus
  10. N. A. Santos-Filho, L. B. Silveira, C. Z. Oliveira et al., “A new acidic myotoxic, anti-platelet and prostaglandin I2 inductor phospholipase A2 isolated from Bothrops moojeni snake venom,” Toxicon, vol. 52, no. 8, pp. 908–917, 2008. View at Publisher · View at Google Scholar · View at Scopus
  11. B. F. Santos, S. M. T. Serrano, A. Kuliopulos, and S. Niewiarowski, “Interaction of viper venom serine peptidases with thrombin receptors on human platelets,” FEBS Letters, vol. 477, no. 3, pp. 199–202, 2000. View at Publisher · View at Google Scholar · View at Scopus
  12. M. A. Belisario, S. Tafuri, C. Di Domenico et al., “H2O2 activity on platelet adhesion to fibrinogen and protein tyrosine phosphorylation,” Biochimica et Biophysica Acta, vol. 1495, no. 2, pp. 183–193, 2000. View at Publisher · View at Google Scholar · View at Scopus
  13. K. J. Clemetson, Q. Lu, and J. M. Clemetson, “Snake venom proteins affecting platelets and their applications to anti-thrombotic research,” Current Pharmaceutical Design, vol. 13, no. 28, pp. 2887–2892, 2007. View at Publisher · View at Google Scholar · View at Scopus
  14. A. S. Kamiguti, M. Zuzel, and R. D. G. Theakston, “Snake venom metalloproteinases and disintegrins: interactions with cells,” Brazilian Journal of Medical and Biological Research, vol. 31, no. 7, pp. 853–862, 1998. View at Google Scholar · View at Scopus
  15. S. Braud, C. Bon, and A. Wisner, “Snake venom proteins acting on hemostasis,” Biochimie, vol. 82, no. 9-10, pp. 851–859, 2000. View at Publisher · View at Google Scholar · View at Scopus
  16. J. J. Calvete, C. Marcinkiewicz, D. Monleón et al., “Snake venom disintegrins: evolution of structure and function,” Toxicon, vol. 45, no. 8, pp. 1063–1074, 2005. View at Publisher · View at Google Scholar · View at Scopus
  17. J. A. Eble, “Matrix biology meets toxinology,” Matrix Biology, vol. 29, no. 4, pp. 239–247, 2010. View at Publisher · View at Google Scholar · View at Scopus
  18. K. J. Clemetson, Q. Lu, and J. M. Clemetson, “Snake C-type lectin-like proteins and platelet receptors,” Pathophysiology of Haemostasis and Thrombosis, vol. 34, no. 4-5, pp. 150–155, 2006. View at Publisher · View at Google Scholar · View at Scopus
  19. T. Morita, “Structures and functions of snake venom CLPs (C-type lectin-like proteins) with anticoagulant-, procoagulant-, and platelet-modulating activities,” Toxicon, vol. 45, no. 8, pp. 1099–1114, 2005. View at Publisher · View at Google Scholar · View at Scopus
  20. C. P. Bernardes, N. A. Santos-Filho, T. R. Costa et al., “Isolation and structural characterization of a new fibrin(ogen)olytic metalloproteinase from Bothrops moojeni snake venom,” Toxicon, vol. 51, no. 4, pp. 574–584, 2008. View at Publisher · View at Google Scholar · View at Scopus
  21. 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
  22. A. Vilca-Quispe, L. A. Ponce-Soto, F. V. Winck, and S. Marangoni, “Isolation and characterization of a new serine protease with thrombin-like activity (TLBm) from the venom of the snake Bothrops marajoensis,” Toxicon, vol. 55, no. 4, pp. 745–753, 2010. View at Publisher · View at Google Scholar · View at Scopus
  23. P. Edman, “Method for determination of the amino acid sequence in peptides,” Acta Chemica Scandinavica, vol. 4, pp. 283–293, 1950. View at Publisher · View at Google Scholar
  24. W. Edgar and C. R. M. Prentice, “The proteolytic action of ancrod on human fibrinogen and its polypeptide chains,” Thrombosis Research, vol. 2, no. 1, pp. 85–95, 1973. View at Google Scholar · View at Scopus
  25. E. F. Sanchez, F. S. Schneider, A. Yarleque et al., “The novel metalloproteinase atroxlysin-I from Peruvian Bothrops atrox (Jergón) snake venom acts both on blood vessel ECM and platelets,” Archives of Biochemistry and Biophysics, vol. 496, no. 1, pp. 9–20, 2010. View at Publisher · View at Google Scholar · View at Scopus
  26. G. B. Naumann, L. F. Silva, L. Silva et al., “Cytotoxicity and inhibition of platelet aggregation caused by an l-amino acid oxidase from Bothrops leucurus venom,” Biochimica et Biophysica Acta, vol. 1810, no. 7, pp. 683–694, 2011. View at Publisher · View at Google Scholar · View at Scopus
  27. J. W. Fox and S. M. T. Serrano, “Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity,” FEBS Journal, vol. 275, no. 12, pp. 3016–3030, 2008. View at Publisher · View at Google Scholar · View at Scopus
  28. M. S. Della-Casa, I. Junqueira-de-Azevedo, D. Butera et al., “Insularin, a disintegrin from Bothrops insularis venom: inhibition of platelet aggregation and endothelial cell adhesion by the native and recombinant GST-insularin proteins,” Toxicon, vol. 57, no. 1, pp. 125–133, 2011. View at Publisher · View at Google Scholar · View at Scopus
  29. L. K. Jennings, “Mechanisms of platelet activation: need for new strategies to protect against platelet-mediated atherothrombosis,” Thrombosis and Haemostasis, vol. 102, no. 2, pp. 248–257, 2009. View at Publisher · View at Google Scholar · View at Scopus
  30. C. Y. Koh and R. M. Kini, “From snake venom toxins to therapeutics—cardiovascular examples,” Toxicon, vol. 59, no. 4, pp. 497–506, 2012. View at Publisher · View at Google Scholar · View at Scopus
  31. H. E. Speich, A. D. Earhart, S. N. Hill et al., “Variability of platelet aggregate dispersal with glycoprotein IIb-IIIa antagonists eptifibatide and abciximab,” Journal of Thrombosis and Haemostasis, vol. 7, no. 6, pp. 983–991, 2009. View at Publisher · View at Google Scholar · View at Scopus
  32. A. D. Michelson, “Antiplatelet therapies for the treatment of cardiovascular disease,” Nature Reviews Drug Discovery, vol. 9, no. 2, pp. 154–169, 2010. View at Publisher · View at Google Scholar · View at Scopus
  33. E. J. Topol, T. V. Byzova, and E. F. Plow, “Platelet GPIIb-IIIa blockers,” The Lancet, vol. 353, no. 9148, pp. 227–231, 1999. View at Publisher · View at Google Scholar · View at Scopus
  34. K. Jurk and B. E. Kehrel, “Platelets: physiology and biochemistry,” Seminars in Thrombosis and Hemostasis, vol. 31, no. 4, pp. 381–392, 2005. View at Publisher · View at Google Scholar · View at Scopus
  35. R. Shlansky-Goldberg, “Platelet aggregation inhibitors for use in peripheral vascular interventions: what can we learn from the experience in the coronary arteries?” Journal of Vascular and Interventional Radiology, vol. 13, no. 3, pp. 229–246, 2002. View at Google Scholar · View at Scopus
  36. E. Ruoslahti, “RGD and other recognition sequences for integrins,” Annual Review of Cell and Developmental Biology, vol. 12, pp. 697–715, 1996. View at Publisher · View at Google Scholar
  37. C. Barja-Fidalgo, A. L. J. Coelho, R. Saldanha-Gama, E. Helal-Neto, A. Mariano-Oliveira, and M. S. de Freitas, “Disintegrins: integrin selective ligands which activate integrin-coupled signaling and modulate leukocyte functions,” Brazilian Journal of Medical and Biological Research, vol. 38, no. 10, pp. 1513–1520, 2005. View at Google Scholar · View at Scopus