Hemostatic properties of Venezuelan Bothrops snake venoms with special reference to Bothrops isabelae venom

Toxicon

Volumn 56, Issue 6, 2010, Pages 926-935

  Rodríguez Acosta, Alexis ^a   Sánchez, Elda E ^a,b   Márquez, Adriana ^a,b   Carvajal, Zoila ^b   Salazar, Ana M ^b   Girón, María E ^a   Estrella, Amalid ^a   Gil, Amparo ^b   Guerrero, Belsy ^b  

^a UNIVERSIDAD CENTRAL DE VENEZUELA   (Venezuela)

^b UNIVERSIDAD CENTRAL DE VENEZUELA   (Venezuela)

Author keywords

Bothrops atrox; Bothrops colombiensis; Bothrops isabelae; Coagulation; Fibrinolytic activity; Hemostasis; Snake venom; Venezuela

Indexed keywords

BLOOD CLOTTING FACTOR 10A; FIBRIN; FIBRINOGEN; FIBRINOLYTIC AGENT; KALLIKREIN; PLASMIN; SNAKE VENOM; THROMBIN;

ALPHA CHAIN; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; BETA CHAIN; BIOLOGICAL ACTIVITY; BLEEDING; BLOOD CLOTTING; COMPARATIVE STUDY; CONTROLLED STUDY; ELECTROPHORESIS; FIBRINOGENOLYSIS; FIBRINOLYSIS; HEMOSTASIS; ION EXCLUSION CHROMATOGRAPHY; LD 50; MALE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; SNAKE; VENEZUELA;

AMIDOHYDROLASES; ANIMALS; BLOOD COAGULATION; BOTHROPS; CROTALID VENOMS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; FIBRIN; FIBRINOLYSIS; FIBRINOLYTIC AGENTS; GELATIN; HEMORRHAGE; HEMOSTASIS; LETHAL DOSE 50; MALE; MICE; SPECIES SPECIFICITY; VENEZUELA;

BOTHROPS; BOTHROPS ATROX; BOTHROPS COLOMBIENSIS; SERPENTES;

EID: 77956094734     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2010.06.015     Document Type: Article

References (55)

1. Arocha-Piñango C.L., Marval E., Guerrero B. Lonomia genus caterpillar toxins. biological aspects. Biochimie 2000, 82:937-942.
2. Bello C.A., Hermogenes A.L., Magalhaes A., Veiga S.S., Gremski L.H., Richardson M., Sanchez E.F. Isolation and biochemical characterization of a fibrinolytic proteinase from Bothrops leucurus (white-tailed jararaca) snake venom. Biochimie 2006, 88:189-200.
3. Braud S., Bon C., Wisner A. Snake venom proteins acting on hemostasis. Biochimie 2000, 82:851-859.
4. Brazón J., D'Suze G., D'Errico M.L., Arocha-Piñango C.L., Guerrero B. Discreplasminin, a plasmin inhibitor isolated from Tityus discrepans scorpion venom. Arch. Toxicol. 2009, 83:669-678.
5. Calvete J.J., Borges A., Segura A., Flores-Díaz M., Alape-Girón A., Gutierrez J.M., Diez N., De Sousa L., Kiriakos D., Sánchez E., Faks J.G., Escolano J., Sanz L. Snake venomics and antivenomics of Bothrops colombiensis, a medically important pitviper of the Bothrops atrox-asper complex endemic to Venezuela: contributing to its taxonomy and snakebite management. J. Proteomics 2009, 72:227-240.
6. Calvete J.J., Sanz L., Angulo Y., Lomonte B., Gutierrez J.M. Venoms, venomics, antivenomics. FEBS Lett. 2009, 583:1736-1743.
7. Chippaux J.P., Williams V., White J. Snake venom variability: methods of study, results and interpretation. Toxicon 1991, 29:1279-1303.
8. Colman R.N. Contact activation kallikrein-kinin pathway: multiple physiologic and pathophysiolic activities. Hemostasis and Thrombosis: Basic Principles and Clinical Practice (Fifth Edition) 2006, 107-130. Lippincott Williams & Wilkins, Philadelphia. fifth ed. R.N. Colman, V.J. Marder, A.W. Clowes, J.N. George, S.Z. Goldhaber (Eds.).
9. Da Silveira R., Dos Santos J., Mangili O., Veiga S., Gremski W., Nader H., Von Dietrich C. Identification of proteases in the extract of venom glands from brown spiders. Toxicon 2002, 40:815-822.
10. Daltry J.C., Wuster W., Thorpe R.S. Diet and snake venom evolution. Nature 1996, 379:537-540.
11. Duque J., Sánchez A., Fierro L., Garzón S., Castaño R. Venenos de serpientes y moléculas antiveneno. Rev. Acad. Colomb. Cienc. 2007, 31:109-137.
12. Eaton M.P. Antifibrinolytic therapy in surgery for congenital heart disease. Anesth. Analg. 2008, 106:1087-1100.
13. Fox J.W., Serrano S.M. Structural considerations of the snake venom metalloproteinases, key members of the M12 reprolysin family of metalloproteinases. Toxicon 2005, 45:969-985.
14. Girón M.E., Salazar A.M., Aguilar I., Pérez J.C., Sánchez E.E., Arocha-Piñango C.L., Rodríguez-Acosta A., Guerrero B. Hemorrhagic, coagulant and fibrino(geno)lytic activities of crude venom and fractions from mapanare (Bothrops colombiensis) snakes. Comp. Biochem. Physiol. C 2008, l(147):113-121.
15. Guerrero B., Arocha-Piñango C.L. Activation of human prothrombin by the venom of Lonomia achelous (Cramer) caterpillars. Thromb. Res. 1992, 66:169-177.
16. Gutierrez J.M. Clinical toxicology of snakebite in Central America. Handbook of Clinical Toxicology of Animal Venoms and Poisons 1995, 645-665. CRC Press, Boca Raton. J. Meier, J. White (Eds.).
17. Gutierrez J.M., Gene J.A., Rojas G., Cerdas L. Neutralization of proteolytic and hemorrhagic activities of Costa Rican snake venoms by a polyvalent antivenom. Toxicon 1985, 23:887-893.
18. Gutierrez J.M., Lomonte B., León G., Alape-Girón A., Flores-Díaz M., Sanz L., Angulo Y., Calvete J.J. Snake venomics and antivenomics: proteomic tools in the design and control of antivenoms for the treatment of snakebite envenoming. J. Proteomics 2009, 72:165-182.
19. Kamiguti A.S., Cardoso J.L. Haemostatic changes caused by the venoms of South American snakes. Toxicon 1989, 27:955-963.
20. Kamiguti A.S., Matsunaga S., Spir M., Sano-Martins I.S., Nahas L. Alterations of the blood coagulation system after accidental human inoculation by Bothrops jararaca venom. Braz. J. Med. Biol. Res. 1986, 19:199-204.
21. Kini R.M. Serine proteases affecting blood coagulation and fibrinolysis from snake venoms. Pathophysiol. Haemost. Thromb. 2005, 34:200-204.
22. Kornacker P.M. Checklist and key to the snakes of Venezuela. Lista sistemática y clave para las serpientes de Venezuela 1999, Pako-Verlag, Rheinbach, Germany. first ed.
23. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
24. Lanari L.C., Rosset S., González M.E., Liria N., de Roodt A.R. A study on the venom of Bothrops alternatus Duméril, Bibron and Duméril, from different regions of Argentina. Toxicon 2010, 55:1415-1424.
25. Lou Z., Hou J., Liang X., Chen J., Qiu P., Liu Y., Li M., Rao Z., Yan G. Crystal structure of a non-hemorrhagic fibrin(ogen)olytic metalloproteinase complexed with a novel natural tri-peptide inhibitor from venom of Agkistrodon acutus. J. Struct. Biol. 2005, 152:195-203.
26. Lowry O.H., Rosembrough N.J., Farr A.L., Randall R.J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 1951, 1193:265-275.
27. Lucena S., Guerrero B., Salazar A.M., Gil A., Arocha-Piñango C.L. Degradation of extracellular matrix proteins (fibronectin, vitronectin and laminin) by serine-proteinases isolated from Lonomia achelous caterpillar hemolymph. Blood Coagul. Fibrinol 2006, 17:427-435.
28. Mackessy S.P., Williams K., Ashton K.G. Ontogenetic variation in venom composition and diet of Crotalus oreganos concolor: a case of venom paedomorphosis?. Copeia 2003, 769-782.
29. Markland F. Snake venoms and the hemostatic system. Toxicon 1998, 36:1749-1800.
30. Marsh N.A., Arocha-Piñango C.L. Evaluation of the fibrin plate method for estimating plasminogen activators. Thromb. Diath. Haemorrh. 1972, 28:75-88.
31. Masci P.P., Whitaker A.N., Sparrow L.G., de Jersey J., Winzor D.J., Watters D.J., Lavin M.F., GaVney P.J. Textilinins from Pseudonaja textilis textilis. Characterization of two plasmin inhibitors that reduce bleeding in an animal model. Blood Coagul. Fibrinol 2000, 11:385-393.
32. Menezes M.C., Furtado M.F., Travaglia-Cardoso S.R., Camargo A.C., Serrano S.M. Sex-based individual variation of snake venom proteome among eighteen Bothrops jararaca siblings. Toxicon 2006, 47:304-312.
33. Moura-da-Silva A.M., Cardoso D.F., Tanizaki M.M. Differences in distribution of myotoxic proteins in venoms from different Bothrops species. Toxicon 1990, 28:1293-1301.
34. NIH Principles of Laboratory Animal Care 1985, 85. National Institute of Health, USA, pp. 1-112.
35. Núñez V., Cid P., Sanz L., De La Torre P., Angulo Y., Lomonte B., Gutierrez J.M., Calvete J.J. Snake venomics and antivenomics of Bothrops atrox venoms from Colombia and the Amazon regions of Brazil, Perú and Ecuador suggest the occurrence of geographic variation of venom phenotype by a trend towards paedomorphism. J. Proteomics 2009, 73:57-78.
36. Pifano F., Rodriguez-Acosta A. Ecological niche and redescription of Crotalus vegrandis (Serpentes: Crotalidae) in Venezuela. Brenesia 1996, 45-46:169-175.
37. Queiroz G.P., Pessoa L.A., Portaro F.C., Furtado M., de F., Tambourgi D.V. Interspecific variation in venom composition and toxicity of Brazilian snakes from Bothrops genus. Toxicon 2008, 52:842-851.
38. Rengifo C., Rodríguez-Acosta A. Serpientes, venenos y su tratamiento en Venezuela 2004, Fondo de Publicaciones de la Facultad de Medicina de la Universidad Central de Venezuela, Caracas. first ed.
39. Rodríguez-Acosta A., Mondolfi A., Orihuela R. ¿Qué hacer frente a un accidente ofídico? 1995, Venediciones. C.A, Caracas. first ed.
40. Rodríguez-Acosta A., Uzcategui W., Azuaje R., Aguilar I., Girón M.E. Análisis clínico y epidemiológico de los accidentes por mordeduras de serpientes del género Bothrops en Venezuela. Rev. Cubana. Med. Trop. 2000, 52:90-94.
41. de Roodt A.R., Estévez J., Dolab J.A., Manzanelli M.V., Piñeiro N., Paniagua J.F., Vogt A.U. Biological and immunological characteristics of the poison of Bothrops cotiara (Serpentes: Viperidae). Rev. Biol. Trop. 2006, 54:889-901.
42. Salazar A.M., Rodríguez-Acosta A., Girón M.E., Aguilar I., Guerrero B. A comparative analysis of the clotting and fibrinolytic activities of the mapanare (Bothrops atrox) snake venom from different geographical areas in Venezuela. Thromb. Res. 2007, 120:95-104.
43. Saldarriaga M.M., Otero R., Núñez V., Toro M.F., Díaz A., Gutierrez J.M. Ontogenetic variability of Bothrops atrox and Bothrops asper snake venoms from Colombia. Toxicon 2003, 42:405-411.
44. Salomão M.G., Wuster W., Thorpe R.S., Touzet J.M., B.B.B.S.P. MtDNA phylogeny of Neotropical pitvipers of the genus Bothrops (Squamata: Serpentes: Viperidae). Kaupia (Darmstadt) 1999, 8:127-134.
45. Sandner-Montilla F. Una nueva especie de genero Bothrops (Serpentes, Crotalidae, Bothropinae) de la región de Guanare, estado Portuguesa, Venezuela. Mem. Cient. Ofidiol. 1979, 4:1-19.
46. Schagger H., von Jagow G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 1987, 166:368-379.
47. Serrano S.M., Matos M.F., Mandelbaum F.R., Sampaio C.A. Basic proteinases from Bothrops moojeni (caissaca) venom-I. Isolation and activity of two serine proteinases, MSP 1 and MSP 2, on synthetic substrates and on platelet aggregation. Toxicon 1993, 31:471-481.
48. Shannon J.D., Baramova E.N., Bjarnason J.B., Fox J.W. Amino acid sequence of a Crotalus atrox venom metalloproteinase which cleaves type IV collagen and gelatin. J. Biol. Chem. 1989, 264:11575-11583.
49. Spearman-Karber R. Alternative methods of analysis for quantal responses. Statistical Method in Biological Assay 1964, Charles Griffin, London, U.K. second ed. D. Finney (Ed.).
50. Swenson S., Markland F.S. Snake venom fibrin (ogen)olytic enzymes. Toxicon 2005, 45:1021-1039.
51. Weinberg M.L.D., Felicori L.F., Bello A.B., Magalhães H.P.B., Almeida A.P., Magalhães A., Sanchez E.F. Biochemical properties of a Bushmaster snake venom serine protease (LV-Ka), and its kinin releasing activity evaluated in rat mesenteric arterial rings. J. Pharm. Sci. 2004, 96:333-342.
52. Weinberg M.L., Felicori L.F., Bello C.A., Magalhães H.P., Almeida A.P., Magalhães A., Sanchez E.F. Biochemical properties of a bushmaster snake venom serine proteinase (LV-Ka), and its kinin releasing activity evaluated in rat mesenteric arterial rings. J. Pharmacol. Sci. 2004, 96:333-342.
53. White J. Snake venoms and coagulopathy. Toxicon 2005, 45:951-967.
54. a, a fibrinolytic enzyme from Agkistrodon acutus venom. Toxicon 2001, 39:1133-1139.
55. Zhang Y., Wisner A., Xiong Y., Bon C. A novel plasminogen activator from snake venom. Purification, characterization, and molecular cloning. J. Biol. Chem. 1995, 270:10246-10255.