Activation of factor X by snake venom proteases

Toxins and Hemostasis: From Bench to Bedside

Volumn , Issue , 2011, Pages 447-464

  Siigur, Jüri ^a   Siigur, Ene ^a  

^a NATIONAL INSTITUTE OF CHEMICAL PHYSICS AND BIOPHYSICS   (Estonia)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84920138463     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-90-481-9295-3_26     Document Type: Chapter

References (62)

1. Amphlett, G.W., Byrne, R., Castellino, F.J., 1982. Cation binding properties of the multiple subforms of RVV-X, the coagulant protein from Vipera russelli. Biochemistry 21, 125-132.
2. Aurell, L., Friberger, P., Karlsson, G., Claeson, G., 1977. A new sensitive and highly specific chromogenic peptide substrate for Factor Xa. Thromb. Res. 11, 595-605.
3. Baugh, R.J., Krishnaswamy, S., 1996. Role of the activation peptide domain in human factor X activation by the extrinsic Xase complex. J. Biol. Chem. 271, 16126-16134.
4. Bjarnason, J.B., Fox J.W., 1995. Snake venom metalloendopeptidases: reprolysins. Meth. Enzymol. 248, 345-368.
5. Cerretti, D.P., DuBose, R.F., Black, R.A., Nelson, N., 1999. Isolation of two novel metalloproteinase-disintegrin (ADAM) cDNAs that show testis-specific gene expression. Biochem. Biophys. Res. Commun. 263, 810-815.
6. Chen, H.-S., Chen, J.-M., Lin, C.-V., Khoo, K.-H., Tsai, I.-H., 2008. New insights into the functions and N-glycan structures of factor X activator from Russell's viper venom. FEBS J. 275, 3944- 3958.
7. Durkee, K.H., Roh, B.H., Doellgast, G.J., 1993. Immunoaffinity chromatographic purification of Russell's viper venom factor X activator using elution in high concentrations of magnesium chloride. Protein Expr. Purif. 4, 405-411.
8. El-Asmar, M.F., Shaban, E., Hagag, M., Swelam, N., Tu, A.T., 1986. Coagulant component in Cerastes cerastes (Egyptian sand viper) venom. Toxicon 24, 1037-1044.
9. Esnouf, M.P., 1978. Current perspectives of factor X, in: Recent Progress in Blood Coagulation and Thrombosis Research. Biblthca. Haemat. (vol. 44). Karger, Basel, pp. 75-80.
10. Farid, T., Nasser, H., Zaki, K., El-Asmar, M.F., 1993. Low molecular weight factor X activator from Cerastes vipera (Sahara sand viper) venom. Toxicon 31, 1007-1017.
11. Fox, J.W., Serrano, S.M.T., 2008. Insights into and speculations about snake venom metalloproteinase (SVMP) synthesis, folding and disulfide bond formation and their contribution to venom complexity. FEBS J. 275, 3016-3030.
12. Franssen, J.H.L., Janssen-Claessen, T., van Dieijen, G., 1983. Purification and properties of an activating enzyme of blood clotting factor X from the venom of Cerastes cerastes. Biochim. Biophys. Acta 747, 186-190.
13. Fujikawa, K., Coan, M.H., Legaz, M.E., Davie, E.W., 1974. The mechanism of activation of bovine factor X (Stuart factor) by intrinsic and extrinsic pathways. Biochemistry 13, 5290-5299.
14. Fujikawa, K., Titani, K., Davie, E.W., 1975. Activation of bovine factor X (Stuart factor): conversion of factor Xaα to factor Xaβ. Proc. Natl. Acad. Sci. U.S.A. 72, 3359-3363.
15. Furie, B.C., Furie, B., 1975. Interaction of lanthanide ions with bovine factor X and their use in the affinity chromatography of the venom coagulant protein of Vipera russelli. J. Biol. Chem. 250, 601-608.
16. Furukawa, Y., Matsunaga, Y., Hayashi, K., 1976. Purification and characterization of a coagulant protein from the venom of Russell's viper. Biochim. Biophys. Acta 453, 48-61.
17. Gowda, D.C., Jackson, C.M., Hensley, P., Davidson, E.A., 1994. Factor X-activating glycoprotein of Russell's viper venom. J. Biol. Chem. 269, 10644-10650.
18. Gowda, D.C., Jackson, C.M., Kurzban, G.P., McPhie, P., Davidson, E.A., 1996. Core sugar residues of the N-linked oligosaccharides of Russell's viper venom factor X-activator maintain functionally active polypeptide structure. Biochemistry 35, 5833-5837.
19. Grams, F., Huber, R., Kress, L.F., Moroder, L., Bode, W., 1993. Activation of snake venom metalloproteinases by a cysteine switch like mechanism. FEBS Lett. 335, 76-80.
20. Hertzberg, M., 1994. Biochemistry of factor X. Blood Rev. 8, 56-62.
21. Hofmann, H., Bon, C., 1987. Blood coagulation induced by the venom of Bothrops atrox. 2. Identification, purification and properties of two factor X activators. Biochemistry 26, 780-787.
22. Hofmann, H., Dumarey, C., Bon, C., 1983. Blood coagulation induced by Bothrops atrox venom. Identification and properties of a factor X activator. Biochimie 65, 201-210.
23. Jackson, C.M., Gordon, J.G., Hanahan, D.J., 1971, Separation of the tosyl arginine esterase activity from the factor X activating enzyme of Russell's viper venom. Biochim. Biophys. Acta 252, 255-261.
24. Jesty, J., 1986. Analysis of the generation and inhibition of activated coagulation factor X in pure systems and in human plasma. J. Biol. Chem. 261, 8695-8702.
25. Kishimoto, M., Takahashi, T., 2002. Molecular cloning of HR1a and HR1b, high molecular hemorrhagic factors, from Trimeresurus flavoviridis venom. Toxicon 40, 1369-1375.
26. Kisiel, W., Hermodson, M.A., Davie, E.W., 1976. Factor X activating enzyme from Russell's viper venom: isolation and characterization. Biochemistry 15, 4901-4906.
27. Komori, Y., Nikai, T., Sugihara, H., 1990. Isolation and characterization of factor X activator from the venom of Vipera aspis aspis. Int. J. Biochem. 22, 1053-1060.
28. Kosow, D.P., 1976. Purification and activation of human factor X: cooperative effect of Ca2+ on the activation reaction. Thromb. Res. 9, 565-573.
29. Lee, W.H., Zhang, Y., Wang, W.-Y., Xiong, Y.-L., Gao, R., 1995. Isolation and properties of a blood coagulation factor X activator from the venom of king cobra (Ophiophagus hannah). Toxicon 33, 1263-1276.
30. Leonardi, A., Fox, J.W., Trampuš-Bakija, A., Križaj, I., 2008. Two coagulation factor X activators from Vipera a. ammodytes venom with potential to treat patients with dysfunctional factors IXa or VIIa. Toxicon 52, 628-637.
31. Leytus, S.P., Chung, D.W., Kisiel, W., Kurachi, K., Davie, E.W., 1984. Characterization of a cDNA coding for human factor X. Proc. Natl. Acad. Sci. U.S.A. 81, 3699-3702.
32. Lindhout, M.J., Kop-Klaassen, B.H.M., Hemker, H.C., 1978. Activation of decarboxyfactor X by a protein from Russell's viper venom. Purification and partial characterization of activated decarboxyfactor X. Biochim. Biophys. Acta 533, 327-341.
33. Marsh, N.A., 2001. Diagnostic use of snake venoms. Haemostasis 31, 211-217.
34. Matsui, T., Fujimura, Y., Titani, K., 2000. Snake venom proteases affecting hemostasis and thrombosis. Biochim. Biophys. Acta 1477, 146-156.
35. Matsuzaki, R., Yoshiara, E., Yamada, M., Shima, K., Atoda, H., Morita, T., 1996. cDNA cloning of IX/X-BP, a heterogeneous two-chain anticoagulant protein from snake venom. Biochem. Biophys. Res. Commun. 220, 382-387.
36. Morita, T., 1998. Proteases which activate factor X, in: Bailey, G.S. (Ed.), Enzymes from Snake Venoms. Alaken Inc., Fort Collins, Colorado, pp. 179-208.
37. Nishida, S., Fujita, T., Kohno, N., Atoda, H., Morita, T., Takeya, H., Kido, I., Paine, M.J., Kawabata, S., Iwanaga, S., 1995. cDNA cloning and deduced amino acid sequence of prothrombin activator (ecarin) from Kenyan Echis carinatus venom. Biochemistry 34, 1771-1778.
38. Owen, C.A. Jr., 2001. Inherited coagulation factor deficiencies, in: Nichols, W.L., Bowie, E.J.W. (Eds.), A History of Blood Coagulation. Mayo Foundation for Medical Education and Research, Rochester, MN, pp. 117-132.
39. Pryzdial, E.L.G., Lavigne, N., Dupuis, N., Kessler, G.E., 1999. Plasmin converts factor X from coagulation zymogen to fibrinolysis cofactor. J. Biol. Chem. 274, 8500-8505.
40. Pukrittayakamee, S., Esnouf, M.P., McMichael, A.J., 1983. Purification and inactivation of the factor X activator of Russell's viper venom with monoclonal antibodies. Mol. Biol. Med. 1, 123-135.
41. Samel, M., Siigur, J., 1995. Medium molecular weight factor X activating enzyme from Vipera berus berus venom. Toxicon 33, 41-52.
42. Samel, M., Vija, H., Subbi, J., Siigur, J., 2003. Metalloproteinase with factor X activating and fibrinolytic activities from Vipera berus berus venom. Comp. Biochem. Physiol. B. 135, 575-582.
43. Sekiya, F., Yoshida, M., Yamashita, T., Morita, T., 1996. Magnesium (II) is a crucial constituent of the blood coagulation cascade. J. Biol. Chem. 271, 8541-8544.
44. Siigur, E., Aaspõllu, A., Trummal, K., Tõnismägi, K., Tammiste, I., Kalkkinen, N., Siigur, J., 2004. Factor X activator from Vipera lebetina venom is synthesized from different genes. Biochim. Biophys. Acta 1702, 41-51.
45. Siigur, E., Tõnismägi, K., Trummal, K., Samel, M., Vija, H., Subbi, J., Siigur, J., 2001a. Factor X activator from Vipera lebetina snake venom, molecular characterization and substrate specificity. Biochim. Biophys. Acta 1568, 90-98.
46. Siigur, J., Aaspõllu, A., Tõnismägi, K., Trummal, K., Samel, M., Vija, H., Subbi, J., Siigur, E., 2001b. Proteases from Vipera lebetina venom affecting coagulation and fibrinolysis. Haemostasis 31, 123-132.
47. Siigur, J., Siigur, E., 2006. Factor X activating proteases from snake venoms. Toxin Rev. 25, 235-255.
48. Silva, M.B., Schattner, M., Ramos, C.R.R., Junqueira-De-Azevedo, I.L.M., Guarnieri, M.C., Lazzari, M.A., Sampaio, C.A.M., Pozner, R.G., Ventura, J.S., Ho, P.L., Chudzinski-Tavassi, A.M., 2003. A prothrombin activator from Bothrops erythromelas (Jararaca-da-seca) snake venom: characterization and molecular cloning. Biochem. J. 369, 129-139.
49. Sinha, U., Wolf, D.L., 1993. Carbohydrate residues modulate the activation of coagulation factor X. J. Biol. Chem. 268, 3048-3051.
50. Skogen, W.F., Bushone, D.S., Johnson, A.E., Cox, A.C., 1983. The role of the Gla domain in the activation of bovine coagulation factor X by the snake venom protein XCP. Biochem. Biophys. Res. Commun. 111, 14-20.
51. Stocker, K., 1990. Snake venom proteins affecting hemostasis and fibrinolysis, in: Stocker, K. (Ed.), Medical Use of Snake Venom Proteins. CRC Press, Boca Raton, Ann Arbor, Boston, pp. 97-160.
52. Stocker, K., 1998. Research, diagnostic and medicinal uses of snake venom enzymes, in: Bailey, G.S. (Ed.), Enzymes in Snake Venoms. Alaken Inc., Fort Collins, CO, pp. 705-736.
53. Strachan, N.J.C., Ogden, I.D., 2000. A sensitive microsphere coagulation ELISA for Escherichia coli O157:H7 using Russell's viper venom. FEMS Microbiol. Lett. 186, 79-84.
54. Takeda, S., Igarashi, T., Mori, H., 2007. Crystal structure of RVV-X: An example of evolutionary gain of specificity by ADAM proteinases. FEBS Lett. 581, 5859-5864.
55. Takeya, H., Nishida, S., Miyata, T., Kawada, S., Saisaka, Y., Morita, T., Iwanaga, S., 1992. Coagulation factor X activating enzyme from Russell's viper venom (RVV-X). J. Biol. Chem. 267, 14109-14117.
56. Tans, G., Rosing, J., 2001. Snake venom activators of factor X: An overview. Haemostasis 31, 225-233.
57. Teng, C.-M., Chen, Y.-H., Ouyang, C., 1984. Purification and properties of the main coagulant and anticoagulant principles of Vipera russelli snake venom. Biochim. Biophys. Acta 786, 204-212.
58. van Dieijen, G., Tans, G., van Rijn, J., Zwaal, R.F.A., Rosing, J., 1981. Simple and rapid method to determine the binding of blood clotting factor X to phospholipid vesicles. Biochemistry 20, 7096-7101.
59. Wagstaff, S.C., Laing, G.D., Theakston, R.D.G., Pappaspyridis, C., Harrison, R.A., 2006. Bioinformatics and multiepitope DNA immunization to design rational snake antivenom. PloS Med. 3, e184.
60. Williams, W.J., Esnouf, M.P., 1962. The fractionation of Russell's viper (Vipera russellii) venom with special reference to the coagulant protein. Biochem. J. 84, 52-62.
61. Yamada, D., Sekiya, F., Morita, T., 1997. Prothrombin and factor X activator activities in the venoms of Viperidae snakes. Toxicon 35, 1581-1589.
62. Zhang, Y., Xiong, Y.-L., Bon, C., 1995. An activator of blood coagulation factor X from the venom of Bungarus fasciatus. Toxicon 33, 1277-1288.