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Table of Contents
Vol. 31, No. 3-6, 2001
Issue release date: March 2002
Section title: Fibrinolysis
Haemostasis 2001;31:133–140
(DOI:10.1159/000048056)

Snake Venom Proteinases as Tools in Hemostasis Studies: Structure-Function Relationship of a Plasminogen Activator Purified from Trimeresurus stejnegeri Venom

Wisner A. · Braud S. · Bon C.
Unité des Venins, Institut Pasteur, Paris, France
email Corresponding Author

Dr. Cassian Bon

Head of the Venoms Unit, Institut Pasteur

25–28, rue du Docteur-Roux

F–75724 Paris Cedex 15 (France)

Tel. +33 1 45 68 86 85, Fax +33 1 40 61 30 57, E-Mail cbon@pasteur.fr


References

  1. Siezen RJ: Multi-domain, cell-envelope proteinases of lactic acid bacteria. Antonie Van Leeuwenhoek 1999;76:139–155.
    External Resources
  2. Rudenskaya GN, Bogdanova EA, Revina LP, Golovkin BN, Stepanov VM: Macluralisin – a serine proteinase from fruits of Maclura pomifera (Raf.). Schneid Planta 1995;196:174–179.
  3. Neurath H: Evolution of proteolytic enzymes. Science 1984;224:350–357.
    External Resources
  4. Neurath H: Proteolytic enzymes, past and present. Fed Proc 1985;44:2907–2913.
    External Resources
  5. DiBella EE, Scheraga HA: Thrombin specificity: Further evidence for the importance of the beta-insertion loop and Trp96. Implications of the hydrophobic interaction between Trp96 and Pro60B Pro60C for the activity of thrombin. J Protein Chem 1998;17:197–208.
  6. Hedstrom L, Szilagyi L, Rutter WJ: Converting trypsin to chymotrypsin: The role of surface loops. Science 1992;255:1249–1253.
    External Resources
  7. Le Bonniec BF, Guinto ER, MacGillivray RT, Stone SR, Esmon CT: The role of thrombin’s Tyr-Pro-Pro-Trp motif in the interaction with fibrinogen, thrombomodulin, protein C, antithrombin III, and the Kunitz inhibitors. J Biol Chem 1993;268:19055–19061.
  8. Madison EL, Goldsmith EJ, Gerard RD, Gething MJ, Sambrook JF: Serpin-resistant mutants of human tissue-type plasminogen activator. Nature 1989;339:721–724.
  9. Matthews BW, Sigler PB, Henderson R, Blow DM: Three-dimensional structure of tosyl-alpha-chymotrypsin. Nature 1967;214:652–656.
    External Resources
  10. Ruhlmann A, Kukla D, Schwager P, Bartels K, Huber R: Structure of the complex formed by bovine trypsin and bovine pancreatic trypsin inhibitor. Crystal structure determination and stereochemistry of the contact region. J Mol Biol 1973;77:417–436.
    External Resources
  11. Bode W, Chen Z: The X-ray structures of porcine pancreatic kallikrein and of its complex with bovine pancreatic trypsin inhibitor. Adv Exp Med Biol 1983;156:289–308.
    External Resources
  12. Bode W, Mayr I, Baumann U, Huber R, Stone SR, Hofsteenge J: The refined 1.9 Å crystal structure of human alpha-thrombin: Interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment. EMBO J 1989;8:3467–3475.
  13. Padmanabhan K, Padmanabhan KP, Tulinsky A, Park CH, Bode W, Huber R, Blankenship DT, Cardin AD, Kisiel W: Structure of human des(1–45) factor Xa at 2.2 Å resolution. J Mol Biol 1993;232:947–966.
  14. Lamba D, Bauer M, Huber R, Fischer S, Rudolph R, Kohnert U, Bode W: The 2.3 angstrom crystal structure of the catalytic domain of recombinant two-chain human tissue-type plasminogen activator. J Mol Biol 1996:258:117–135.
  15. Greer J: Comparative modeling methods: Application to the family of the mammalian serine proteases. Proteins 1990;7:317–334.
    External Resources
  16. Perona JJ, Craik CS: Structural basis of substrate specificity in the serine proteases (Review). Protein Sci 1995:4:337–360.
  17. Perona JJ, Craik CS: Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold. J Biol Chem 1997;272:29987–29990.
  18. Kini RM, Evans HJ: Effects of snake venom proteins on blood platelets. Toxicon 1990;28:1387–1422.
  19. Markland FS Jr: Snake venoms. Drugs 1997;3:1–10.
  20. Mitrakul C: Effect of five Thai snake venoms on coagulation, fibrinolysis and platelet aggregation. Southeast Asian J Trop Med Public Health 1979;10:266–275.
  21. Marrakchi N, Zingali RB, Karoui H, Bon C, el Ayeb M: Cerastocytin, a new thrombin-like platelet activator from the venom of the Tunisian viper Cerastes cerastes. Biochim Biophys Acta 1995;1244:147–156.
  22. Serrano SM, Mentele R, Sampaio CA, Fink E: Purification, characterization, and amino acid sequence of a serine proteinase, PA-BJ, with platelet-aggregating activity from the venom of Bothrops jararaca. Biochemistry 1995;34:7186–7193.
    External Resources
  23. Kirby EP, Niewiarowski S, Stocker K, Kettner C, Shaw E, Brudzynski TM: Thrombocytin, a serine protease from Bothrops atrox venom. 1. Purification and characterization of the enzyme. Biochemistry 1979;18:3564–3570.
    External Resources
  24. Santos ABF, Serrano SMT, Kuliopulos A, Niewiarouski S: Interaction of viper venom serine peptidases with thrombin receptors on human platelets. FEBS Lett 2000;477:199–202.
  25. Kisiel W: Molecular properties of the factor V-activating enzyme from Russell’s viper venom. J Biol Chem 1979;254:12230–12234.
    External Resources
  26. Stocker K, Fischer H, Meier J, Brogli M, Svendsen L: Characterization of the protein C activator Protac from the venom of the southern copperhead (Agkistrodon contortrix) snake. Toxicon 1987;25:239–252.
  27. Pirkle H, Theodor I: Thrombin-like venom enzymes: Structure and function. Adv Exp Med Biol 1990;281:165–175.
  28. Pirkle H: Thrombin-like enzymes from snake venoms: An updated inventory. Scientific and Standardization Committee’s Registry of Exogenous Hemostatic Factors. Thromb Haemost 1998:79:675–683.
  29. Stocker K, Fischer H, Meier J: Thrombin-like snake venom proteinases. Toxicon 1982;20:265–273.
  30. 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.
  31. Parry MA, Jacob U, Huber R, Wisner A, Bon C, Bode W: The crystal structure of the novel snake venom plasminogen activator TSV-PA: A prototype structure for snake venom serine proteinases. Structure 1998;6:1195–1206.
  32. Nakashima K, Ogawa T, Oda N, Hattori M, Sakaki Y, Kihara H, Ohno M: Accelerated evolution of Trimeresurus flavoviridis venom gland phospholipase A2 isozymes. Proc Natl Acad Sci USA 1993;90:5964–5968.
  33. Nakashima K, Nobuhisa I, Deshimaru M, Nakai M, Ogawa T, Shimohigashi Y, Fukumaki Y, Hattori M, Sakaki Y, Hattori S: Accelerated evolution in the protein-coding regions is universal in Crotalinae snake venom gland phospholipase A2 isozyme genes. Proc Natl Acad Sci USA 1995;92:5605–5609.
    External Resources
  34. Ogawa T, Oda N, Nakashima K, Sasaki H, Hattori M, Sakaki Y, Kihara H, Ohno M: Unusually high conservation of untranslated sequences in cDNAs for Trimeresurus flavoviridis phospholipase A2 isozymes. Proc Natl Acad Sci USA 1992;89:8557–8561.
    External Resources
  35. Collen D: On the regulation and control of fibrinolysis. Edward Kowalski Memorial Lecture. Thromb Haemost 1980;43:77–89.
    External Resources
  36. Collen D, Lijnen HR, Todd PA, Goa KL: Tissue-type plasminogen activator. A review of its pharmacology and therapeutic use as a thrombolytic agent. Drugs 1989;38:346–388.
  37. Collen D, Lijnen HR: Basic and clinical aspects of fibrinolysis and thrombolysis. Blood 1991;78:3114–3124.
  38. Lijnen HR, Collen D: Molecular interactions between tissue-type plasminogen activator and plasminogen. Methods Enzymol 1993;223:197–206.
  39. Kohnert U, Hellerbrand K, Martin U, Stern A, Popp F, Fischer S: The recombinant Escherichia coli-derived protease-domain of tissue-type plasminogen activator is a potent and fibrin specific fibrinolytic agent. Fibrinolysis 1996;10:93–102.
  40. Martin U, Kohnert U, Stern A, Popp F, Fischer S: Comparison of the recombinant Escherichia coli-produced protease domain of tissue-type plasminogen activator with alteplase, reteplase and streptokinase in a canine model of coronary artery thrombolysis. Thromb Haemost 1996;76:1096–1101.
  41. Zhang Y, Wisner A, Maroun RC, Choumet V, Xiong Y, Bon C: Trimeresurus stejnegeri snake venom plasminogen activator. Site-directed mutagenesis and molecular modeling. J Biol Chem 1997;272:20531–20537.
  42. Shohet RV, Spitzer S, Madison EL, Bassel-Duby R, Gething MJ, Sambrook JF: Inhibitor-resistant tissue-type plasminogen activator: An improved thrombolytic agent in vitro. Thromb Haemost 1994;71:124–128.
  43. Itoh N, Tanaka N, Mihashi S, Yamashina I: Molecular cloning and sequence analysis of cDNA for batroxobin, a thrombin-like snake venom enzyme. J Biol Chem 1987;262:3132–3135.
  44. Au LC, Lin SB, Chou JS, Teh GW, Chang KJ, Shih CM: Molecular cloning and sequence analysis of the cDNA for ancrod, a thrombin-like enzyme from the venom of Calloselasma rhodostoma. Biochem J 1993;294(pt 2):387–390.
  45. Tokunaga F, Nagasawa K, Tamura S, Miyata T, Iwanaga S, Kisiel W: The factor V-activating enzyme (RVV-V) from Russell’s viper venom. Identification of isoproteins RVV-V alpha, -V beta, and -V gamma and their complete amino acid sequences. J Biol Chem 1988;263:17471–17481.
  46. Wang D, Bode W, Huber R: Bovine chymotrypsinogen A X-ray crystal structure analysis and refinement of a new crystal form at 1.8 Å resolution. J Mol Biol 1985;185:595–624.