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Thromb Haemost 1972; 27(01): 008-018
DOI: 10.1055/s-0038-1649004
Originalarbeiten — Original Articles — Travaux Originaux
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The Action of Vipera aspis Venom on Blood Clotting Factors and Platelets

M. C Boffa
1   Laboratoires d’Hémostase et de Biochimie Moléculaire, Centre National de Transfusion Sanguine (Directeur: Prof. J.P.Soulier), Paris 15°, France
,
F Josso
1   Laboratoires d’Hémostase et de Biochimie Moléculaire, Centre National de Transfusion Sanguine (Directeur: Prof. J.P.Soulier), Paris 15°, France
,
G. A Boffa
1   Laboratoires d’Hémostase et de Biochimie Moléculaire, Centre National de Transfusion Sanguine (Directeur: Prof. J.P.Soulier), Paris 15°, France
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Publication Date:
29 June 2018 (online)

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Summary

On human plasma, the venom of Vipera aspis has both an immediate procoagulant effect and a late fibrinogenolytic and fibrinolytic activity. This procoagulant effect is shown in presence of calcium ions and is observed even in the absence of phospholipids. Factors V and X are the main substrates necessary for this action.

The venom progressively hydrolyses fibrinogen impairing clot formation. It has a fibrinolytic action in the absence of plasminogen.

On platelets, the venom of Vipera aspis inhibits the aggregation induced by ADP, collagen or small amounts of adrenalin. Platelet phospholipids are hydrolysed by the venom and the hydrolysis products are hemolytic. With venom, platelets lose part of their procoagulant properties. The clot formation of PRP is impaired in the presence of the venom as seen on thromboelastogram.

 

  • References

  • 1 Allain J. P, Caen J. L’analyse des fonctions plaquettaires: mesure de l’activité coagulante des plaquettes appelée facteur 3. Rev. fran£. Ét. clin. biol 12: 732 1967;
    PubMedSearch in Google Scholar
  • 2 Astrup T, Mullertz S. The fibrin plate method for estimating fibrinolytic activity. Arch. Bioch 40: 346 1952;
    CrossrefPubMedSearch in Google Scholar
  • 3 Blatrix C, Vignal A, Steinbuch M. Technique de préparation d’un fibrinogène, réactifs pour les dosages d’activité fibrinolytique. Hémostase 03: 179 1963;
    PubMedSearch in Google Scholar
  • 4 Blombäck B. Studies on the action of thrombic enzymes on bovine fibrinogen as measured by N. terminal analysis. Arkiv. for Kemi 12: 321 1958;
    PubMedSearch in Google Scholar
  • 5 Blombäck B, Blombäck M, Nilsson I. M. Coagulation studies on “Reptilase”, an extract of the venom from Bothrops jararaca. Thrombos. Diathes. haemorrh. (Stuttg.) 01: 76 1957;
    PubMedSearch in Google Scholar
  • 6 Boffa M. C, Boffa G. A, Josso F. Effets du venin de Yipera aspis sur les facteurs plasmati- ques de l’hémostase. C. R. Acad. Sci. (Paris) 270: 1284 1970;
    PubMedSearch in Google Scholar
  • 7 Bojfa M. C, Josso F, Boffa G. A. Relations entre les actions hémolytiques et l’activité lécithinasique du venin de Naja nigricollis. C. R. Acad. Sci 269: 2036 1969;
    PubMedSearch in Google Scholar
  • 8 Burstein M, Soulier J. P. Sur la préparation d’un plasma exempt du facteur thromboplasti- que d’origine plaquettaire. Rev. Hémat 12: 341 1957;
    PubMedSearch in Google Scholar
  • 9 Cesari E, Boquet P. Recherches sur les antigènes des venins et les anticorps des sérums anti- venimeux. Ann. Inst. Pasteur 55: 307 1935;
    PubMedSearch in Google Scholar
  • 10 Davey M. G, Esnouf M. P. The isolation of a component of the venom of Trimeresurus oki- navensis that causes the aggregation of blood platelets. Biochem. J Ill: 733 1969;
    PubMedSearch in Google Scholar
  • 11 Esnouf M. P, Tunnah G. W. The isolation and properties of the thrombin-like activity from Ancistrodon rhodostoma venom. Brit. J. Haemat 13: 581 1967;
    CrossrefPubMedSearch in Google Scholar
  • 12 Esnouf M. P, Williams W. J. The isolation and purification of a bovine-plasma protein which is a substrate for the coagulant fraction of Russell’s-Viper venom. Biochem. J 84: 62 1962;
    CrossrefPubMedSearch in Google Scholar
  • 13 Gram H. G. A new method for the determination of the fibrin percentage in blood and plasma. J. biol. Chem 49: 279 1921;
    PubMedSearch in Google Scholar
  • 14 Grasset E, Brechbuhler T, Schwartz D. E, Pongratz E. Comparative analysis and electrophoretic fractionations of snake venoms with special reference to Vipera russellii and Viper a aspis venoms. Venoms Buckley Porges E.E. et N.Amer. Ass. Adv. Sci. Washington, D.C: 153 1956
    Search in Google Scholar
  • 15 Grotto L, Jerushalmy Z, de Vries A. Effect of purified Vipera palestinae hemorrhagin on blood coagulation and platelet function. Thrombos. Diathes. haemorrh. (Stuttg.) 22: 482 1969;
    PubMedSearch in Google Scholar
  • 16 Herzig R. H, Ratnojf O. D, Shainoff J. R. Studis on a procoagulant fraction of southern copperhead snake venom: The preferential release of fibrinopeptide B. J. Lab. clin. Med 76: 451 1970;
    PubMedSearch in Google Scholar
  • 17 Holleman W. H, Coen L. J. Characterization of peptides released from human fibrinogen by Arvin. Biochim. biophys. Acta (Amst.) 200: 587 1970;
    CrossrefPubMedSearch in Google Scholar
  • 18 Josso F, Prou-Wartelle O, Alagille D, Soulier J. P. Le déficit congénital en facteur stabilisant de la fibrine (facteur XIII). Etude de deux cas. Nouv. Rev. franc. Hémat 04: 267 1964;
    PubMedSearch in Google Scholar
  • 19 Rechnic J, de Vries A, Perlmutter C, Levi G, Kochwa S, Gitter S. Coagulation factors in the venoms of Vipera palestinae and Echis colorata. Bull. Res. Counc. of Israël 8E: 81 1960;
    PubMedSearch in Google Scholar
  • 20 Rechnic J. P, Trachtenberg J, Casper C, Moroz A de Vries. Afibrinogenemia and thrombocytopenia in Guinea Pigs following injection of Echis colorata venom. Blood 20: 735 1962;
    PubMedSearch in Google Scholar
  • 21 Schiffman S. I, Theodor S. I. Rapaport. Separation from E-ussell’s Viper venom of one fraction reacting with factor X and another reacting with factor V. Biochemistry 08: 1397 1969;
    CrossrefPubMedSearch in Google Scholar
  • 22 SinaJcos Z, Caen J. Une technique simple, quantitative de mesure de l’agrégation plaquet- taire. Rev. frang. Ét. clin. biol 11: 539 1966;
    PubMedSearch in Google Scholar
  • 23 Soulier J. P, Larrieu M. J. Etude analytique des temps de Quick allongés. Dosages de pro- thrombine, de proconvertine et de proaccélérine. Sang 23: 549 1952;
    PubMedSearch in Google Scholar
  • 24 Soulier J. P, Larrieu M. J. Nouvelle méthode de diagnostic de l’hémophilie. Dosage des facteurs antihémophiliques A et B. Sang 24: 205 1953;
    PubMedSearch in Google Scholar
  • 25 Williams W. J, Esnouf M. P. The fractionation of Russell’s Viper (Vipera russellii) venom with special reference to the coagulant protein. Biochem. J 84: 52 1962;
    CrossrefPubMedSearch in Google Scholar
  • 26 Zeller E. A. The formation of pyrophosphate from adenosine triphosphate in the presence of a snake venom. Arch. Biochem 28: 138 1950;
    PubMedSearch in Google Scholar