Download PDF
Thromb Haemost 1988; 60(03): 355-360
DOI: 10.1055/s-0038-1646971
Review Article
Schattauer GmbH Stuttgart

Meizothrombin, a Major Product of Factor Xa-Catalyzed Prothrombin Activation

Jan Rosing
The Department of Biochemistry, University of Limburg, Maastricht, The Netherlands
,
Guido Tans
The Department of Biochemistry, University of Limburg, Maastricht, The Netherlands
› Author Affiliations
Further Information

Publication History

Received 01 June 1988

Accepted after revision 07 October 1988

Publication Date:
30 June 2018 (online)

Also available at
  PDF Download Permissions and Reprints

Keywords

Meizothrombin - Thrombin - Prothrombin activation
 

  • References

  • 1 Jackson CM, Nemerson Y. Blood coagulation. Annu Rev Biochem 1980; 49: 765-811
    CrossrefPubMedGoogle Scholar
  • 2 Tans G, Rosing J. Multicomponent enzyme complexes of blood coagulation. In: Blood Coagulation Zwaal RFA, Hemker HC. (eds) Elsevier; Amsterdam: 1986: 59-85
  • 3 Fenton II JW. Thrombin specificity. Ann NY Acad Sci 1981; 370: 468-495
    CrossrefPubMedGoogle Scholar
  • 4 Rosing J, Zwaal RF A, Tanss G. Formation of meizothrombin as an intermediate in factor Xa-catalyzed prothrombin activation. J Biol Chem 1986; 261: 4224-4228
    PubMedGoogle Scholar
  • 5 Krishnaswamy S, Mann KG, Nesheim ME. The prothrombinase-catalyzed activation of prothrombin proceeds through the intermediate meizothrombin in an ordered, sequential reaction. J Biol Chem 1986; 261: 8977-8984
    PubMedGoogle Scholar
  • 6 Suttie JW, Jackson CM. Prothrombin structure, activation and biosynthesis. Physiol Rev 1977; 57: 1-65
    CrossrefPubMedGoogle Scholar
  • 7 Stenn KS, Blout ER. Mechanism of bovine prothrombin activation by an insoluble preparation of bovine factor Xa (Thrombokinase). Biochemistry 1972; 11: 4502-4515
    CrossrefPubMedGoogle Scholar
  • 8 Rabiet MJ, Blashill A, Furie B, Furie BC. Prothrombin fragment 1.2.3, a major product of prothrombin activation in human plasma. J Biol Chem 1986; 261: 13210-13215
    PubMedGoogle Scholar
  • 9 Boissel J-P, Le Bonniec B, Rabiet MJ, Labie D, Elion J. Covalent structures of (β- and γ-autolytic derivatives of human α-thrombin. J Biol Chem 1984; 259: 5691-5697
    PubMedGoogle Scholar
  • 10 Heldebrant CM, Mann KG. The activation of prothrombin I. Isolation and preliminary characterization of intermediates. J Biol Chem 1973; 248: 3642-3652
    PubMedGoogle Scholar
  • 11 Heldebrant CM, Butkowski RJ, Bajaj SP, Mann KG. The activation of prothrombin II. Partial reactions, physical and chemical characterization of the intermediates of activation. J Biol Chem 1973; 248: 7149-7163
    PubMedGoogle Scholar
  • 12 Esmon CT, Jackson CM. The conversion of prothrombin to thrombin III. The factor Xa-catalyzed activation of prothrombin. J Biol Chem 1974; 249: 7782-7790
    PubMedGoogle Scholar
  • 13 Esmon CT, Owen WG, Jackson CM. The conversion of prothrombin to thrombin V. The activation of prothrombin by factor Xa in the presence of phospholipid. J Biol Chem 1974; 249: 7798-7807
    PubMedGoogle Scholar
  • 14 Esmon CT, Owen WG, Jackson CM. A plausible mechanism for prothrombin activation by factor Xa, phospholipid and calcium ions. J Biol Chem 1974; 249: 8045-807
    PubMedGoogle Scholar
  • 15 Morita T, Iwanaga S, Suzuki T. The mechanism of activation of bovine prothrombin by an activator isolated from Echis carinatus venom and characterization of the new active intermediates. J Biochem 1976; 79: 1089-1108
    CrossrefPubMedGoogle Scholar
  • 16 Franza RB, Aronson DL, Finlayson JS. Activation of human prothrombin by a procoagulant fraction from the venom of Echis carinatus. Identification of a high molecular weight intermediate with thrombin activity. J Biol Chem 1975; 250: 7057-7068
    PubMedGoogle Scholar
  • 17 Kornalik F, Blombäck B. Prothrombin activation induced by ecarin –a prothrombin converting enzvme from Echis carinatus venom. Thromb Res 1975; 6: 53-65
    CrossrefPubMedGoogle Scholar
  • 18 Rhee M-J, Morris S, Kosow DP. Role ot meizothrombin and meizothromhin (des FI) in the conversion of prothrombin to thrombin by the Echis carinatus venom coagulant. Biochemistry 1982; 21: 3437-3443
    CrossrefPubMedGoogle Scholar
  • 19 Briët E, Noyes CM, Roberts HR, Griffith MJ. Cleavage and activation of human prothrombin by Echis carinatus venom. Thromb Res 1982; 27: 591-600
    CrossrefPubMedGoogle Scholar
  • 20 Tans G, Govers-Riemslag JW P, van Rijn JL M L, Rosing J. Puiification and properties of a prothrombin activator from the venom of Notechis scutatus scutatus. J Biol Chem 1985; 260: 9366-9372
    PubMedGoogle Scholar
  • 21 Rabiet MJ, Elion J, Benarous R, Labie D, Josso F. Activation of prothrombin Barcelona. Evidence for active high molecular weight intermediates. Biochim Biophys Acta 1979; 584: 66-75
    PubMedGoogle Scholar
  • 22 Rabiet MJ, Furie BC, Furie B. Molecular defect of prothrombin Barcelona. Substitution of cysteine for arginine at residue 273. J Biol Chem 1986; 261: 15045-15048
    PubMedGoogle Scholar
  • 23 Novoa E, Seegers WH. Mechanisms of α-thrombin and β-thrombin-E formation: use of ecarin for isolation of meizothrombin 1. Thromb Res 1980; 18: 657-668
    CrossrefPubMedGoogle Scholar
  • 24 Nesheim ME, Mann KG. The kinetics and cofactor dependence of the two cleavages involved in prothrombin activation. J Biol Chem 1983; 258: 5386-5391
    CrossrefPubMedGoogle Scholar
  • 25 Rosing J, Tans G, Govers-Riemslag JW P, Zwaal RFA, Hemker HC. The role of phospholipids and factor Va in the prothrombinase complex. J Biol Chem 1980; 255: 274-283
    PubMedGoogle Scholar
  • 26 Nesheim ME, Taswell JB, Mann KG. The contribution of bovine factor V and factor Va to the activity of prothrombinase. J Biol Chem 1979; 254: 10952-10962
    PubMedGoogle Scholar
  • 27 Tans G, Rosing J, van Dieijen G, Hemker HC. Conjectures on the mode of action of factors V and VIII. In: The regulation of coagulation Mann KG, Taylor FB. (eds) Elsevier/North Holland; New York : 1979: 173-185
  • 28 Krishnaswamy S, Church WR, Nesheim ME, Mann KG. Activation of human prothrombin by human prothrombinase. Influence of factor Va on the reaction mechanism. J Biol Chem 1987; 262: 3291-3299
    PubMedGoogle Scholar
  • 29 Seegers WH, Teng C-M, Ghosh A, Novoa E. Three aspects of prothrombin-activation related to protein M, ecarin, acutin, meizothrombin 1 and prethrombin 2. Ann NY Acad Sci 1981; 370: 453-467
    CrossrefPubMedGoogle Scholar
  • 30 Walker FJ, Esmon CT. The effect of prothrombin fragment 2 on the inhibition of thrombin by antithrombin III. J Biol Chem 1979; 254: 5618-5622
    PubMedGoogle Scholar
  • 31 Schoen P, Lindhout T. The in situ inhibition of prothombinase. formed human α-thrombin and meizothrombin (des FI) by antithrombin III and heparin. J Biol Chem 1987; 262: 11268-11274
    PubMedGoogle Scholar
  • 32 Pieters J, Pranssen J, Visch C, Lindhout T. Neutralization of heparin by prothrombin activation products. Thromb Res 1987; 45: 573-580
    CrossrefPubMedGoogle Scholar
  • 33 Magnusson S, Sottrup-Jensen L, Petersen TL, Claeys H. The primary structure of prothrombin, the role of vitamin K in bluod coagulation and a thrombin catalyzed negative feed-back control mechanism for limiting the activation of prothrombin. In: Prothrombin and related coagulation factors Hemker HC, Veltkamp JJ. (eds) Leiden University Press; Leiden: 1975: 25-46
  • 34 Patthy L, Trexler M, Váli Z, Bányai L, Váradi A. Kringles: modules specialized for protein binding. FEBS Lett 1984; 71: 131-136
    PubMedGoogle Scholar