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DOI: 10.1055/s-0038-1645045
The Increased Rate of Activation of Factor XII in Late Pregnancy Can Contribute to the Increased Reactivity of Factor VII
Publikationsverlauf
Received 26. Oktober 1989
Accepted after revision 23. Januar 1990
Publikationsdatum:
30. Juni 2018 (online)
![](https://www.thieme-connect.de/media/10.1055-s-00035024/199003/lookinside/thumbnails/10-1055-s-0038-1645045-1.jpg)
Summary
The amidolytic activity of enzymes derived from factor XII (XIIa) was 3-fold higher in plasmas collected during pregnancy than from control subjects. Factor VII coagulant activity (VIIc) and XIIa increased in both kinds of plasmas on incubation on ice for 24 h (cold activation). These increases could be attributed to the decreased potency of C1 inhibitor (C1INH). However, variations in the concentration of C1INH and of factor XII could not explain the differences in VIIc and in XIIa between late pregnancy and control plasmas following cold activation under the same conditions. It is concluded that in vitro the increased amount of contact surface in the late pregnancy plasma promotes a higher rate of generation of XIIa and consequently a higher rate of activation of factor VII. The increased amount of contact surface could also be responsible for the increased concentration of XIIa in non-treated plasma from late pregnancy and could contribute in vivo to the higher reactivity of factor VII in this condition.
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References
- 1 Berrettini M, Lämmle B, Griffin JH. Initiation of coagulation and relationships between intrinsic and extrinsic coagulation pathways. In: Thrombosis XIth Congress Haemostasis Verstraete M, Vermylen J, Lijnen R, Arnout J. (eds) Leuven University Press; Leuvenz: 1987: 473-95
- 2 Margolis J. The interrelationship of coagulation of plasma and release of peptides. Ann N Y Acad Sci 1963; 104: 133-45
- 3 Kluft C. Determination of prekallikrein in human plasma: optimal conditions for activating prekallikrein. J Lab Clin Med 1978; 91: 83-95
- 4 Bock PE, Srinivasan KR, Shore JD. Activation of intrinsic blood coagulation by ellagic acid: insoluble ellagic acid-metal ion complexes are the activating species. Biochemistry 1981; 20: 7258-66
- 5 Fujikawa K, Heimark RL, Kurachir K, Davie EW. Activation of bovine factor XII (Hageman factor) by plasma kallikrein. Biochemistry 1980; 19: 1322-30
- 6 Dunn JT, Silverberg M, Kaplan AP. The cleavage and formation of activated human Hageman factor by autodigestion and by kallikrein. J Biol Chem 1982; 257: 1779-84
- 7 Mandle Jr R, Kaplan AP. Hageman factor substrates. Human plasma prekallikrein: mechanism of activation by Hageman factor and participation in Hageman factor-dependent fibrinolysis. J Biol Chem 1977; 252: 6097-6104
- 8 Kaplan AP, Austen KF. A pre-albumin activator of prekallikrein. J Immunol 1970; 105: 802-11
- 9 Ratnoff OD, Davie EW, Mallett DL. Studies on the action of Hageman factor: evidence that activated Hageman factor in turn activates plasma thromboplastin antecedent. J Clin Invest 1961; 40: 803-19
- 10 Rosenthal RL, Dreskin OH, Rosenthal N. New haemophilia-like disease caused by deficiency of a third plasma thromboplastin factor. Proc Soc Exp Biol Med 1953; 82: 171-4
- 11 Schiffman S, Lee P. Partial purification and characterization of contact activation cofactor. J Clin Invest 1975; 56: 1082-92
- 12 Meier HL, Pierce JV, Colman RW, Kaplan AP. Activation and function of human Hageman factor. Thr role of high molecular weight kininogen and prekallikrein J Clin Invest 1977 60. 18-31
- 13 Cochrane CG, Revak SD, Wuepper KD. Activation of Hageman factor in solid and fluid phases. A critical role of kallikrein. J Exp Med 1973 138. 1564-83
- 14 Revak SD, Cochrane CG, Griffin JH. The binding and cleavage characteristics of human Hageman factor during contact activation. A comparison of normal plasma with plasmas deficient in factor XI, prekallikrein or high molecular weight kininogen. J Clin Invest 1977 59. 1167-75
- 15 Revak SD, Cochrane CG. The relationship of structure and function in human Hageman factor. The association of enzymatic and binding activities with separate regions of the molecule. J Clin Invest 1976 57. 852-60
- 16 Revak SD, Cochrane CG, Bouma BN, Griffin JH. Surface and fluid phase activities of two forms of activated Hageman fartnr produced during contact activation of plasma. J Exp Med 1978; 147: 719-29
- 17 Radcliffe R, Bagdasarian A, Colman R, Nemerson Y. Activation of bovine factor VII by Hageman factor fragments. Blood 1977; 50: 611-7
- 18 Seligsohn U, Osterudz B, Brown SF, Griffin JH, Rapaport SI. Activation of human factor VII in plasma and in purified systems. Roles of activated factor IX, kallikrein and activated factor XII. J Clin Invest 1979 64. 1056-65
- 19 Gjonnaess H. Cold-promoted activation of factor VII. IV. Relation to the coagulation system. Thromb Diathes Haemorrh 1972 28. 194-205
- 20 Masys DR, Bajaj SP, Rapaport SI. Activation of human factor VII by activated factors IX and X. Blood 1982; 60: 1143-50
- 21 Radcliffe R, Nemerson Y. Activation and control of factor VIT by activated factor X and thrombin. Isolation and characteiizaLion of a single chain form of factor VH. J Biol Chem 1975 250. 388-95
- 22 Pixlcy RA, Schapira M, Colman RW. The regulation of human factor XIIa by plasma proteinase inhibitors. J Biol Chem 1985; 260: 1723-9
- 23 de Agostini A, Lijnen HR, Pixley RA, Colman RW, Schapira M. Inactivation of factor XII active fragment in normal plasma. Predominant role of CT-inhibitor. J Clin Invest 1984 73. 1542-9
- 24 Schapira M, Scott CF, Colman RW. Contribution of plasma protease inhibitors to the inactivations of kallikrein in plasma. J Clin Invest 1982; 69: 462-8
- 25 Mitropoulos KA, Martin JC, Reeves AB E, Esnouf MP. The activation of the contact phase of coagulation by physiological surfaces in plasma: the effect of large negatively charged liposomal vesicles. Blood 1989; 73: 1525-33
- 26 Fujikawa K, Davie EW. Human factor XII (Hageman factor). Methods Enzymol 1981; 80: 198-211
- 27 Fujikawa K, McMullen EBA. Amino acid sequence of human factor XIIa . J Biol Chem 1983; 258: 10924-33
- 28 Sim RB, Reboul A. Preparation and properties of human Cl inhibitor. Methods Enzymol 1981; 80: 43-54
- 29 Silverberg SA, Nemerson Y, Zur M. Kinetics of the activation of bovine coagulation factor X by components of the extrinsic pathway. Kinetic behaviour of two-chain factor VII in the presence and absence of tissue factor. J Biol Chem 1977 252. 8481-8
- 30 Mitropoulos KA, Esnouf MP, Meade TW. Increased factor VII coagulant activity in the rabbit following diet-induced hypercholes-terolaemia. Evidence for increased conversion of VII to aVIIa and higher flux within the coagulation pathway. Atherosclerosis 1987 63. 43-52
- 31 Rao LV M, Bajaj SP, Rapaport SI. Activation of human factor VII during clotting in vitro. Blood 1985; 65: 218-26
- 32 Tans G, Janssen-Claessen T, Rosing J, Griffin JH. Studies on the effect of serine protease inhibitors on activated contact factors. Application in amidolytic assays for factor XIIa plasma kallikrein and factor XIa. Eur J Biochem 1987 164. 637-42
- 33 Bieth J. Some kinetic consequences of the tight binding of protein proteinase-inhibitors to proteolytic enzymes and their application to the determination of dissociation constants. In: “Protease Inhibitors” Baayer-Symposium V Springer-Verlag; Berlin: 1974: 463-9
- 34 Laurell CB. Eiectroimmuno assay. Scand J Clin Lab Invest 1972; 29 (124) 21-37
- 35 Kitz R, Wilson IB. Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase. J Biol Chem 1962; 237: 3245-9
- 36 Gordon EM, Ratnoff OD, Jones PK. The role of augmented Hageman factor (factor XII) titers in the cold-promoted activation of factor VII and spontaneous shortening of the prothrombin time in women using oral contraceptives. J Lab Clin Med 1982; 99: 363-9
- 37 Miller GJ, Walter SJ, Stirling Y, Thompson SG, Esnouf MP, Meade TW. Assay of factor VII activity by two techniques: evidence for increased conversion of VII to VIIa in hyperlipidaemia, with possible implications for ischaemic heart disease. Br J Haematol 1985; 59: 249-58
- 38 Mitropoulos KA. Hypercoagulability and factor VII in hypertriglyceridemia. Semin Thromb Haemostas 1988; 14: 246-52
- 39 Mitropoulos KA, Esnouf MP. Turnover of factor X and of prothrombin in rabbits fed on a standard or cholesterol-supplemented diet. Biochem J 1987; 244: 263-9
- 40 Weiss R, Silverberg M, Kaplan AP. The effect of C1 inhibitor upon Hageman factor autoactivation. Blood 1986; 68: 239-43
- 41 Harpel PC. Blood proteolytic enzyme inhibitors: their role in modulating coagulation and fibrinolytic enzyme pathways. In: Haemostasis and Thrombosis Colman RW, Hirsch J, Marder VJ, Salzman EW. (eds). J B Lippincott Co; Philadelphia, PA: 1982: 738-47
- 42 Harpel PC. Human plasma α2-macroglobulin. An inhibitor of plasma kallikrein. J Exp Med 1970 132. 329-52
- 43 Harpel PC, Lewin MF, Kaplan AP. Distribution of plasma kallikrein between C1 inactivator and α2-macrogIobulin kallikrein complexes. J Biol Chem 1985; 260: 4257-63