Download PDF
Thromb Haemost 1991; 66(04): 446-452
DOI: 10.1055/s-0038-1646436
Review Article
Schattauer GmbH Stuttgart

The Autoactivation of Factor XII in the Presence of Long-Chain Saturated Fatty Acids – A Comparison with the Potency of Sulphatides and Dextran Sulphate

K A Mitropoulos
The MRC Epidemiology and Medical Care Unit, Northwick Park Hospital, Harrow, Middlesex, Oxford, UK
,
M P Esnouf
*   Nuffield Dept. of Clinical Biochemistry, The Radcliffe Infirmary, Oxford, UK
› Author Affiliations
Further Information

Publication History

Received 19 December 1990

Accepted 03 April 1991

Publication Date:
25 July 2018 (online)

Also available at
  PDF Download  Permissions and Reprints

Summary

The incubation of purified human factor XII (Hageman factor [HF]) in the presence of long-chain saturated fatty acids (FA) like stearate (C-18) or behenate (C-22) resulted in a time-dependent increase of amidolytic activity. The HF autoactivation progress curves were sigmoidal. The first order rate for the initial period was constant; this was followed by a period of decreasing rate and a plateau of zero rate. These progress curves were similar to those obtained on the incubation of HF in the presence of sulphatide vesicles or dextran sulphate. The initial rate of autoactivation of HF was dependent on the FA concentration of contact surface and increased with increasing concentration of HF. At constant concentration of contact surface and varying concentration of HF, autoactivation rates in the presence of behenate, sulphatide vesicles or dextran sulphate followed Michaelis-Menten kinetics. The Km values for all three contact surfaces were above the physiological plasma concentration of HF whereas the catalytic efficiency in the presence of behenate (0.034 εM-1s-1) was about % of that in the presence of sulphatide vesicles (0.053 εM-1s-1) and considerably higher than that in the presence of dextran sulphate (0.004 εM-1s-1). Long-chain saturated FA bound to human serum albumin at the high- or low-affinity sites are ineffective, whereas the crystalline non-bound stearate or behenate provided a potent contact surface. Since oleic acid or other unsaturated fatty acids did not promote autoactivation it is suggested that the requirement for an effective contact surface is one containing immobile negatively charged groups with a critical charge density such as that found in miscelles composed of FA in the crystalline phase. It is suggested that saturated FA on triglyceride-rich lipoproteins resulting from the action of lipoprotein lipase could provide these requirements.

 

  • References

  • 1 Berrettini M, Lômmle 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, Leuven: 1987. pp 473-95
    Google Scholar
  • 2 Griffin JH, Cochrane CG. Mechanisms for the involvement of high molecular weight kininogen in surface-dependent reactions of Hageman factor. Proc Natl Acad Sci (USA) 1976; 73: 2554-8
    CrossrefPubMedGoogle Scholar
  • 3 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
    PubMedGoogle Scholar
  • 4 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: 6097-104
    PubMedGoogle Scholar
  • 5 Kaplan AP, Austen KF. A pre-albumin activator of prekallikrein. J Immunol 1970; 105: 802-11
    PubMedGoogle Scholar
  • 6 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
    CrossrefPubMedGoogle Scholar
  • 7 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
    CrossrefPubMedGoogle Scholar
  • 8 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
    CrossrefPubMedGoogle Scholar
  • 9 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
    CrossrefPubMedGoogle Scholar
  • 10 Schiffman S, Lee P. Partial purification and characterization of contact activation co-factor. J Clin Invest 1975; 56: 1082-92
    CrossrefPubMedGoogle Scholar
  • 11 Meier HL, Pierce JV, Colman RW, Kaplan AP. Activation and function of human Hageman factor. The role of high molecular weight kininogen and prekallikrein. J Clin Invest 1977; 60: 18-31
    CrossrefPubMedGoogle Scholar
  • 12 Østerud B, Bouma BN, Griffin JH. Human blood coagulation factor IX. Purification properties and mechanism of activation by activated factor XI. J Biol Chem 1978; 253: 5946-51
    PubMedGoogle Scholar
  • 13 Radcliffe R, Bagdasarian A, Colman R, Nemerson Y. Activation of bovine factor VII by Hageman factor fragments. Blood 1977; 50: 611-7
    PubMedGoogle Scholar
  • 14 Seligsohn U, Østerud 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
    CrossrefPubMedGoogle Scholar
  • 15 Gjønnaess H. Cold-promoted activation of factor VII. IV. Relation to the coagulation system. Thromb Diathes Haemorrh 1972; 28: 194-205
    PubMedGoogle Scholar
  • 16 Mitropoulos KA, Martin JC, Burgess AI, Esnouf MP, Stirling Y, Howarth DJ, Reeves BEA. The increased rate of activation of factor XII in late pregnancy can contribute to the increased reactivity of factor VII. Thromb Haemostas 1990; 63: 349-55
    PubMedGoogle Scholar
  • 17 España F, Ratnoff OD. Activation of Hageman factor (factor XII) by sulfatides and other agents in the absence of plasma proteases. J Lab Clin Med 1983; 102: 31-45
    PubMedGoogle Scholar
  • 18 Tans G, Rosing J, Griffin JH. Sulfatide-dependent autoactivation of human blood coagulation factor XII (Hageman factor). J Biol Chem 1983; 258: 8215-22
    PubMedGoogle Scholar
  • 19 Tankersley DL, Finlayson JS. Kinetics of activation and autoactivation of human factor XII. Biochemistry 1984; 23: 273-9
    CrossrefPubMedGoogle Scholar
  • 20 Silverberg M, Dunn JT, Garen L, Kaplan AP. Autoactivation of human Hageman factor. Demonstration utilizing a synthetic substrate. J Biol Chem 1980; 255: 7281-6
    PubMedGoogle Scholar
  • 21 Griep MA, Fujikawa K, Nelsestuen GL. Binding and activation properties of human factor XII, prekallikrein and derived peptides with acidic lipid vesicles. Biochemistry 1985; 24: 4124-30
    CrossrefPubMedGoogle Scholar
  • 22 Mitropoulos KA, Martin JC, Reeves BEA, 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
    PubMedGoogle Scholar
  • 23 Fujikawa K, Davie EW. Human factor XII (Hageman factor). Methods Enzymol 1981; 80: 198-211
    PubMedGoogle Scholar
  • 24 Fujikawa K, McMullen BA. Amino acid sequence of human factor XIIa. J Biol Chem 1983; 258: 10924-33
    PubMedGoogle Scholar
  • 25 Miller G, Silverberg M, Kaplan AP. Autoactivatability of human Hageman factor (Factor XII). Biochem Biophys Res Commun 1980; 92: 803-10
    CrossrefPubMedGoogle Scholar
  • 26 Spector AA, John K, Fletcher JE. Binding of long-chain fatty acids to bovine serum albumin. J Lipid Res 1969; 10: 56-67
    PubMedGoogle Scholar
  • 27 Cistola DP, Small DM, Hamilton JA. Carbon 13 NMR studies of saturated fatty acids bound to bovine serum albumin. I. The filling of individual fatty acid binding sites. J Biol Chem 1987; 262: 10971-9
    PubMedGoogle Scholar
  • 28 Cistola DP, Small DM, Hamilton JA. Carbon 13 NMR studies of saturated fatty acids bound to bovine serum albumin. II. Electrostatic interactions in individual fatty acid binding sites. J Biol Chem 1987; 262: 10980-5
    PubMedGoogle Scholar
  • 29 Cistola DP, Sacchettini JC, Banaszak LJ, Walsh MT, Gordon JI. Fatty acid interactions with rat intestinal and liver fatty acid-binding proteins expressed in Escherichia coli. A comparative 13C NMR study. J Biol Chem 1989; 264: 2700-10
    PubMedGoogle Scholar
  • 30 Doody MC, Pownall HJ, Kao YJ, Smith LC. Mechanism and kinetics of transfer of a fluorescent fatty acid between single-walled phosphatidylcholine vesicles. Biochemistry 1980; 19: 108-16
    CrossrefPubMedGoogle Scholar
  • 31 Carey MC, Small DM, Bliss CM. Lipid digestion and absorption. Annu Rev Physiol 1983; 45: 651-77
    CrossrefPubMedGoogle Scholar
  • 32 Abrahamsson S, Pascher I, Larsson K, Karlsson KA. Molecular arrangements in glycosphingolipids. Chem Phys Lipids 1972; 8: 152-79
    CrossrefPubMedGoogle Scholar
  • 33 Hojima Y, Tankersley DL, Miller-Anderson M, Pierce JV, Pisano JY. Enzymatic properties of human Hageman factor fragment with Plasma Prekallikrein and synthetic substrates. Thromb Res 1980; 18: 417-30
    CrossrefPubMedGoogle Scholar
  • 34 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 αVIIa and higher flux within the coagulation pathway. Atherosclerosis 1987; 63: 43-52
    CrossrefPubMedGoogle Scholar
  • 35 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
    CrossrefPubMedGoogle Scholar
  • 36 Blanchette-Mackie EJ, Scow RO. Retention of lypolytic products in chylomicrons incubated with lipoprotein lipase: electron microscope study. J Lipid Res 1976; 17: 57-67
    PubMedGoogle Scholar
  • 37 Brecher P, Saouaf R, Sugarman M, Eisenberg D, LaRosa K. Fatty acid transfer between multilamellar liposomes and fatty acid-binding proteins. J Biol Chem 1984; 259: 13395-401
    PubMedGoogle Scholar
  • 38 Scow RO, Olivecrona T. Effect of albumin on products formed from chylomicron triacylglycerol by lipoprotein lipase in vitro. Biochim Biophys Acta 1977; 487: 472-86
    CrossrefPubMedGoogle Scholar
  • 39 Sammett D, Tall AR. Mechanisms of enhancement of cholesteryl ester transfer protein activity by lipolysis. J Biol Chem 1985; 260: 6687-97
    PubMedGoogle Scholar