Primary Structure of Human Coagulation Factor XIII
Factor XIII (fibrin stabilizing factor or fibrinoligase) is a plasma transglutaminase that plays an important role in the final stages of blood coagulation and the regulation of fibrinolysis. The molecule occurs in blood as a tetramer, a 2 b 2 (about 320 kD), consisting of two a subunits (75 kD each) and two b subunits (80 kD each) as estimated by SDS-polyacrylamide gel electrophoresis (Schwartz et al., 1973; Chung et al., 1974) (Fig. 1). The molecular complex is held together by noncovalent bonds (Schwartz et al., 1973). During the final stage of blood coagulation, thrombin converts the proenzyme (factor XIII) to an active form (factor XIIIa) by releasing an activation peptide (4 kD) from the N-terminus of each of the a subunits (Schwartz et al., 1973; Takagi and Doolittle, 1974). This reaction is stimulated by fibrin monomers (Lewis et al., 1985). In the presence of calcium ions, the activated a dimer dissociates from the b dimer (Cooke and Holbrook, 1974; Chung et al., 1974; Lorand et al., 1974) and binds to fibrin more tightly. Fibrin also lowers the calcium concentration required for the release of the b dimer (Credo et al., 1981). Calcium binds to the a subunit and unmasks its active site (Curtis et al., 1974; Cooke, 1974).
KeywordsFactor Xiii Blood Coagulation Factor Fibrin Monomer Human Blood Platelet Coagulation Factor Xiii
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- Carmassi, F., and Chung, S. I., 1983, Regulation of fibrinolysis by factor XIII, Prog. Fibrinolysis, 6:281–285.Google Scholar
- Folk, J. E., and Finlayson, J. S., 1977, The epsilon-(gamma-glutamyl)lysine crosslink and the catalytic role of transglutaminases, Adv. Prot. Chem., 31:1–133.Google Scholar
- Ichinose, A., Bottenus, R. E., Loeb, K. R., and Davie, E. W., 1987, Isolation and characterization of the genes for the a and b subunits of human factor XIII, Thromb. Haemostas., in press.Google Scholar
- Leonard, W. J., Depper, J. M., Crabtree, G. R., Rudikoff, S., Pumpbrey, J., Robb, R. J., Kronke, M., Svetlik, P. B., Peffer, N. J., Waldmann, T. A., and Greene, W. C., 1984, Molecular cloning and expression of cDNAs for the human interleukin-2 receptor, Nature, 311:626–631.PubMedCrossRefGoogle Scholar
- Medof, M. E., Lublin, D. M., Holers, V. M., Ayers, D. J., Getty, R. R., Leykam, J. F., Atkinson, J. P., and Tykocinski, M. L., 1987, Cloning and characterization of cDNAs encoding the complete sequence of decay-accelerating factor of human complement, Proc. Natl. Acad. Sci. USA. 84:2007–2011.PubMedCrossRefGoogle Scholar
- Schrode, J., Chung, S. I., and Folk, J. E., 1976, Thrombin cleavage products of human placental transglutaminase, Fed. Proc., 35:1487.Google Scholar
- Sixma, J. J., van den Berg, A., Schiphorst, M., Gueze, H. J., McDonagh, J., 1984, Immunocytochemical localization of albumin and factor XIII in thin cryo sections of human blood platelets, Thromb. Haemostas., 51:388–391.Google Scholar