Download PDF
Hamostaseologie 2002; 22(01): 08-13
DOI: 10.1055/s-0037-1622011
Original Article
Schattauer GmbH

Blutgerinnungsfaktor XIII: Aktivierung, Substrate und Struktur einer Transglutaminase

Blood coagulation factor XIII: Activation, substrates and structure of a transglutaminase
T. Sicker
,
R. Hilgenfeld
Institut für Molekulare Biotechnologie, Jena
› Author Affiliations
Further Information

Publication History

Publication Date:
29 December 2017 (online)

Also available at
    Permissions and Reprints

Zusammenfassung

Der Blutgerinnungsfaktor XIII wurde lange Zeit wenig beachtet, und die Forschung auf dem Gebiet der Transglutaminasen wurde vernachlässigt. Durch die interessanten Ergebnisse der vergangenen Jahre wird jedoch deutlich, wie wichtig dieses Protein für den dauerhaften Wundverschluss ist. Auch wenn Feinregulation von Aktivierung und lokal begrenzter Aktivität noch nicht vollständig verstanden sind, zeigen die bereits gefundenen Mechanismen einen hohen Grad an Komplexität. In dieser übersicht werden jüngste biochemische und strukturelle Ergebnisse zum Faktor XIII diskutiert.

Summary

For a long time blood coagulation factor XIII did not get the attention it deserves, and research in the field of transglutaminases was neglected. The interesting results obtained in recent years demonstrate the importance of this protein for the stabilization of a blood clot. The accurate regulation of activation and of localization of factor XIII is not fully understood. Yet the proposed mechanisms suggest a high degree of complexity. In this review, recent biochemical and structural results on factor XIII are discussed.

Schlüsselwörter

Faktor XIII - Blutgerinnung - Transglutaminase

Keywords

Factor XIII - blood coagulation - transglutaminase
 

  • Literatur

  • 1 Adany R, Antal M. Three different cell types can synthesize factor XIII subunit A in the human liver. Thromb Haemost 1996; 76: 74-6.
    PubMedGoogle Scholar
  • 2 Ando Y, Imamura S, Yamagata Y, Kitahara A, Saji H, Murachi T, Kannagi R. Platelet factor XIII is activated by calpain. Biochem Biophys Res Commun 1987; 144: 484-90.
    CrossrefPubMedGoogle Scholar
  • 3 Ariens RAS, Kohler HP, Mansfield MW, Grant PJ. Subunit antigen and activity levels of blood coagulation factor XIII in healthy individuals. Arterioscler Thromb Vasc Biol 1999; 19: 2012-6.
    CrossrefPubMedGoogle Scholar
  • 4 Carrell NA, Erickson HP, McDonagh J. Electron microscopy and hydrodynamic properties of factor XIII subunits. J Biol Chem 1989; 264: 551-6.
    PubMedGoogle Scholar
  • 5 Catto AJ, Kohler HP, Bannan S, Strickland M, Carter A, Grant PJ. Factor XIII Val 34 Leu: a novel association with primary intracerebral hemorrhage. Stroke 1998; 29: 813-6.
    CrossrefPubMedGoogle Scholar
  • 6 Credo RB, Curtis CG, Lorand L. Ca2+-related regulatory function of fibrinogen. Proc Natl Acad Sci USA 1978; 75: 675-82.
    PubMedGoogle Scholar
  • 7 Elbaz A, Poirier O, Canaple S, Chedru F, Cambien F, Amarenco P. The association between the Val34Leu polymorphism in the factor XIII gene and brain infarction. Blood 2000; 95: 586-91.
    PubMedGoogle Scholar
  • 8 Fox BA, Yee VC, Pedersen LC, Le Trong I, Bishop PD, Stenkamp RE, Teller DC. Identification of the calcium binding site and a novel ytterbium site in blood coagulation factor XIII by X-ray crystallography. J Biol Chem 1999; 274: 4917-23.
    CrossrefPubMedGoogle Scholar
  • 9 Greenberg CS, Miraglia CC. The effect of fibrin polymers on thrombin catalyzed plasma factor XIII formation. Blood 1985; 66: 466-9.
    PubMedGoogle Scholar
  • 10 Greenberg CS, Achyuthan KE, Rajagopalan S, Pizzo SV. Characterization of the fibrin polymer structure that accelerates thrombin cleavage of plasma factor XIII. Arch Biochem Biophys 1988; 262: 142-8.
    CrossrefPubMedGoogle Scholar
  • 11 Hilgenfeld R, Liesum A, Storm R, Metzner HJ, Karges HE. Crystallization of blood coagulation factor XIII by an automated procedure. FEBS Lett 1990; 265: 110-2.
    CrossrefPubMedGoogle Scholar
  • 12 Hornyak TJ, Bishop PD, Shafer JA. α-Thrombin-catalyzed activation of human platelet factor XIII: Relationship between proteolysis and factor XIIIa activity. Biochemistry 1989; 28: 7326-32.
    CrossrefPubMedGoogle Scholar
  • 13 Hornyak TJ, Shafer JA. Interactions of factor XIII with fibrin as substrate and cofactor. Biochemistry 1992; 31: 423-9.
    CrossrefPubMedGoogle Scholar
  • 14 Ikematsu S. An approach to the metabolism of factor XIII. Acta Haematol (Basel) 1981; 33: 299-301.
    PubMedGoogle Scholar
  • 15 Kohler HP, Stickland NH, Ossei-Gering N, Carter A, Mikkola H, Grant PJ. Association of a common polymorphism in the factor XIII gene with myocardial infarction. Thromb Haemost 1998; 79: 8-13.
    Article in Thieme ConnectPubMedGoogle Scholar
  • 16 Lorand L, Jeong JM, Radek JT, Wilson J. Human plasma factor XIII: Subunit interactions and activation of zymogen. Methods Enzymol 1993; 222: 22-35.
    PubMedGoogle Scholar
  • 17 Mikkola H, Syrjälä M, Rasi V, Vahtera E, Hämäläinen E, Peletonen L, Palotie A. Deficiency in the A-subunit of coagulation factor XIII: Two novel point mutations demonstrate different effects on transcript levels. Blood 1994; 84: 517-25.
    PubMedGoogle Scholar
  • 18 Moaddel M, Farrell DH, Daugherty MA, Fried MG. Interactions of human fibrinogens with factor XIII: Roles of calcium and the γ’ peptide. Biochemistry 2000; 39: 6698-705.
    CrossrefPubMedGoogle Scholar
  • 19 Mosesson MW, Finlayson JS, Umfleet RA. Human fibrinogen heterogeneities: Identification of chain variants. J Biol Chem 1972; 247: 5223-7.
    PubMedGoogle Scholar
  • 20 Murray RK, Granner DK, Mayes PA, Rodwell VW. Haper‛s Biochemistry. Stamford: Appletton & Lange; 1999
    Google Scholar
  • 21 Muszbek L, Yee VC, Hevessy Z. Blood coagulation factor XIII: structure and function. Thromb Res 1999; 94: 271-305.
    CrossrefPubMedGoogle Scholar
  • 22 Nagy JA, Kradin RL, McDonagh J. Biosynthesis of factor XIII A and B subunits. Adv Exp Med Biol 1988; 231: 29-49.
    PubMedGoogle Scholar
  • 23 Nishigaki T, Omoto K, Juji T. Genetic polymorphism of the A subunit of human coagulation factor XIII in Japanese. Jap J Hum Genet 1981; 26: 237-41.
    CrossrefPubMedGoogle Scholar
  • 24 Noguchi K, Ishikawa K, Yokoyama K, Ohtsuka T, Nio N, Suzuki E. Crystal structure of red sea bream transglutaminase. J Biol Chem 2001; 276: 12055-9.
    CrossrefPubMedGoogle Scholar
  • 25 Pedersen LC, Yee VC, Bishop PD, Le Trong I, Teller DC, Stenkamp RE. Transglutaminase factor XIII uses proteinase-like catalytic triad to crosslink macromolecules. Prot Sci 1994; 3: 1131-5.
    CrossrefPubMedGoogle Scholar
  • 26 Polgar J, Hidasi V, Muszbek L. Non-proteolytic activation of cellular protransglutaminase (placenta macrophage Factor XIII). Biochem J 1990; 267: 557-60.
    CrossrefPubMedGoogle Scholar
  • 27 Saito M, Asakura H, Yoshida T. et al A familial factor XIII subunit B deficiency. Br J Haematol 1990; 74: 290-4.
    CrossrefPubMedGoogle Scholar
  • 28 Sicker T. Metallbindung, Aktivierung und Inhibierung von Blutgerinnungsfaktor XIII. Diplomarbeit Universität Jena; 1999
    Google Scholar
  • 29 Weisberg LJ, Shiu DT, Conkling PR, Shuman MA. Identification of normal peripheral blood monocytes and liver as sites of synthesis of coagulation factor XIII A-chain. Blood 1987; 70: 579-82.
    PubMedGoogle Scholar
  • 30 Weiss MS, Metzner HJ, Hilgenfeld R. Two nonprolin cis peptide bonds may be important for factor XIII function. FEBS Lett 1998; 423: 291-6.
    CrossrefPubMedGoogle Scholar
  • 31 Weiss MS, Sicker TS, Djinovic-Carugo K, Hilgenfeld R. On the routine use of soft X-rays in macromolecular crystallography. Acta Cryst 2001; D57: 689-95.
    PubMedGoogle Scholar
  • 32 Yee VC, Pedersen LC, Bishop PD, Stenkamp RE, Teller DC. Structural evidence that the activation peptide is not released upon thrombin cleavage of factor XIII. Thromb Res 1995; 78: 389-97.
    CrossrefPubMedGoogle Scholar
  • 33 Yee VC, Pedersen L, Le Trong I, Bishop PD, Senkamp RE, Teller DC. Three-dimensional structure of a transglutaminase: Human blood coagulation factor XIII. Proc Natl Acad Sci USA 1994; 91: 7296-300.
    CrossrefPubMedGoogle Scholar
  • 34 Yorifuji H, Anderson K, Lynch GW, Van deWater L, McDonagh J. B protein of factor XIII: Differentiation between free B and complexed B. Blood 1988; 72: 1645-50.
    PubMedGoogle Scholar