Download PDF
Thromb Haemost 2003; 89(04): 632-636
DOI: 10.1055/s-0037-1613569
Blood Coagulation, Fibrinolysis and Cellular Haemostasis
Schattauer GmbH

Protofibrils within fibrin fibres are packed together in a regular array

Giulio Caracciolo
1   Istituto di Fisica and INFM, Università Cattolica S. Cuore, Rome, Italy
,
Marco De Spirito
1   Istituto di Fisica and INFM, Università Cattolica S. Cuore, Rome, Italy
,
Agostina Congiu Castellano
2   Dipartimento di Fisica and INFM, Università di Roma ‘La Sapienza’, Rome, Italy
,
Daniela Pozzi
2   Dipartimento di Fisica and INFM, Università di Roma ‘La Sapienza’, Rome, Italy
,
Gino Amiconi
3   CNR Centre for Molecular Biology and Department of Biochemical Sciences, Università di Roma ‘La Sapienza’, Rome, Italy
,
Angela De Pascalis
3   CNR Centre for Molecular Biology and Department of Biochemical Sciences, Università di Roma ‘La Sapienza’, Rome, Italy
,
Ruggero Caminiti
4   Dipartimento di Chimica and INFM, Università di Roma ‘La Sapienza’, Rome, Italy
,
Giuseppe Arcovito
1   Istituto di Fisica and INFM, Università Cattolica S. Cuore, Rome, Italy
› Author Affiliations
Further Information

Publication History

Received 16 October 2002

Accepted after revision 27 January 2003

Publication Date:
07 December 2017 (online)

    Permissions and Reprints

Summary

The inner structure of fibrin fibres grown from fibrinogen solution activated by human α-thrombin was investigated by means of an Energy Dispersive X-ray Diffraction technique. The experiments show evidence for the well-characterized 22.5 nm repeat distance, which indicates the high order of protofibril arrangement in the longitudinal direction of fibres. The diffraction pattern also manifested a further pronounced peak at 18.1 nm (and its second order reflection at 18.1/√2) demonstrating the existence in fibrin of a high degree of lateral order. The reported results directly confirm, on unperturbed wet samples, that protofibrils closely associate giving rise to a crystalline axial and equatorial packing according to the conclusions of the multibundle model.

Theme paper: Part of this work was originally presented at the joint meetings of the 16th International Congress of the International Society of Fibrinolysis and Proteolysis (ISFP) and the 17th International Fibrinogen Workshop of the International Fibrinogen Research Society (IFRS) held in Munich, Germany, September, 2002.

Keywords

Coarse fibrin gel - protofibril - fibrin fibre - EDXD
 

  • References

  • 1 Ferry JD, Morrison PR. Preparation and properties of serum and plasma proteins. VIII. The conversion of human fibrinogen to fibrin under variuos conditions. J Am Chem Soc 1947; 69: 388-400.
    CrossrefPubMedGoogle Scholar
  • 2 Carr ME, Kaminski M, McDonagh J, Gabriel DA. Influence of ionic strength, peptide release and calcium ions on the structure of reptilase and thrombin derived fibrin gels. Thromb Haemost 1985; 34: 159-65.
    Article in Thieme ConnectPubMedGoogle Scholar
  • 3 Kaminski M, Siebenlist KR, Mosesson MW. Evidence for thrombin enhancement of fibrin polymerization that is independent of ist catalytic activity. J Lab Clin Med 1991; 117: 218-25.
    PubMedGoogle Scholar
  • 4 Weisel JW, Nagaswami C. Computer mode-ling of fibrin polymerization kinetics correlated with electron microscopy and turbidity observations: clot structure and assembly are kinetically controlled. Biophys J 1992; 63: 111-28.
    CrossrefPubMedGoogle Scholar
  • 5 Blombäck B, Carlsson K, Fatah B, Hessel B, Procyk R. Fibrin in human plasma: gel architectures governed by rate and nature of fibrinogen activation. Thromb Res 1994; 75: 521-38.
    CrossrefPubMedGoogle Scholar
  • 6 Weisel JW. The electron microscope band pattern of human fibrin: various stains, lateral order, and carbohydrate localization. J Ultr Molec Struc Res 1986; 96: 176-88.
    PubMedGoogle Scholar
  • 7 Di Stasio E, Nagaswami C, Weisel JW, Di Cera E. Cl-regulates the structure of fibrin clot. Biophys J 1998; 75: 1973-9.
    CrossrefPubMedGoogle Scholar
  • 8 Stryer L, Cohen C, Langridge R. Axial period of fibrinogen. Nature 1963; 197: 793-4.
    CrossrefPubMedGoogle Scholar
  • 9 Doolittle RF. Fibrinogen and fibrin. Annu Rev Biochem 1984; 53: 195-236.
    CrossrefPubMedGoogle Scholar
  • 10 Mosesson MW, Siebenlist KR, Meh DA. The structure and biological features of fibrinogen and fibrin. Ann New York Acad Sci 2001; 936: 11-30.
    PubMedGoogle Scholar
  • 11 Ferri F, Greco M, Arcovito G, Andreasi Bassi F, De Spirito M, Paganini E, Rocco M. Growth kinetics and structure of fibrin gels. Phys Rev E 2000; 63: 1-17.
    PubMedGoogle Scholar
  • 12 Wolfe JK, Waugh DF. Relations between enzymatic and association reactions in the development of bovine fibrin clot structure. Arch Biochem Biophys 1981; 211: 125-42.
    CrossrefPubMedGoogle Scholar
  • 13 Mullin JL, Gorkun OV, Lord ST. Decreased lateral aggregation of a variant recombinant fibrinogen provide insight into the polymerization mechanism. Biochemistry 2000; 39: 9843-9.
    CrossrefPubMedGoogle Scholar
  • 14 Ferri F, Greco M, Arcovito G, De Spirito M, Rocco M. Structure of fibrin gels studied by elastic light scattering techniques: dependence of fractal dimension, gel crossover length, fiber diameter, and fiber density on monomer concentration. Phys Rev E 2002; 66 011913 1-13.
    PubMedGoogle Scholar
  • 15 Müller MF, Ferry JD. Small-angle X-ray scattering of fibrin film: comparison of the fine coarse films prepared with thrombin and ancrod. Biopolymers 1989; 28: 1011-8.
    CrossrefPubMedGoogle Scholar
  • 16 Blombäck B, Carlsson K, Hessel B, Liljeborg A, Aslund N. Native fibrin gel networks observed by 3D microscopy, permeation and turbidity. Biochim Biophys Acta 1989; 997: 96-110.
    CrossrefPubMedGoogle Scholar
  • 17 McKee PA, Mattock P, Hill RL. Subunit structure of human fibrinogen, soluble fibrin, and cross-linked insoluble fibrin. Proc Natl Acad Sci USA 1970; 66: 738-44.
    CrossrefPubMedGoogle Scholar
  • 18 Yang Z, Mochalkin I, Doolittle RF. A model of fibrin formation based on crystal structures of fibrinogen and fibrin fragments complexed with synthetic peptides. Proc Natl Acad Sci USA 2000; 97: 14156-61.
    CrossrefPubMedGoogle Scholar
  • 19 Torbet J, Freyssent JM, Hudry-Clergeon GH. Oriented fibrin gels formed by polymerization in strong magnetic fields. Nature 1981; 289: 1189-93.
    PubMedGoogle Scholar
  • 20 Hudry-Clergeon G, Freyssinet J-M, Torbet J, Marx J. Orientation of fibrin in strong magnetic fields. Ann New York Acad Sci 1983; 408: 380-7.
    CrossrefPubMedGoogle Scholar
  • 21 Hermans J. Models of fibrin. Proc Natl Acad Sci USA 1979; 76: 1189-93.
    CrossrefPubMedGoogle Scholar
  • 22 De Cristofaro R, Di Cera E. Effect of protons on the amidase activity of human α-thrombin. J Mol Biol 1990; 226: 1077-85.
    PubMedGoogle Scholar
  • 23 Caminiti R, Sadun C, Rossi V, Cillocco F, Bencivenni L. A new technique for the study of phase transition by means of energy dispersive X-ray diffraction: application to polymeric samples. J Macromol Sci Phys 1996; 835: 199-213.
    PubMedGoogle Scholar
  • 24 Caracciolo G, Amiconi G, Bencivenni L, Boumis G, Caminiti R, Finocchiaro E, Maras B, Paolinelli C, Congiu Castellano A. Conformational study of proteins by SAXS and EDXD: the case of trypsin and trypsino-gen. Eur Biophys J 2001; 30: 163-70.
    CrossrefPubMedGoogle Scholar
  • 25 Kerker M. The Scattering of Light and Other Electromagnetic Radiation. New York: Academic Press; 1969
    Google Scholar
  • 26 Caminiti R, Rossi Albertini V. Review on the kinetics of phase transition observed by energy dispersive X-ray diffraction. Int Rev Phys Chem 1999; 18 (02) 263-99.
    CrossrefPubMedGoogle Scholar
  • 27 Roska FJ, Ferry JD. Studies of fibrin film. II. Small-angle X-ray scattering. Biopolymers 1982; 21: 1833-45.
    CrossrefPubMedGoogle Scholar
  • 28 Weisel JW, Phillips GN, Cohen C. The structure of fibrinogen and fibrin: II. Architecture of the fibrin clot. Ann New York Acad Sci 1983; 408: 367-79.
    CrossrefPubMedGoogle Scholar
  • 29 Sakharov DV, Rijken DC. Superficial accumulation of plasminogen during plasma clot lysis. Circulation 1995; 92: 1883-9.
    CrossrefPubMedGoogle Scholar
  • 30 Sakharov DV, Nagelkerke JF, Rijken DC. Rearrangements of the fibrin network and spatial distribution of fibrinolytic components during plasma clot lysis. J Biol Chem 1996; 271: 2133-8.
    CrossrefPubMedGoogle Scholar
  • 31 Carrell NA, Erickson HP, McDonagh J. Electron microscopy and hydrodynamic properties of factor XIII subunits. J Biol Chem 1989; 264: 551-6.
    PubMedGoogle Scholar
  • 32 Markland FS. Snake venoms and the hemosta-tic systems. Toxicon 1998; 36: 1749-800.
    CrossrefPubMedGoogle Scholar