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Thromb Haemost 1989; 62(03): 875-879
DOI: 10.1055/s-0038-1651020
Original Article
Schattauer GmbH Stuttgart

The Polymerization of Fibrin Prepared from Fibrinogen Haifa (γ275Arg→His)

Kevin R Siebenlist
*   The Sinai-Samaritan Medical Center, University of Wisconsin Medical School, Milwaukee Clinical Campus, Milwaukee, Wisconsin, USA
,
Michael W Mosesson
*   The Sinai-Samaritan Medical Center, University of Wisconsin Medical School, Milwaukee Clinical Campus, Milwaukee, Wisconsin, USA
,
James P Di Orio
*   The Sinai-Samaritan Medical Center, University of Wisconsin Medical School, Milwaukee Clinical Campus, Milwaukee, Wisconsin, USA
,
Shulamith Tavori
**   The Rambam Medical Center, Haifa, Israel
,
lllana Tatarsky
**   The Rambam Medical Center, Haifa, Israel
,
Abraham Rimon
**   The Rambam Medical Center, Haifa, Israel
› Author Affiliations
Further Information

Publication History

Received 15 February 1989

Accepted after revision 30 June 1989

Publication Date:
30 June 2018 (online)

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Summary

Fibrinogen Haifa is a congenital heterozygous fibinogen variant (γ275 Arg→His) characterized by prolonged thrombin and reptilase times and normal fibrinopeptide (FPA, FPB) release. We compared the polymerization rate (by turbidity measurements at 350 nm) and the ultrastructure of Haifa α-, β-, and α, β-fibrin with that of normal. Haifa α, β-fibrin polymerized less rapidly than did normal and formed a highly branched matrix with a smaller mean fiber diameter; this network closely resembled that of normal α, β-fibrin with EDTA added. In the presence of CaCl2 (1 to 10 mM), Haifa α, β-fibrin polymerized more rapidly than in buffer alone and possessed a matrix structure closely resembling that of normal fibrin. From these observations it appears that the functional defect in Haifa fibrin can be related to the inability of the abnormal molecule to effectively utilize available calcium. The polymerization profile of Haifa α-fibrin differed only modestly from that of normal α-fibrin, whereas that of Haifa β-fibrin was markedly impaired. This finding plus similarities in the ultrastructure of Haifa and normal α-fibrin specimens suggests that the defective γ chain structure of Haifa fibrinogen results in greater impairment of the carboxy terminal “b” polymerization domain reacting with the site exposed by cleavage of FPB (“B” site) than it does that of the carboxy terminal “a” domain reacting with the site exposed by cleavage of FPA (“A” site). Whether this effect is due to absolute differences in the degree of impairment of these two types of polymerization sites, or whether proper utilization of the “B” to “b” site is dependent upon participation of the “A” to “a” site remains to be determined.

Keywords

Dysfibrinogen - Fibrinogen - Fibrin polymerization - Electron microscopy
 

  • References

  • 1 Brook JG, Tavori S, Tatarsky I, Hashmonai M, Schramek A. Fibrinogen “Haifa”-a new fibrinogen variant. Haemostasis 1983; 13: 277-281
    PubMedGoogle Scholar
  • 2 Soria J, Soria C, Samama M, Tabori S, Kehl M, Henschen A, Nieuwenhuizen W, Rimon A, Tatarski I. Fibrinogen Haifa: Firbino-gen variant with absence of protective effect of calcium on plasmin degradation of gamma chains. Thromb Haemostas 1987; 57: 310-313
    PubMedGoogle Scholar
  • 3 Kehl M, Henschen A, Tavori S, Rimon A, Soria J, Soria C. The structural error in fibrinogen Haifa, a genetically abnormal fibrinogen with a polymerization defect. Proceedings, VIII International Congress on Thrombosis 1984
    Google Scholar
  • 4 Reber P, Furlan M, Henschen A, Kaudewitz H, Barbui T, Hilgard P, Nenci GG, Berrettini M, Beck EA. Three abnormal fibrinogen variants with the same amino acid substitution (γ275Arg to His): Fibrinogens Bergamo II, Essen and Perugia. Thromb Haemostas 1986; 56: 401-406
    PubMedGoogle Scholar
  • 5 Haverkate F, Timon G. Protective effect of calcium in the plasmin degradation of fibrinogen and fibrin fragment D. Thromb Res 1977; 10: 803-812
    CrossrefPubMedGoogle Scholar
  • 6 Nieuwenhuizen W, Haverkate F. Calcium-binding regions in fibrinogen. Ann NY Acad Sci 1983; 408: 92-96
    CrossrefPubMedGoogle Scholar
  • 7 Kazal LA, Amsel S, Miller OP, Tocantins LM. The preparation and some properties of fibrinogen precipitated from human plasma by glycine. Proc Soc Exp Biol Med 1963; 113: 989-994
    CrossrefPubMedGoogle Scholar
  • 8 Mosesson MW, Sherry S. The preparation and properties of human fibrinogen of relatively high solubility. Biochemistry 1966; 5: 2829-2835
    CrossrefPubMedGoogle Scholar
  • 9 Blombäck B, Blombäck M. Purification of human and bovine fibrinogen. Ark Kemi 1956; 10: 415-443
    PubMedGoogle Scholar
  • 10 Mosesson MW, Finlayson JS. Subfractions of human fibrinogen-preparation and analysis. J Lab Clin Med 1963; 62: 663-674
    PubMedGoogle Scholar
  • 11 Herzig RH, Ratnoff OD, Shainoff JR. Studies on a procoagulant fraction of southern copperhead venom: The preferential release of fibrinopeptide B. J Lab Clin Med 1970; 76: 451-465
    PubMedGoogle Scholar
  • 12 Müller MF, Ris H, Ferry JD. Electron microscopy of fine fibrin clots and coarse fibrin films. J Mol Biol 1984; 174: 369-384
    CrossrefPubMedGoogle Scholar
  • 13 Anderson TF. Techniques for the preservation of three dimensional structure in preparing specimens for the electron microscope. Trans NY Acad Sci 1951; 13: 130-134
    CrossrefPubMedGoogle Scholar
  • 14 Boyer MH, Shainoff JR, Ratnoff OD. Acceleration of fibrin polymerization by calcium ions. Blood 1972; 39: 382-387
    PubMedGoogle Scholar
  • 15 Furlan M, Rupp C, Beck EA, Svendsen L. Effect of calcium and synthetic peptides on fibrin polymerization. Thromb Haemostas 1982; 47: 118-121
    PubMedGoogle Scholar
  • 16 Carr Jr J, Shen LL, Hermans J. Mass-length ratio of fibrin fibres from gel permeation and light scattering. Biopolymers 1977; 16: 01-15
    CrossrefPubMedGoogle Scholar
  • 17 Shah GA, Ferguson IA, Dhall TZ, Dhall DP. Poly dispersion in the diameter of fibres in fibrin networks consequences on the measurement of mass-lenght ratio by permeability and turbidity. Biopolymers 1982; 21: 1037-1047
    CrossrefPubMedGoogle Scholar
  • 18 Carr ME, Hermans J. Size and density of fibrin fibers from turbidity. Macromolecules 1978; 11: 46-50
    CrossrefPubMedGoogle Scholar
  • 19 Rosser RW, Roberts WW, Ferry JD. Rheology of fibrin clots. IV. Darcy constants and fiber thickness. Biophys Chem 1977; 7: 153-157
    CrossrefPubMedGoogle Scholar
  • 20 Wolfe JK, Waugh DF. Relations between enzymatic and association reactions in the development of bovine clot structures. Arch Biochem Biophys 1981; 211: 125-142
    CrossrefPubMedGoogle Scholar
  • 21 Shah GA, Nair CH, Dhall DP. Physiological studies on fibrin network structure. Thromb Res 1985; 40: 181-188
    CrossrefPubMedGoogle Scholar
  • 22 Mosesson MW, Di Orio JP, Muller MF, Shainoff JR, Siebenlist KR, Amrani DL, Homandberg GA, Soria J, Soria C, Samama M. Studies on the ultrastructure of fibrin lacking fibrinopeptide B (p-fibrin). Blood 1987; 69: 1073-1081
    CrossrefPubMedGoogle Scholar
  • 23 Shainoff JR, Dardik BN. Fibrinopeptide B and aggregation of fibrinogen. Science 1979; 204: 200-202
    CrossrefPubMedGoogle Scholar
  • 24 Shainoff JR, Dardik BN. Fibrinopeptide B in fibrin assembly and metabolism: Physiologic significance in delayed release of the peptide. Ann NY Acad Sci 1983; 408: 254-268
    CrossrefPubMedGoogle Scholar
  • 25 Blombäck B, Hessel B, Hogg D, Therkildsen L. A two-step fibrinogen-fibrin transition in blood coagulation. Nature 1978; 275: 501-505
    CrossrefPubMedGoogle Scholar
  • 26 Olexa SA, Budzynski AZ. Evidence for four different polymerization sites involved in human fibrin formation. Proc Natl Acad Sci USA 1980; 77: 1374-1378
    CrossrefPubMedGoogle Scholar
  • 27 Laudano AP, Doolittle RF. Influence of calcium ion on the binding of fibrin amino terminal peptides to fibrinogen. Science 1981; 212: 457-459
    CrossrefPubMedGoogle Scholar
  • 28 Laudano AP, Cottrell BA, Doolittle RF. Synthetic peptides modeled on fibrin polymerization sites. Ann NY Acad Sci 1983; 408: 315-329
    CrossrefPubMedGoogle Scholar