Thromb Haemost 2007; 98(02): 467-469
DOI: 10.1160/TH07-01-0012
Case Report
Schattauer GmbH

Congenital hypodysfibrinogenaemia (Fibrinogen Des Moines) due to a γ320Asp deletion at the Ca2+ binding site

Stephen O. Brennan
1   Molecular Pathology Laboratory, Christchurch School of Medicine, Christchurch, New Zealand
,
Ryan L. Davis
1   Molecular Pathology Laboratory, Christchurch School of Medicine, Christchurch, New Zealand
,
Michael W. Mosesson
2   Blood Research Institute, Blood Center of Wisconsin, Milwaukee, Wisconsin, USA
,
Irene Hernandez
2   Blood Research Institute, Blood Center of Wisconsin, Milwaukee, Wisconsin, USA
,
Robin Lowen
1   Molecular Pathology Laboratory, Christchurch School of Medicine, Christchurch, New Zealand
,
Saramma J. Alexander
3   Medical Oncology and Hematology Associates, Des Moines, Iowa, USA
› Author Affiliations
Further Information

Publication History

Received 07 January 2007

Accepted after resubmission 08 April 2007

Publication Date:
28 November 2017 (online)

 

 
  • References

  • 1 Henschen AH, McDonagh J. Fibrinogen, fibrin and factor XIII. In: Blood Coagulation. Vol 13. Zwaal RFA, Hemker HC. eds. Amsterdam: Elsevier Science Publishers BV; 1986: 171-241.
  • 2 Doolittle RF. The molecular biology of fibrin. In: The Molecular Basis of Blood Diseases. Philadelphia: WB Saunders Co.; 1994: 701-726.
  • 3 Spraggon G, Everse SJ, Doolittle RF. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature 1997; 389: 455-462.
  • 4 Yee VC, Pratt KP, Cote HCF. et al. Crystal structure of a 30 kDa C-terminal fragment from the γ chain of human fibrinogen. Structure 1997; 5: 125-138.
  • 5 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: 14156-14161.
  • 6 Mosesson MW, Siebenlist KR, Hainfeld JF. et al. The covalent structure of factor XIIIa crosslinked fibrinogen fibrils. J Struct Biol 1995; 115: 88-101.
  • 7 Huang S, Mulvihill ER, Farrell DH. et al. Biosynthesis of human fibrinogen. Subunit interactions and potential intermediates in assembly. J Biol Chem 1993; 268: 8919-8926.
  • 8 Huang S, Cao Z, Chung DW. et al. The role of αγ and βγ complexes in the assembly of human fibrinogen. J Biol Chem 1996; 271: 27942-27947.
  • 9 Maghzal GJ, Brennan SO, Homer VM. et al. The molecular mechanisms of congenital hypofibrinogenaemia. Cell Mol Life Sci 2004; 61: 1427-1438.
  • 10 Hanss M, Biot FA. A database for human fibrinogen variants. Ann NY Acad Sci 2001; 86: 154-163 Available online at http://www.geht.org/databaseang/fibrinogen .
  • 11 Brennan SO, Hammonds B, George PM. Aberrant hepatic processing causes removal of activation peptide and primary polymerisation site from fibrinogen Canterbury(Aγ20Val→Asp). J Clin Invest 1995; 96: 2854-2858.
  • 12 Brennan SO. Electrospray ionisation analysis of human fibrinogen. Thromb Haemost 1997; 78: 1055-1058.
  • 13 Brennan SO, Wyatt J, Medicina D. et al. Fibrinogen Brescia; hepatic endoplasmic reticulum storage and hypofibrinogenaemia because of a γ284 Gly→Argmutation. Am J Pathol 2000; 157: 189-196.
  • 14 Fellowes AP, Brennan SO, Ridgway HJ. et al. Electrospray ionization mass spectrometry identification of fibrinogen Banks Peninsula (γ280Tyr→Cys) -a new variant with defective polymerization. Br J of Haematol 1998; 101: 24-31.
  • 15 Mullin JL, Brennan SO, Ganly PS. et al. Fibrinogen Hillsborough: a novel γ309Gly→Asp dysfibrinogen with impaired clotting. Blood 2002; 99: 3597-3610.
  • 16 Koopman J, Haverkate F, Briet E. et al. Congenitally abnormal fibrinogen (Vlissingen) with a 6-base pair deletion in the γ gene, causing defective calcium binding and impaired fibrin polymerization. J Biol Chem 1991; 266: 13456-13461.
  • 17 Terasawa F, Hogan KA, Kani S. et al. Fibrinogen Otsu I; a γAsn319, γAsp 320 deletion dysfibrinogen identified in a pregnant woman. Thromb Haemost 2003; 90: 757-758.
  • 18 Kelley KA, Gourkun OV, Lounes KC. et al. Recombinant fibrinogen Vlissingen/Frankfurt IV the deletion of residues 319 and 320 from the? chain alters calcium binding, fibrin polymerization, cross-linking and platelet aggregation. J Biol Chem 2000; 275: 17778-17785.
  • 19 Kani S, Terasawa F, Lord ST. et al. In vitro expression demonstrates impaired secretion of the γAsn319, Asp320 deletion variant fibrinogen. Thromb Haemost 2005; 94: 53-59.
  • 20 Haverkate F, Samama M. Familial dysfibrinogenaemia and thrombophilia: Report on a study of the SSC subcommittee on fibrinogen. Thromb Haemost 1995; 73: 151-161.