Download PDF
Thromb Haemost 2010; 103(02): 478-479
DOI: 10.1160/TH09-07-0459
Letters to the Editor
Schattauer GmbH

New fibrinogen substitution (γSer313Arg) causes diminished γ chain expression and hypodysfibrinogenaemia

Stephen O. Brennan
1   Molecular Pathology Laboratory, Pathology Department, University of Otago, Christchurch, New Zealand
,
Ryan L. Davis
1   Molecular Pathology Laboratory, Pathology Department, University of Otago, Christchurch, New Zealand
,
Meera Chitlur
2   Department of Paediatric Hematology, Children’s Hospital of Michigan, Detroit, Michigan, USA
› Author Affiliations
Further Information

Publication History

Received: 16 July 2009

Accepted after major revision: 10 October 2009

Publication Date:
22 November 2017 (online)

Also available at
    Permissions and Reprints

 

 

  • References

  • 1 Mosesson MW, Siebenlist KR, Meh DA. The structure and biological features of fibrinogen and fibrin. Ann NY Acad Sci 2001; 936: 11-30.
    PubMedGoogle Scholar
  • 2 Everse SJ, Spraggon G, Doolittle RF. A three-dimensional consideration of variant human fibrinogens. Thromb Haemost 1998; 80: 1-9.
    Article in Thieme ConnectPubMedGoogle Scholar
  • 3 Maghzal GJ, Brennan SO, Homer VM. et al. The molecular mechanisms of congenital hypofibrinogenaemia. Cell Mol Life Sci 2004; 61: 1427-1438.
    PubMedGoogle Scholar
  • 4 Hanss M, Biot F. A Database for human fibrinogen variants. Ann NY Acad Sci 2001; 936: 89-90. Available at: http://www.geht.org/databaseang/fibrinogen.
    PubMedGoogle Scholar
  • 5 Brennan SO, Hammonds B, George PM. Aberrant hepatic processing causes removal of activation peptide and primary polymerization site from fibrinogen Canterbury (Aα20Val→Asp). J Clin Invest 1995; 96: 2854-2858.
    CrossrefPubMedGoogle Scholar
  • 6 Wenker OC, Wojciechowski Z, Sheinbaum R. et al. Thrombelastography. The Internet Journal of Anesthesiology. 1997 Volume 1 Number 3. Available at: http://www.ispub.com/ostia/index.php?xmlFile Path=journals/ija/vol1n3/teg.xml
    PubMedGoogle Scholar
  • 7 Brennan SO. Electrospray ionization analysis of human fibrinogen. Thromb Haemost 1997; 78: 1055-1058.
    Article in Thieme ConnectPubMedGoogle Scholar
  • 8 Meyer M, Bergmann F, Brennan SO. Novel fibrinogen mutation (γ313 Ser→Asn) associated with hypofibrinogenemia in two unrelated families. Blood Coagul Fibrinolysis 2006; 17: 63-67.
    CrossrefPubMedGoogle Scholar
  • 9 Kruse KB, Dear A, Kaltenbrun ER. et al. Mutant fibrinogen cleared from the endoplasmic reticulum via endoplasmic reticulum-associated protein degradation and autophagy: an explanation for liver disease. Am J Pathol 2006; 168: 1299-1308.
    CrossrefPubMedGoogle Scholar
  • 10 Brennan SO, Wyatt J, Medicina D. et al. Fibrinogen Brescia: hepatic endoplasmic reticulum storage and hypofibrinogenaemia because of a γ284 Gly→Arg mutation. Am J Pathol 2000; 157: 189-196.
    CrossrefPubMedGoogle Scholar
  • 11 Brennan SO, Maghzal G, Shneider BL. et al. Novel fibrinogen γ375 Arg→Trp mutation (fibrinogen Aguadilla) causes hepatic endoplasmic reticulum storage and hypofibrinogenemia. Hepatology 2002; 36: 652-658.
    CrossrefPubMedGoogle Scholar
  • 12 Dib N, Quelin F, Ternisien C. et al. Fibrinogen Angers with a new deletion (γ GVYYQ 346–350) causes hypofibrinogenemia with hepatic storage. J Thromb Haemost 2007; 5: 1999-2005.
    CrossrefPubMedGoogle Scholar