Thromb Haemost 2013; 109(06): 1180-1182
DOI: 10.1160/TH13-01-0068
Letters to the Editor
Schattauer GmbH

Hypodysfibrinogenaemia and thrombosis in association with a new fibrinogen γ chain with two mutations (γ114Tyr→His, and γ320Asp deleted)

Stephen O. Brennan
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: 27 January 2013

Accepted after minor revision: 20 February 2013

Publication Date:
22 November 2017 (online)

 

 
  • References

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  • 2 Mosesson MW, Siebenlist KR, Meh DA. The structure and biological features of fibrinogen and fibrin. Ann NY Acad Sci 2001; 936: 11-30.
  • 3 Brennan SO, Davis RL, Mosesson MW. et al. Congenital hypodysfibrinogenaemia (Fibrinogen Des Moines) due to a (320Asp deletion at the Ca2+ binding site”. Thromb Haemost 2007; 98: 467-469.
  • 4 Morris TA, Marsh JJ, Chiles PG. et al. High prevalence of dysfibrinogenemia among patients with chronic thromboembolic pulmonary hypertension. Blood 2009; 114: 1929-1936.
  • 5 Tennent GA, Brennan SO, Stangou AJ. et al. Human plasma fibrinogen is synthesized in the liver. Blood 2007; 109: 1971-1974.
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  • 7 Yakovlev S, Makogonenko E, Kurochkina N. et al. Conversion of fibrinogen to fibrin: mechanism of exposure of tPA- and plasminogen-binding sites. Biochemistry 2000; 39: 15730-15741.
  • 8 Brennan SO, Fellowes AP, Faed JM. et al. Hypofibrinogenemia in an individual with two coding (γ82 Ala→Gly and Bβ235 Pro→Leu) and two noncoding mutations. Blood 2000; 95: 1709-1713.