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

• References

• 1 Doolittle RF. The molecular biology of fibrin. The Molecular Basis of Blood Diseases. Saunders, Philadelphia: 1994: 701-723.
• 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.
• 6 Yonekawa O, Voskuilen M, Nieuwenhuizen W. Localization in the fibrinogen gamma-chain of a new site that is involved in the acceleration of the tissue type plasminogen activator-catalysed activation of plasminogen. Biochem J 1992; 283: 187-191.
• 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.