Fibrinogen Leipzig II (γ351Gly→Ser and γ82Ala→Gly): Hypodysfibrinogenaemia due to two independent amino acid substitutions within the same polypeptide chain

• References

• 1 Maghzal GJ, Brennan SO, Homer VM. et al. The molecular mechanisms of congenital hypofibrinogenaemia.. Cell Mol Life Sci 2004; 61: 1427-1438.
• 2 Asselta R, Duga S, Tenchini ML. The molecular basis of quantitative fibrinogen disorders.. J Thromb Haemost 2006; 4: 2115-2129.
• 3 Database of fibrinogen variants. Available at: http://www.geht.org.
• 4 Brennan SO, Fellowes AP, Faed JM. et al. Hypofibrinogenemia in an individual with two coding (γ82 A→G and BβP→L) and two noncoding mutations.. Blood 2000; 95: 1709-1713.
• 5 Ivaskievicius V, Jusciute E, Steffens M. et al. γAla82Gly represents a common fibrinogen γ-chain variant in Caucasians.. Blood Coagul Fibrinol 2005; 16: 205-208.
• 6 Wyatt J, Brennan SO, May S. et al. Hypofibrinogenaemia with compound heterozygosity for two γ chain mutations – γ82 Ala→Gly and an intron two GT→AT splice site mutation.. Thromb Haemost 2000; 84: 449-452.
• 7 Meyer M, Franke K, Richter W. et al. New molecular defects in the γ subdomain of fibrinogen D-domain in four cases of (hypo)dysfibrinogenemia: fibrinogen variants Hannover VI, Homburg VII, Stuttgart and Suhl.. Thromb Haemost 2003; 89: 637-646.
• 8 Hanss M, Ffrench P, Vinciguerra C. et al. Four cases of hypofibrinogenemia associated with four novel mutations.. J Thromb Haemost 2005; 3: 2347-2349.
• 9 Steinmann C, Boegli C, Jungo M. et al. A new substitution, γ358 Ser→Cys, in fibrinogen Milano VII causes defective fibrin polymerisation.. Blood 1994; 84: 1874-1880.
• 10 Mathonnet F, Guillon L, Detruit H. et al. Fibrinogen Poissy II (gammaN361K): a novel dysfibrinogenemia associated with defective polymerisation and peptide B release.. Blood Coagul Fibrinol 2003; 14: 293-298.