A novel fibrinogen γ chain mutation (γ 239 Gln→His) is the cause of dysfibrinogenemia Vicenza

Spectrum of mutations in Indian patients with fibrinogen disorders and its application in genetic diagnosis of the affected families

“…Patient 9 shows Glu to Ala substitution at amino acid position 239 of FGG which involves the substitution of an polar neutral amino acid Glutamine with a nonpolar strongly hydrophobic Alanine. The mutation in the same position but by his substitution has earlier been reported in a case of dysfibrino-genaemia [9]. The amino acid is located in a nonstructured segment helix C and the 7th b strand of the carboxyl domain of fibrinogen b chain.…”

“…failure, but this normally occurs in childhood [9]. The patient in this case had never previously developed a FVIII inhibitor.…”

“…Both products have an efficacy of approximately 80%. However, haemostasis is never guaranteed during a particular episode with a particular agent and so clinical monitoring of efficacy is essential [9]. This was demonstrated in the current case with the initial failure of rFVIIa and the need to change treatment to an activated prothrombin complex concentrate to achieve haemostasis.…”

“…The patient in this case had never previously developed a FVIII inhibitor. This presentation with spontaneous acute compartment syndrome and life-threatening bleeding due to the development of an inhibitor for the first time in an adult with congenital haemophilia A is very rare with only a few cases documented in the literature [4,9,10].…”

A novel fibrinogen variant – Liberec: dysfibrinogenaemia associated with γ Tyr262Cys substitution

“…Castaman et al. described mutation γ Q239H (fibrinogen Vicenza) causing dysfibrinogenaemia (19). The mutation is 23 residues proximal to the Liberec substitution.…”