LETTERS TO THE EDITOR: Four cases of hypofibrinogenemia associated with four novel mutations

Hanss, Michel; Ffrench, Patrick; Vinciguerra, Christine; Bertrand, Mathieu; Mazancourt, Philippe de

doi:10.1111/j.1538-7836.2005.01580.x

Cited by 25 publications

(23 citation statements)

References 11 publications

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“…Three others are situated in FGB exon 8. One (p.Trp432X) was identified in heterozygosity in a French patient with hypofibrinogenemia [Hanss et al, 2005] and although not experimentally proven to be the causative mutation, it is very likely that this mutation is indeed responsible for the fibrinogen deficiency. Two other FGB nonsense mutations, p.Trp467X and p.Trp470X, are localized even closer to the C-terminus and are expected to cause the synthesis of b-chains truncated of only 25 and 22 residues respectively.…”

Section: Nonsense Mutationsmentioning

confidence: 99%

Mutations in the fibrinogen gene cluster accounting for congenital afibrinogenemia: an update and report of 10 novel mutations

Neerman-Arbez

Moerloose

2007

Hum. Mutat.

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Communicated by Arupa GangulyFibrinogen is synthesized in hepatocytes in the form of a hexamer composed of two sets of three polypeptides (Aa, Bb, and c). Each polypeptide is encoded by a distinct gene, FGA, FGB, and FGG, all three clustered in a region of 50 kb on 4q31. Congenital afibrinogenemia is characterized by the complete absence of fibrinogen, the precursor of the major protein constituent of the blood clot, fibrin. Although the disease was first described in 1920, the genetic defect responsible for this disorder long remained unknown. We identified the gene and the first causative mutations for this disease in a nonconsanguineous Swiss family in 1999. Since this first report, 61 additional mutations, the majority in FGA, have been identified in patients with afibrinogenemia (in homozygosity or in compound heterozygosity) or in heterozygosity in hypofibrinogenemia, since many of these patients are in fact asymptomatic carriers of afibrinogenemia mutations. Mutations in the fibrinogen genes may lead to deficiency of fibrinogen by several mechanisms: these can act at the DNA level, at the RNA level by affecting mRNA splicing or stability, or at the protein level by affecting protein synthesis, assembly, or secretion. The expression of selected mutations has shown that mechanisms acting at all three levels play a role in the molecular basis of this disease. We report here the identification of 10 novel mutations, of which eight are localized in FGA, thus increasing the total number of causative mutations identified to 72 and confirming the relative importance of FGA in the molecular basis of fibrinogen deficiency. Hum Mutat 28(6), [540][541][542][543][544][545][546][547][548][549][550][551][552][553] 2007. r r 2007 Wiley-Liss, Inc.

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Section: Nonsense Mutationsmentioning

confidence: 99%

Mutations in the fibrinogen gene cluster accounting for congenital afibrinogenemia: an update and report of 10 novel mutations

Neerman-Arbez

Moerloose

2007

Hum. Mutat.

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“…Concerning the other novel mutation identified in this study, FGGp.Asn230Lys, it involves a residue that resulted substituted by an histidine or by an aspartic acid in fibrinogen Lyon IV and Middlemore, respectively [18,19]. In our case, the substitution results in the addition of a positive charge in the central region of the γD sub-domain, which takes part in the formation of the fibrinogen C-terminal globular D domain [30], and it consequently might affect packing of the γD domain itself.…”

Section: Discussionmentioning

confidence: 91%

Molecular characterization of 7 patients affected by dys- or hypo-dysfibrinogenemia: Identification of a novel mutation in the fibrinogen Bbeta chain causing a gain of glycosylation

Asselta

Robusto

Platé

et al. 2015

Thrombosis Research

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“…This suggests that the Aa chain synthesis is not rate limiting and that one normal FGA allele is sufficient for achieving normal synthesis. Very few exceptions are described (Fibrinogen Grand-Lyon [15]), and most of the Aa chain gene mutations require homozygosity or compound heterozygosity to induce a significant decrease in fibrinogen level. The data reported here favor the concept that there is an excess of Aa chains over Bb and g chains, since neither of the parents can be regarded as hypofibrinogenemic.…”

Section: Discussionmentioning

confidence: 96%

A case of afibrinogenemia associated with A-alpha chain gene compound heterozygosity (HUMFIBRA c.[4110delA]+[3200+1G>T])

Anglès-Cano

Mathonnet

Dreyfus

et al. 2007

Blood Coagulation &Amp; Fibrinolysis

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The clinical features and molecular biology data of a case of afibrinogenemia are reported. The propositus is a 14-year-old girl who suffered several bleeding manifestations that were successfully treated with fibrinogen infusion. The afibrinogenemia results from compound heterozygosity for two mutations on the Aalpha chain gene (c.[4110delA]+[3200+1G>T]). The first mutation is a novel frameshift mutation inherited from her father. The second is a previously described Aalpha chain gene splice junction mutation inherited from her mother. Neither of the parents fulfills the criteria for hypofibrinogenemia.

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LETTERS TO THE EDITOR: Four cases of hypofibrinogenemia associated with four novel mutations

Cited by 25 publications

References 11 publications

Mutations in the fibrinogen gene cluster accounting for congenital afibrinogenemia: an update and report of 10 novel mutations

Mutations in the fibrinogen gene cluster accounting for congenital afibrinogenemia: an update and report of 10 novel mutations

Molecular characterization of 7 patients affected by dys- or hypo-dysfibrinogenemia: Identification of a novel mutation in the fibrinogen Bbeta chain causing a gain of glycosylation

A case of afibrinogenemia associated with A-alpha chain gene compound heterozygosity (HUMFIBRA c.[4110delA]+[3200+1G>T])

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