A new heterozygous mutation in gamma fibrinogen gene leading to 326 Cys-->Ser substitution in fibrinogen Cordoba is associated with defective polymerization and familial hypodysfibrinogenemia.

GUGLIELMONE, HUGO; SANCHEZ, M. CECILIA; ABATE DAGA, DANIEL; BOCCO, JOSE LUIS

JOURNAL OF THROMBOSIS AND HAEMOSTASIS

Blackwell Pub

Lugar: Londres; Año: 2004 vol. 2 p. 352 - 352

1538-7933

ince the first dysfibrinogenemia case was described in 1964, more than 300 abnormal fibrinogens have been reported. However the identification of the underlying structural defect in the molecule has been elucidated only in a few cases as registered in a database for this pathology (www.geht.org/databaseang/fibrinogen/). The majority of the patients suffering from dysfibrinogenemia are asymptomatic therefore most of them were detected accidentally in routine coagulation screening where they presented prolonged clotting times. It has been reported that approximately two-thirds of the abnormal fibrinogen variants have the anomaly at or near the thrombin cleavage site on the amino terminal A± or B gamma chains, whereas one-quarter has the molecular defect in the carboxy terminal region of the gamma-chain, encompassing the complementary polymerization site(s). In this study, we identified a novel missense mutation in an Argentinean family showing altered biochemical parameters compatibl