Fibrinogen geneva II: a new congenitally abnormal fibrinogen alpha chain (Gly17Asp) with a review of similar mutations resulting in abnormal knob A

Blood Coagul Fibrinolysis. 2014 Apr;25(3):280-2. doi: 10.1097/MBC.0000000000000039.

Abstract

Congenital dysfibrinogenemias are characterized by biosynthesis of a structurally abnormal fibrinogen molecule that exhibits reduced functional levels compared with the level of fibrinogen antigen. To date a large number of mutations have been identified in patients with dysfibrinogenemia. Mutations occurring at the thrombin cleavage site (Arg16-Gly17 in the mature alpha-chain) at the amino-terminal end of the fibrinogen alpha chain are a common cause of the disease. These mutations causing abnormal fibrin polymerization are associated with different phenotypes. Here, we report the identification of a novel heterozygous missense mutation of Glycine 17 (Gly17Asp) in a female patient with mild bleeding manifestations, and compare it with other previously reported mutations also resulting in abnormal knob A.

Publication types

  • Case Reports

MeSH terms

  • Afibrinogenemia / genetics*
  • Female
  • Fibrinogens, Abnormal / genetics*
  • Fibrinogens, Abnormal / metabolism
  • Humans
  • Middle Aged
  • Mutation, Missense*

Substances

  • Fibrinogens, Abnormal
  • fibrinogen Geneva

Supplementary concepts

  • Dysfibrinogenemia, Congenital