Adjacent substitutions (γ352Gly→Cys and 353Thr→Pro) in fibrinogen Ilam cause diminished γ chain expression

• References

• 1 Tennent GA, Brennan SO, Stangou AJ. et al. Human plasma fibrinogen is synthesized only in the liver. Blood 2007; 109: 1971-1974.
• 2 Huang S, Cao A, Chung DW. et al. The Role of βγ and αγ Complexes in the Assembly of Human Fibrinogen. J Biol Chem 1996; 271: 27942-27947.
• 3 Haverkate F, Samama M. Familial dysfibrinogenaemia and thrombophilia: Report on a study of the SSC subcommittee on fibrinogen. Thomb Haemost 1995; 73: 151-161.
• 4 Brennan SO, Fellowes AP, George PM. Molecular Mechanisms of Hypo- and Afibrinogenemia. Ann NY Acad Sci 2001; 936: 91-100.
• 5 Hanss M, Biot F. A Database For Human Fibrinogen Variants. Ann NY Acad Sci 2001; 936: 89-90. Available at: http://www.geht.org/databaseang/fibrinogen/
• 6 Fellowes AP, Brennan SO, Ridgway HJ. et al. PM. Electrospray ionisation mass spectrometry identification of fibrinogen Banks peninsula (γ280 Tyr→Cys): a new variant with defective polymerisation. Br J Haematol 1998; 101: 24-31.
• 7 Yee VC, Pratt KP, Cote HCF. et al. Crystal structure of a 30 kDa C-terminal fragment from the γ chain of human fibrinogen. Structure 1997; 5: 125-138.
• 8 Meyer M, Dietzel H, Kaetzel R. et al. Fibrinogen Leipzig II (γ351Gly→Ser and γ82Ala→Gly); Hypodysfibrinogenemia due to two independent substitutions within the same polypeptide chain. Thromb Haemost 2007; 89: 903-905.
• 9 Brennan SO, Davis RL. Substitution (γ335Trp→Arg) in fibrinogen Fremantle causes diminished γ chain expression and increased sialic acid content. Thromb Haemost 2010; 104: 1274-1276.
• 10 Dib N, Quelin F, Ternisien C. et al. Fibrinogen Angers with a new deletion (γ GVYYQ 346–350) causes hypofibrinogenemia with hepatic storage. J Thromb Haemost 2007; 5: 1999-2005.
• 11 Kruse KB, Dear A, Kaltenbrun ER. et al. Mutant fibrinogen cleared from the ER via ERAD and auto-phagy: an explanation for liver disease. Am J Pathol 2006; 168: 1299-1308.