Thromb Haemost 2015; 113(04): 903-905
DOI: 10.1160/TH14-10-0849
Letter to the Editor
Schattauer GmbH

Novel FGG variant (ү339C→S) confirms importance of the ү326–339 disulphide bond for plasma expression of newly synthesised fibrinogen

Stephen O. Brennan
1   Pathology Department, University of Otago, Christchurch, New Zealand
2   Canterbury Health Laboratories, Christchurch, New Zealand
,
Andrew Laurie
2   Canterbury Health Laboratories, Christchurch, New Zealand
,
Mark Smith
2   Canterbury Health Laboratories, Christchurch, New Zealand
› Author Affiliations
Further Information

Publication History

Received: 12 October 2014

Accepted after major revision: 19 January 2014

Publication Date:
24 November 2017 (online)

 

 
  • References

  • 1 Huang S, Cao Z, Chung DW. et al. The role of βγ and αγ complexes in the assembly of human fibrinogen. J Biol Chem 1996; 271: 27942-27947.
  • 2 Spraggon G, Everse SJ, Doolittle RF. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature 1997; 389: 455-462.
  • 3 Zhang J-Z, Redman C. Fibrinogen assembly and secretion; role of intrachain disulphide loops. J Biol Chem 1996; 271: 30083-30088.
  • 4 Townsend RR, Hilliker E, Li Y-T. et al. Carbohydrate structure of human fibrinogen. J Biol Chem 1982; 257: 9704-9710.
  • 5 Martinez J, MacDonald KA, Palascak JE. The role of sialic acid in the dysfibrinogenemia associated with liver disease: distribution of sialic acid on the constituent chains. Blood 1983; 61: 1196-1202.
  • 6 Brennan SO, Oliver J, Davis RL. Epigenetic, polymorphic and mutational (Aα167Arg→Lys) contribution to a functionally abnormal fibrinogen. J Thromb Haemost 2011; 09: 1414-2.
  • 7 Brennan SO, Hammonds B, George PM. Aberrant hepatic processing causes removal of activation peptide and primary polymerisation site from fibrinogen Canterbury (A20 ValAsp). J Clin Invest 1995; 96: 2854-2858.
  • 8 Brennan SO, Wyatt J, Medicina D. et al. Fibrinogen Brescia; Hepatic Endoplasmic Reticulum Storage and Hypofibrinogenaemia because of a γ284 Gly→Arg mutation. Am J Pathol 2000; 157: 189-196.
  • 9 Brennan SO, Mangos H, Faed J. Benign FGB (148Lys→Asn, and 448Arg→Lys), and novel causative γ211Tyr→His mutation distinguished by time of flight mass spectrometry in a family with hypofibrinogenaemia. Thromb Haemost 2014; 111: 679-684.
  • 10 Brennan SO, Homer VM, Davis RL. et al. Hypofibrinogenaemia associated with common γ82Ala→Gly mutation is not mediated by altered mRNA splicing. Thromb Haemost 2006; 96: 535-537.
  • 11 Cheah CY, Brennan SO, Kennedy H. et.al. Fibrinogen Melbourne: a novel congenital hypodysfibrinogenemia caused by γ326Cys to Phe in the fibrinogen γ chain, presenting as massive splanchnic venous thrombosis. Blood Coagul Fibrinol 2012; 23: 563-565.
  • 12 Brennan SO, Loreth RM, George PM. Oligosaccharide Configuration of Fibrinogen Kaiserslautern: Electrospray Ionisation Analysis of Intact γ Chains. Thromb Haemost 1998; 80: 253-265.
  • 13 Brennan SO, Davis RL, Conard K. et al. Novel fibrinogen mutation γ14ThrPro (fibrinogen AI du-Pont) associated with hepatic fibrinogen storage disease and hypofibrinogenaemia. Liver Int 2010; 30: 1541-1547.
  • 14 Haneish Ai, Terasawa F, Fujihara N. et al. Recombinant variant fibrinogens substituted at residues γ326Cys and γ339Cys demonstrated markedly impaired secretion of assembled fibrinogen. Thromb Res 2009; 124: 368-372.