Thromb Haemost 2017; 117(10): 2000-2002
DOI: 10.1160/TH17-04-0270
Letter to the Editor
Schattauer GmbH

Hypofibrinogenaemia associated with novel Aα126Val→Asp mutation in the fibrinogen coiled coil

Stephen O. Brennan
1   Pathology Department, University of Otago, Christchurch, New Zealand
2   Canterbury Health Laboratories, Christchurch, New Zealand
,
Andrew D. Laurie
2   Canterbury Health Laboratories, Christchurch, New Zealand
› Institutsangaben
Weitere Informationen

Publikationsverlauf

Received: 20. April 2017

Accepted after minor revision: 21. Juni 2017

Publikationsdatum:
28. November 2017 (online)

 

 
  • References

  • 1 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.
  • 2 Huang S, Cao Z, Chung DW. et al. The role of ßγ and βγ complexes in the assembly of human fibrinogen. J Biol Chem 1996; 271: 27942-27947.
  • 3 Brennan SO. Variation of fibrinogen oligosaccharide structure in the acute phase response; possible haemorrhagic implications. Biochim Biophy Acta Clinical 2015; 03: 221-226.
  • 4 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.
  • 5 Dear A, Brennan SO. Sheat et al. Acquired dysfibrinogenemia caused by monoclonal production of immunoglobulin λ light chain. Haematologica 2007; 92: e111-e117.
  • 6 Hanss M, Biot F. A database for human fibrinogen variants. Ann NY Acad Sci 2001; 936: 89-90.
  • 7 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.
  • 8 Huang S, Mulvihill ER, Farrell DH. et al. Biosynthesis of human fibrinogen. Subunit interactions and potential intermediates in the assembly. J Biol Chem 1993; 268: 8919-8926.
  • 9 Lefebvre P, Velasco PT, Dear A. et al. Coagulopathy in compound heterozygotes with the fibrinogen Aaivs-4 mutation and AaGln328 truncation (fibrinogen Keokuk). Blood 2004; 103: 2571-2576.
  • 10 Asselta R, Duga S, Tenchini ML. The molecular basis of quantitative fibrinogen disorders. J Thromb Haemost 2006; 04: 2115-2129.
  • 11 Fellowes AP, Brennan SO, Stromorken H. et al. Homozygous truncation of the fibrinogen Aa chain within the coiled coil causes congenital afibrinogenaemia. Blood 2000; 96: 773-775.
  • 12 Doolittle RF, Goldbaum DM, Doolittle LR. Designation of sequences involved in the “coiled-coil” interdomainal connections in fibrinogen: constructions of an atomic scale model. J Mol Biol 1978; 120: 311-325.
  • 13 Conway JF, Parry DA. Three-stranded alpha-fibrous proteins: the heptad repeat and its implications for structure. Int J Biol Macromol 1991; 13: 14-16.
  • 14 Platé M, Asselta R, Peyvandi F. et al. Molecular characterization of the first missense mutation in the fibrinogen Aalpha-chain gene identified in a compound heterozygous afibrinogenemic patient. Biochim Biophys Acta 2007; 1772: 781-787.