Thromb Haemost 2002; 88(03): 533-534
DOI: 10.1055/s-0037-1613248
Letters to the Editor
Schattauer GmbH

Low Expression of Truncated Aα Chain Variant in Circulating Fibrinogen

Stephen O. Brennan
1   Molecular Pathology Laboratory, Canterbury Health Laboratories, Christchurch, New Zealand
,
Vivienne M. Homer
1   Molecular Pathology Laboratory, Canterbury Health Laboratories, Christchurch, New Zealand
,
Paul Ockelford
2   Haematology Department, Auckland Hospital, Auckland, New Zealand
,
Peter M. George
1   Molecular Pathology Laboratory, Canterbury Health Laboratories, Christchurch, New Zealand
› Author Affiliations
Further Information

Publication History

Received 11 February 2002

Accepted after revision 29 May 2002

Publication Date:
27 December 2017 (online)

 

 
  • References

  • 1 Ridgway H, Brennan SO, Gibbons S, George PM. Fibrinogen Lincoln: A new mutation causing α chain truncation and defective polymerisation. Br J Haematol 1996; 93: 117-84.
  • 2 Brennan SO, Hammonds B, George PM. Aberrant hepatic processing causes removal of activation peptide and primary polymerisation site from fibrinogen Canterbury (Aα20 Val→Asp). J Clin Invest 1995; 96: 2854-8.
  • 3 Mullin J, Gorkun O, Lord S. Decreased lateral aggregation of a variant recombinant fibrinogen provides insights into the polymerisation mechanism. Biochemistry 2000; 9843-9.
  • 4 Brennan SO. Electrospray ionisation analysis of human fibrinogen. Thromb Haemost 1997; 78: 1055-8.
  • 5 Fellowes AP, Brennan SO, Stromorken H, Holme R, Brosstad F, George PM. Homozygous truncation of the fibrinogen Aα chain within the coiled coil causes congenital afibrinogenaemia. Blood 2000; 96: 773-5.
  • 6 Gorkun OV, Veklich YI, Medved LV, Henchen AH, Weiel JW. Role of the αC domains of fibrin in clot formation. Biochemistry 1994; 33: 6986-97.