New fibrinogen substitution (γSer313Arg) causes diminished γ chain expression and hypodysfibrinogenaemia

Thrombosis and Haemostasis

Volumn 103, Issue 2, 2010, Pages 478-479

  Brennan, Stephen O ^a   Davis, Ryan L ^a   Chitlur, Meera ^b  

^a UNIVERSITY OF OTAGO   (New Zealand)

^b CHILDREN'S HOSPITAL OF MICHIGAN   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; FIBRINOGEN; POLYACRYLAMIDE GEL; SERINE; VON WILLEBRAND FACTOR;

ALPHA CHAIN; AMINO ACID SUBSTITUTION; BETA CHAIN; BLEEDING DISORDER; DYSFIBRINOGENEMIA; EPISTAXIS; FIBRINOGEN BLOOD LEVEL; GAMMA CHAIN; HUMAN; HYPOFIBRINOGENEMIA; LETTER; MUTATION; PHENOTYPE; PRIORITY JOURNAL; PROTEIN STRUCTURE; THROMBIN TIME;

AFIBRINOGENEMIA; CHILD, PRESCHOOL; FAMILY HEALTH; FEMALE; FIBRINOGEN; HUMANS; MUTATION, MISSENSE;

EID: 75749093431     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1160/TH09-07-0459     Document Type: Letter

References (12)

1. Mosesson MW, Siebenlist KR, Meh DA. The structure and biological features of fibrinogen and fibrin. Ann NY Acad Sci 2001; 936: 11-30.
2. Everse SJ, Spraggon G, Doolittle RF. A three-dimensional consideration of variant human fibrinogens. Thromb Haemost 1998; 80: 1-9.
3. Maghzal GJ, Brennan SO, Homer VM, et al. The molecular mechanisms of congenital hypofibrinogenaemia. Cell Mol Life Sci 2004; 61: 1427-1438.
4. 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/fibri nogen.
5. Brennan, SO, Hammonds, B, George PM. Aberrant hepatic processing causes removal of activation peptide and primary polymerization site from fibrinogen Canterbury (Aα20Val→Asp). J Clin Invest 1995; 96: 2854-2858.
6. Wenker OC, Wojciechowski Z, Sheinbaum R, et al. Thrombelastography. The Internet Journal of Anesthesiology. 1997 Volume 1 Number 3. Available at: http://www.ispub.com/ostia/index.php?xmlFile Path=journals/ija/vol1n3/teg.xml
7. Brennan SO. Electrospray ionization analysis of human fibrinogen. Thromb Haemost 1997; 78: 1055-1058.
8. Meyer M, Bergmann F, Brennan SO. Novel fibrinogen mutation (γ313 Ser→Asn) associated with hypofibrinogenemia in two unrelated families. Blood Coagul Fibrinolysis 2006; 17: 63-67.
9. Kruse KB, Dear A, Kaltenbrun ER, et al. Mutant fibrinogen cleared from the endoplasmic reticulum via endoplasmic reticulum-associated protein degradation and autophagy: an explanation for liver disease. Am J Pathol 2006; 168: 1299-1308.
10. 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.
11. Brennan SO, Maghzal G, Shneider BL, et al. Novel fibrinogen γ375 Arg→Trp mutation (fibrinogen Aguadilla) causes hepatic endoplasmic reticulum storage and hypofibrinogenemia. Hepatology 2002; 36: 652-658.
12. 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.