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Thromb Haemost 2007; 98(05): 1136-1138
DOI: 10.1160/TH07-05-0354
Case Report
Schattauer GmbH

Fibrinogen Tolaga Bay: A novel γAla341Val mutation causing hypofibrinogenaemia

Ryan L. Davis
1   Christchurch School of Medicine and Health Sciences, University of Otago, Christchurch, New Zealand
,
Stephen O. Brennan
1   Christchurch School of Medicine and Health Sciences, University of Otago, Christchurch, New Zealand
2   Canterbury Health Laboratories, Christchurch, New Zealand
› Institutsangaben
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Publikationsverlauf

Received 15. Mai 2007

Accepted after revision 28. Juni 2007

Publikationsdatum:
30. November 2017 (online)

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  • References

  • 1 Mosesson MW, Siebenlist KR, Meh DA. The structure and biological features of fibrinogen and fibrin. Ann NY Acad Sci 2001; 936: 11-30.
    PubMedGoogle Scholar
  • 2 McKee PA, Rogers LA, Marler E. et al. The subunit polypeptides of human fibrinogen. Arch Biochem Biophys 1966; 116: 271-279.
    CrossrefPubMedGoogle Scholar
  • 3 Kant JA, Fornace Jr. AJ, Saxe D. et al. Evolution and organization of the fibrinogen locus on chromosome 4: gene duplication accompanied by transposition and inversion. Proc Natl Acad Sci USA 1985; 82: 2344-2348.
    CrossrefPubMedGoogle Scholar
  • 4 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.
    PubMedGoogle Scholar
  • 5 Brennan SO. Electrospray ionisation analysis of human fibrinogen. Thromb Haemost 1997; 78: 1055-1058.
    Artikel in Thieme ConnectPubMedGoogle Scholar
  • 6 Brennan SO, Fellowes AP, Faed JM. et al. Hypofibrinogenemia in an individual with 2 coding (gamma82 A-->G and Bbeta235 P-->L) and 2 noncoding mutations. Blood 2000; 95: 1709-1713.
    PubMedGoogle Scholar
  • 7 Shimizu A, Nagel GM, Doolittle RF. Photoaffinity labeling of the primary fibrin polymerization site: isolation and characterization of a labeled cyanogen bromide fragment corresponding to gamma-chain residues 337–379. Proc Natl Acad Sci USA 1992; 89: 2888-2892.
    CrossrefPubMedGoogle Scholar
  • 8 Vu D, Di Sanza C, Caille D. et al. Quality control of fibrinogen secretion in the molecular pathogenesis of congenital afibrinogenemia. Hum Mol Genet 2005; 14: 3271-3280.
    CrossrefPubMedGoogle Scholar
  • 9 Dear A, Dempfle CE, Brennan SO. et al. Fibrinogen Mannheim II: a novel gamma307 His-->Tyr substitution in the gammaD domain causes hypofibrinogenemia. J Thromb Haemost 2004; 2: 2194-2199.
    CrossrefPubMedGoogle Scholar
  • 10 Meyer M, Franke K, Richter W. et al. New molecular defects in the gamma subdomain of fibrinogen D-domain in four cases of (hypo)dysfibrinogenemia: fibrinogen variants Hannover VI Homburg VII Stuttgart and Suhl. Thromb Haemost 2003; 89: 637-646.
    Artikel in Thieme ConnectPubMedGoogle Scholar
  • 11 de Raucourt E, de Mazancourt P, Maghzal GJ. et al. Fibrinogen Saint-Germain II: hypofibrinogenemia due to heterozygous gamma N345S mutation. Thromb Haemost 2005; 94: 965-968.
    Artikel in Thieme ConnectPubMedGoogle Scholar
  • 12 Song KS, Park NJ, Choi JR. et al. Fibrinogen Seoul (FGG Ala341Asp): A Novel Mutation Associated With Hypodysfibrinogenemia. Clin Appl Thromb Hemost 2006; 12: 338-343.
    CrossrefPubMedGoogle Scholar