Novel γ230 Asn→Asp substitution in fibrinogen Middlemore associated hypofibrinogenaemia

Thrombosis and Haemostasis

Volumn 93, Issue 6, 2005, Pages 1196-1197

  Brennan, Stephen O ^a   Sheen, Campbell R ^a   George, Peter M ^a  

^a UNIVERSITY OF OTAGO   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; ASPARTIC ACID; FIBRINOGEN; FIBRINOGEN VARIANT; THROMBIN;

ADULT; AMINO ACID SUBSTITUTION; ARTICLE; BLEEDING; CASE REPORT; FEMALE; FIBRINOGEN BLOOD LEVEL; GENE MUTATION; GENE SEQUENCE; GENETIC POLYMORPHISM; HETEROZYGOSITY; HUMAN; HYPOFIBRINOGENEMIA; PEPTIDE MAPPING; PHENOTYPE; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN STRUCTURE; SPONTANEOUS ABORTION; THIRD TRIMESTER PREGNANCY; THROMBIN TIME; AFIBRINOGENEMIA; AMINO ACID SEQUENCE; BLOOD; CHEMICAL STRUCTURE; CHEMISTRY; ELECTROSPRAY MASS SPECTROMETRY; GENETICS; NEWBORN; PREGNANCY; PROTEIN TERTIARY STRUCTURE;

ADULT; AFIBRINOGENEMIA; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; FEMALE; FIBRINOGENS, ABNORMAL; HUMANS; INFANT, NEWBORN; MODELS, MOLECULAR; PEPTIDE MAPPING; PREGNANCY; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION;

EID: 20444456264     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0037-1616629     Document Type: Article

References (16)

1. Henschen AH, McDonagh J. Fibrinogen, fibrin and factor XIII. In: Blood Coagulation, Vol 13. Zwaal RFA, Hemker HC, eds. Amsterdam: Elsevier Science Publishers BV 1986; 171-241.
2. Doolittle RF. The molecular biology of fibrin. In: The Molecular Basis of Blood Diseases. Stamatoyannopoulos G, Nienhuis AW, Majerus PW, Varmus H, eds. Philadelphia: WB Saunders Company 1994; 701-26.
3. Marchant RE, Barb MD, Shainoff R et al. Three dimensional structure of human fibrinogen under aqueous conditions visualised by atomic force microscopy. Thromb Haemost 1997; 77: 1048-51.
4. Spraggon G, Everse SJ, Doolittle RF. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart ftom fibrin. Nature 1997; 389: 455-62.
5. Yee VC, Pratt KP, Cote HCF et al. Crystal structure of a 30 kDa C-terminal fragment from the g chain of human fibrinogen. Structure 1997; 5: 125-38.
6. Yang Z, Mochalkin I, Doolittle RF. A model of fibrin formation based on crystal structures of fibrinogen and fibrin fragments complexed with synthetic peptides. Proc Natl Acad Sci USA 2000; 97: 14156-61.
7. Huang S, Mulvhill ER, Farrell DH et al. Biosynthesis of human fibrinogen. Subunit interactions and potential intermediates in assembly. J Biol Chem 1993; 268: 8919-26.
8. Huang S, Cao Z, Chung DW et al. The role of βg and αg complexes in the assembly of human fibrinogen. J Biol Chem 1996; 271: 27942-7.
9. Maghzal GJ, Brennan SO, Homer VM et al. The molecular mechanisms of congenital hypofibrinogenaemia. Cell Mol Life Sci 2004; 61: 1427-38.
10. Hanss M, Biot FA. A database for human fibrinogen variants. Ann N Y Acad Sci 2001; 86: 154-63. http://www.geht.org/databaseang/fibrinogen
11. Brennan SO, Hammonds B, George PM. Aberrant hepatic processing causes removal of activation peptide and primary polymerisation site from fibrinogen Canterbury (Aa20Val→Asp). J Clin Invest 1995; 96: 2854-8.
12. Brennan SO. Electrospray ionisation analysis of human fibrinogen. Thromb Haemost 1997; 78: 1055-8.
13. Brennan SO. The separation of globin chains by high pressure cation exchange chromatography. Hemoglobin 1986; 9: 53-63.
14. Brennan SO, Fellowes AP, Faed JM et al. Hypofibrinogenaemia in an individual with 2 coding (γ82 A→G and Bβ235 P→L) and 2 noncoding mutations. Blood 2000; 95: 1709-13.
15. McCracken AA, Brodsky JL. Evolving questions and paradigm shifts in endoplasmic-reticulum-associated degradation (ERAD). Bioessays 2003; 9: 868-77.
16. http://www.bmsc.washington.edu/people/teller/fbg_ident.html