A case of congenital afibrinogenemia: Fibrinogen Hakata, a novel nonsense mutation of the fibrinogen γ-chain gene

Thrombosis and Haemostasis

Volumn 84, Issue 1, 2000, Pages 49-53

  Iida, Hiroko ^a   Ishii, Eiichi ^a   Nakahara, Mutsuko ^a   Urata, Michiyo ^a   Wakiyama, Machiko ^a   Kurihara, Masako ^a   Watanabe, Kumiko ^a   Kai, Takeshi ^a   Ihara, Kenji ^b   Kinoshita, Sachiko ^a   Hamasaki, Naotaka ^a  

^a KYUSHU UNIVERSITY HOSPITAL   (Japan)

^b HAMANOMACHI HOSPITAL   (Japan)

Author keywords

Afibrinogenemia; Gene analysis; Nonsense mutation; chain of fibrinogen

Indexed keywords

DNA; FIBRINOGEN; GUANINE; THYMINE;

AFIBRINOGENEMIA; ARTICLE; CASE REPORT; FEMALE; FIBRINOGEN BLOOD LEVEL; HUMAN; LEUKOCYTE; NONSENSE MUTATION; PRIORITY JOURNAL; SCHOOL CHILD; SUPPLEMENTATION;

EID: 0033936548     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0037-1613966     Document Type: Article

References (37)

1. Martinez J. Congenital dysfibrinogenemia. Curr Opin Hematol 1997; 4: 357-65.
2. Galanakis DK. Dysfibrinogenemia. Clin Lab Med 1984; 4: 395-418.
3. Beck EA. Congenital abnormalities of fibrinogen. Clin Haematol 1979; 8: 169-81.
4. Goodwin TM. Congenital hypofibrinogenemia in pregnancy. Obstet Gynecol Surv 1989; 44: 157-61.
5. De Marco L, Girolami A, Zimmerman TS, Ruggeri ZM. von Willebrand factor interaction with the glycoprotein IIb/IIa complex. Its role in platelet function as demonstrated in patients with congenital afibrinogenemia. J Clin Invest 1986; 77: 1272-7.
6. Henschen AH. Human fibrinogen-structural variants and functional sites. Thromb Haemost 1993; 70: 42-7.
7. Matsuda M. The structure-function relationship of hereditary dysfibrinogens. Int J Hematol 1996; 64: 167-79.
8. Neerman-Arbez M, Honsberger A, Antonarakis SE, Morris MA. Deletion of the fibrinogen alpha-chain gene (FGA) causes congenital afibrogenemia. J Clin Invest 1999; 103:215-8.
9. Zhang JZ, Redman CM. Role of interchain disulfide bonds on the assembly and secretion of human fibrinogen. J Biol Chem 1994; 269: 652-8.
10. Kamura T, Tsuda H, Yae Y, Hattori S, Ohga S, Shibata Y, Kawabata S, Hamasaki N. An abnormal fibrinogen Fukuoka II (Gly-Bβ15-Cys) characterized by defective fibrin lateral association and mixed disulfide formation. J Biol Chem 1995; 270: 29392-9.
11. Ridgway HJ, Brennan SO, Faed JM, George PM. Fibrinogen Otago: a major a chain truncation associated with severe hypofibrinogenaemia and recurrent miscarriage. Br J Haematol 1997; 98: 632-9.
12. Pizzolato MA, Goni FR, Salvarezza RC. Immunofixation on cellulose acetate: an improved screening method for monoclonal immunoglobulins. J Immunol Methods 1979; 26: 365-8.
13. Yamazaki T, Sugiura I, Matsushita T, Kojima T, Kagami K, Takamatsu J, Saito H. A phenotypically neutral dimorphism of protein S: the substitution of Lys155 by Glu in the second EGF domain predicted by an A to G base exchange in the gene. Thromb Res 1993; 70: 395-403.
14. Cote HC, Lord ST, Pratt KP. γ-chain dysfibrinogenemias: molecular structure-function relationships of naturally occurring mutations in the γ chain of human fibrinogen. Blood 1998; 92: 2195-212.
15. Cierniewski CS, Budzynski AZ. Localization of the cross-linking site of GPRVVERHK in the γ-chain of human fibrinogen. Eur J Biochem 1993; 218: 321-5.
16. Dang CV, Ebert RF, Bell WR. Localization of a fibrinogen calcium binding site between γ-subunit positions 311 and 336 by terbium fluorescence. J Biol Chem 1985; 260: 9713-9.
17. Varadi A, Scheraga HA. Localization of segments essential for polymerization and for calcium binding in the γ-chain of human fibrinogen. Biochemistry 1986; 25: 519-28.
18. 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 γ-chain residue 337-79. Proc Natl Acad Sci USA 1992; 89: 2888-92.
19. Yamazumi K, Doolittle RF. Photoaffinity labeling of the primary fibrin polymerization site: localization of the label to γ-chain Tyr-363. Proc Natl Acad Sci USA 1992; 89: 2893-6.
20. Kloczewiak M, Timmons S, Lukas TJ, Hawiger J. Platelet receptor recognition site on human fibrinogen. Synthesis and structure-function relationship of peptides corresponding to the carboxy-terminal segment of the γ chain. Biochemistry 1984; 23: 1767-74.
21. Altieri DC, Plescia J, Plow EF. The structural motif glycine 190-valine 202 of the fibrinogen γ chain interacts with CD11b/CD18 integrin (αMβ2, Mac-1) and promotes leukocyte adhesion. J Biol Chem 1993; 268: 1847-53.
22. Varadi A, Patthy L. Location of plasminogen-binding sites in human fibrin(ogen). Biochemistry 1983; 22: 2440-6.
23. Nieuwenhuizen W. Sites in fibrin involved in the acceleration of plasminogen activation by t-PA. Possible role of fibrin polymerization. Thromb Res 1994; 75: 343-7.
24. Yonekawa O, Voskuilen M, Nieuwenhuizen W. Localization in the fibnnogen γ-chain of a new site that is involved in the acceleration of the tissue-type plasminogen activator-catalyzed activation of plasminogen. Biochem J 1992; 283: 187-91.
25. Medved L, Litvinovich S, Ugarova T, Matsuka Y, Ingham K. Domain structure and functional activity of the recombinant human fibrinogen γ-module (γ148-411). Biochemistry 1997; 36: 4685-93.
26. Steinmann C, Jungo M, Beck EA, Lammle B, Furlan M. Fibrinogen Claro-another dysfunctional fibrinogen variant with γ275 arginine-histidine substitution. Thromb Res 1996; 81: 145-50.
27. Niwa K, Takebe M, Sugo T, Kawata Y, Mimuro J, Asakura S, Sakata Y, Mizushima J, Maeda A, Endo H, Matsuda M. A γ Gly-268 to Glu substitution is responsible for impaired fibrin assembly in a homozygous dysfibrinogen Kurashiki I. Blood 1996: 87: 4686-94.
28. Fellowes AP, Brennan SO, Ridgway HJ, Heaton DC, George PM. Electrospray ionization mass spectrometry identification of fibrinogen Banks Peninsula (γ280Tyr-Cys): a new variant with defective polymerization. Br J Haematol 1998; 101: 24-31.
29. Okumura N, Furihata K, Terasawa F, Ishikawa S, Ueno I, Katsuyama T. Fibrinogen Matsumoto II: γ308 Asn-Lys (AAT-AAG) mutation associated with bleeding tendency. Br J Haematol 1996; 94: 526-8.
30. Callea F, Brisigotti M. Fabbretti G, Bonino F, Desmet VJ. Hepatic endoplasmic reticulum storage diseases. Liver 1992; 12: 357-62.
31. Uzan G, Courtois G, Besmond C, Frain M. Sala-Trepat J, Kahn A, Marguerie G. Analysis of fibrinogen genes in patients with congenital afibrino-genemia. Biochem Biophys Res Commun 1984; 120: 376-83.
32. Koopman J, Haverkate F, Grimbergen J, Egbring R, Lord ST. Fibrinogen Marburg: a homozygous case of dysfibrinogenemia, lacking amino acids Aα 461-610 (Lys 461 AAA → stop TAA). Blood 1992; 80:1972-9.
33. Furlan M, Steinmann C, Jungo M, Bogli C, Baudo F, Redaelli R, Fedeli F, Lammle B. A frameshift mutation in Exon V of the A alpha-chain gene leading to truncated A alpha-chains in the homozygous dysfibrinogen Milano III. J Biol Chem 1994; 269: 33129-34.
34. Gorkun OV, Lord ST. Recombinant fibrinogen in clot formation. Fibrinolysis 1996; 10 (Suppl. 4): 7.
35. Suh TT, Holmback K, Jensen NJ, Daugherty CC, Small K, Simon DJ, Potter S, Degen JL. Resolution of spontaneous bleeding events but failure of pregnancy in fibrinogen-deficient mice. Genes Dev 1995; 9: 2020-33
36. Huang S, Mulvihill ER, Farrell DH, Chung DW, Davie EW. Biosynthesis of human fibrinogen. Subunit interactions and potential intermediates in assembly. J Biol Chem 1993; 268: 8919-26.
37. Roy SN, Procyk R, Kudryk BJ, Redman CM. Assembly and secretion of recombinant human fibrinogen. J Biol Chem 1991; 266: 4758-63.