New molecular defects in the γ subdomain of fibrinogen D-domain in four cases of (hypo)dysfibrinogenemia: Fibrinogen variants Hannover VI, Homburg VII, Stuttgart and Suhl

Thrombosis and Haemostasis

Volumn 89, Issue 4, 2003, Pages 637-646

  Meyer, Michael ^a   Franke, Kathrin ^a   Richter, Walter ^b   Steiniger, Frank ^b   Seyfert, Ulrich T ^c   Schenk, Joachim ^c   Treuner, Jörn ^d   Haberbosch, Werner ^e   Eisert, Roswit ^f   Barthels, Monika ^f  

^a UNIVERSITY OF APPLIED SCIENCES JENA   (Germany)

^b FRIEDRICH SCHILLER UNIVERSITY JENA   (Germany)

^c SAARLAND UNIVERSITY   (Germany)

^d OLGAHOSPITAL   (Germany)

^e Suhl Central Hospital   (Germany)

^f HANNOVER MEDICAL SCHOOL   (Germany)

Author keywords

D domain; Dysfibrinogenemia; Fibrinogen variants; Hypofibrinogenemia

Indexed keywords

ALBUMIN; CALCIUM ION; FIBRIN; FIBRINOGEN; FIBRINOGEN HANNOVER 6; FIBRINOGEN HOMBURG 7; FIBRINOGEN STUTTGART; FIBRINOGEN SUHL; FIBRINOGEN VARIANT; UNCLASSIFIED DRUG;

ADULT; AMINO ACID SUBSTITUTION; ARTICLE; CALCIUM BINDING; CALCIUM BLOOD LEVEL; CASE REPORT; CONTROLLED STUDY; DEEP VEIN THROMBOSIS; DYSFIBRINOGENEMIA; FEMALE; FIBRIN CLOT; FIBRIN POLYMERIZATION; FIBRINOGEN DEFECT; GENE MUTATION; HETEROZYGOTE; HUMAN; HYPOFIBRINOGENEMIA; MALE; MUTATIONAL ANALYSIS; PLASMA; PRESCHOOL CHILD; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; THROMBIN TIME; THROMBOPHILIA; THROMBOSIS;

EID: 0037395275     PISSN: 03406245     EISSN: None     Source Type: Journal    
DOI: 10.1055/s-0037-1613585     Document Type: Article

References (35)

1. Henschen A, McDonagh J. Fibrinogen, fibrin and factor XIII. In: Blood Coagulation. Zwaal RFA, Hemker HC, eds. Amsterdam: Elsevier Science Publ 1986; 171-241.
2. Doolittle RF. Fibrinogen and fibrin. In: Haemostasis and Thrombosis, 2nd Edn. Bloom F, Thomas DP, eds. Edinburgh: Churchill Livingstone 1981; 163-91.
3. Cierniewski CS, Budzynski AZ. Localization of the crosslinking site of GPRVVERHK in the γ-chain of human fibrinogen. Eur J Biochem 1993; 218: 321-5.
4. 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.
5. Váradi A, Scheraga HA. Localization of segments essential for polymerization and calcium binding in the γ-chain of human fibrinogen. Biochemistry 1986; 25: 519-28.
6. Shimizu A, Nagel GM, Doolittle RF. Photo-affinity labeling of the primary fibrin polymerization site: Isolation and characterization of a labeled cynogen bromide fragment corresponding to γ-chain of human fibrinogen. Proc Natl Acad Sci USA 1992; 89: 2888-92.
7. Pratt KP, Cotè HCF, Chung DW, Stenkamp RE, Davie EW. The fibrin polymerization pocket: Three-dimensional structure of a 30-kDa C-terminal γ-chain fragment complexed with the peptide Gly-Pro-Arg-Pro. Proc Natl Acad Sci USA 1997; 94: 7176-81.
8. Ebert RF. Index of Variant Human Fibrinogen. CRC Press, Boca Raton, 1994.
9. Fibrinogen variants. Database. www.geht.org/pages/database.
10. Coté HCF, Lord ST, Pratt KP. γ-chain dysfibrinogenemias: Molecular structure-function relationships of naturally occuring mutations in the γ chain of human fibrinogens. Blood 1998; 92: 2195-212.
11. Hogan KA, Gorkun OV, Lounes KC, Coates AI, Weisel JW, Hantgan RR, Lord ST. Recombinant fibrinogen Vlissingen/Frankfurt IV. The deletion of residues 319 and 320 from the γ chain of fibrinogen alters calcium binding, fibrin polymerization, cross-linking, and platelet aggregation. J Biol Chem 2000; 275: 17778-85.
12. Remijn JA, IJsseldijk MJ, Van Hemel BM, Galanakis DK, Hogan KA, Lounes KC, Lord ST, Sixma JJ, De Groot PG. Reduced platelet adhesion in flowing blood to fibrinogen by alterations in segment gamma316-322, part of the fibrin-specific region. Br J Haematol 2002; 117: 650-7.
13. Lord ST, Gorkun OV. Insight from studies with recombinant fibrinogens. Ann N Y Acad Sci 2001; 936: 101-16.
14. Spraggon G, Everse SJ, Doolittle RF. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature 1997; 389: 455-62.
15. Everse SJ, Spraggon G, Veerapandian L, Riley M, Doolittle RF. Crystal structure of fragment double-D from human fibrin with two different bound ligands. Biochemistry 1998; 37: 8637-42.
16. Yee VC, Pratt KP, Cote HC,Trong IL, Chung DW, Davie EW, Stenkamp RE, Teller DC. Crystal structure of a 30 kDa C-terminal fragment from the gamma chain of human fibrinogen. Structure 1997; 5: 125-38.
17. Kazal LA, Amsel S, Miller OP, Tocantins LM. The preparation and some properties of fibrinogen precipitated from human plasma by glycine. Proc Soc Exptl Biol Med 1963; 113: 989-94.
18. Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680-5.
19. Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc Natl Acad Sci USA 1979; 76: 4350-4.
20. Everse SJ, Spraggon G, Doolittle RF. A three-dimensional consideration of variant human fibrinogens. Thromb Haemost 1998; 80: 1-9.
21. Haverkate F, Timan G Protective effect of calcium in the plasmin degradation of fibrinogen and fibrin fragments D. Thromb Res 1977; 10: 803-12.
22. Furlan M, Stucki B, Steinmann C, Jungo M, Laemmle B. Normal binding of calcium to five fibrinogen variants with mutations in the carboxy terminal part of the γ-chain. Thromb Haemost 1996; 76: 377-83.
23. Steinmann C, Reber P, Jungo M, Laemmle B, Heinemann G, Wermuth B, Furlan M. Fibrinogen Bern I: Substitution gamma 337 Asn→Lys is responsible for defective fibrin monomer polymerization. Blood 1993; 82: 2104-8.
24. Koopman J, Haverkate F, Grimbergen J, Lord ST, Mosesson MW, DiOrio JP, Siebenlist KS, Legrand C, Soria J, Soria C, Caen JP. Molecular basis for fibrinogen Dusart (Aα 554 Arg→Cys) and its association with abnormal fibrin polymerization and thrombophilia. J Clin Invest 1993; 91: 1637-43.
25. Marchi R, Lundberg U, Grimbergen J, Koopman J, Torres A, De Bosch NB, Haverkate F, Arocha Pinango CL. Fibrinogen Caracas V, an abnormal fibrinogen with an Aα 532 Ser→Cys substitution associated with thrombosis. Thromb Haemost 2000; 84: 263-70.
26. Steinmann C, Boegli C, Jungo M, Laemmle B, Heinemann G, Wermuth B, Redaelli R, Baudo F, Furlan M. A new substitution, γ358 Ser→Cys, in fibrinogen Milano VII causes defective fibrin polymerization. Blood 1994; 84: 1874-80.
27. Okumura N, Furihata K, Terasawa F, Nakagoshi R, Ueno I, Katsuyama T. Fibrinogen Matsumoto I: A γ364 Asp→His (GAT→CAT) substitution associated with defective fibrin polymerization. Thromb Haemost 1996; 75: 887-91.
28. Bentolila S, Samama MM, Conard J, Horellou MH, French P. Association of dysfibrinogenemia and thrombosis. Apropos of a family (Fibrinogen Melun) and review of the literature. Ann Med Interne Paris 1995; 146: 575-80.
29. Yoshida N, Hirata H, Morigami Y, Imaoka S, Matsuda M, Yamazumi K, Asakura S. Characterization of an abnormal fibrinogen Osaka V with the replacement of γ-arginine 375 by glycine. The lack of high affinity calcium binding to the D-domain and the lack of protective effect of calcium on fibrinolysis. J Biol Chem 1992; 267: 2753-9.
30. Doolittle RF. A detailed consideration of a principal domain of vertebrate fibrinogen and its relatives. Protein Sci 1992; 1: 1563-77.
31. Haverkate F, Samama M. Familial dysfibrinogenemia and thrombophilia. Report on a study of the SSC subcommittee on fibrinogen. Thromb Haemost 1995; 73: 151-61.
32. Reber P, Furlan M, Henschen A, Kaudewitz H, Barbui T, Hilgrad P, Nenci GG, Berrettini M, Beck EA. Three abnormal fibrinogen variants with the same amino acid substitution (γ275 Arg→His): Fibrinogens Bergamo II, Essen and Perugia. Thromb Haemost 1986; 56: 401-6.
33. 275 Arg→His). Thromb Haemost 1989; 62: 875-9.
34. Koopman J, Haverkate F, Briet E, Lord ST. A congenitally abnormal fibrinogen (Vlissingen) with a 6-base deletion in the γ-chain, causing defective calcium binding and impaired fibrin polymerization. J Biol Chem 1991; 266: 13456-61.
35. Collet J-P, Soria J, Mirshahi M, Hirsch M, Dagonnet FB, Caen J, Soria C. Dusart syndrome: A new concept of the relationship between fibrin clot architecture and fibrin clot degradability: Hypofibrinolysis related to an abnormal clot structure. Blood 1993; 82: 2462-9.