Recombinant fibrinogen, γ275Arg → Cys, exhibits formation of disulfide bond with cysteine and severly impaired D:D interactions

Journal of Thrombosis and Haemostasis

Volumn 2, Issue 3, 2004, Pages 468-475

  Ishikawa, S ^a,b   Hirota Kawadobora, M ^b   Tozuka, M ^b   Ishii, K ^b   Terasawa, F ^c   Okumura, Nobuo ^c  

^a SHINSHU UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^b SHINSHU UNIVERSITY HOSPITAL   (Japan)

^c SHINSHU UNIVERSITY   (Japan)

Author keywords

Disulfide bond; Fibrin polymerization; Recombinant fibrinogen; Variant fibrinogen; XIIIa catalyzed cross linking of fibrin

Indexed keywords

ARGININE; CYSTEINE; FIBRIN; FIBRINOGEN; BLOOD CLOTTING FACTOR 13A; DISULFIDE; PRIMER DNA; RECOMBINANT PROTEIN; THROMBIN;

ALPHA CHAIN; ANIMAL CELL; ARTICLE; BETA CHAIN; CARBOXY TERMINAL SEQUENCE; CHO CELL; CONTROLLED STUDY; DIMERIZATION; DISULFIDE BOND; DYSFIBRINOGENEMIA; FIBRIN CLOT; FIBRIN POLYMERIZATION; FIBRINOGEN BLOOD LEVEL; FIBRINOGEN SYNTHESIS; GENETIC TRANSFECTION; HUMAN; IMMUNOAFFINITY CHROMATOGRAPHY; NONHUMAN; PLASMID; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN CROSS LINKING; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; SCANNING ELECTRON MICROSCOPY; AMINO ACID SUBSTITUTION; BINDING SITE; CATALYSIS; CHEMISTRY; KINETICS; METABOLISM; MOLECULAR WEIGHT; NUCLEOTIDE SEQUENCE; SITE DIRECTED MUTAGENESIS; ULTRASTRUCTURE;

AMINO ACID SUBSTITUTION; ARGININE; BASE SEQUENCE; BINDING SITES; CATALYSIS; CYSTEINE; DISULFIDES; DNA PRIMERS; FACTOR XIIIA; FIBRIN; FIBRINOGEN; HUMANS; KINETICS; MICROSCOPY, ELECTRON, SCANNING; MOLECULAR WEIGHT; MUTAGENESIS, SITE-DIRECTED; RECOMBINANT PROTEINS; THROMBIN;

EID: 3242667358     PISSN: 15387933     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1538-7836.2004.00600.x     Document Type: Article

References (31)

1. Hantgan RR, Hermans J. Assembly of fibrin. A light scattering study. J Biol Chem 1979; 254: 11272-81.
2. Budzynski AZ, Olexa SA, Pandya BV. Fibrin polymerization sites in fibrinogen and fibrin fragments. Ann N Y Acad Sci 1983; 408: 301-14.
3. Blomback B, Hessel B, Hogg D, Therkildsen L. A two-step fibrinogen-fibrin transition in blood coagulation. Nature 1978; 275: 501-5.
4. Matsuda M, Baba M, Morimoto K, Nakamikawa C. 'Fibrinogen Tokyo II' an abnormal fibrinogen with an impaired polymerization site on the aligned DD domain of fibrin molecules. J Clin Invest 1983; 72: 1034-41.
5. Mosesson MW, Siebenlist KR, DiOrio JP, Matsuda M, Hainfeld JF, Wall JS. The role of fibrinogen D domain intermolecular association sites in the polymerization of fibrin and fibrinogen Tokyo II (γ 275 Arg- > Cys). J Clin Invest 1995; 96: 1053-8.
6. Henschen A, Kehl M, Southan C. Genetically abnormal fibrinogens - strategies for structure elucidation, including fibrinopeptide analysis. Curr Probl Clin Biochem 1984; 14: 273-320.
7. Cote HCF, 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.
8. Matsuda M, Sugo T. Structure and function of human fibrinogen inferred from dysfibrinogens. Int J Hematol 2002; 76(Suppl. 1): 352-60.
9. http://www.geht.org/pages/database_fibrino_uk.html
10. Terasawa F, Okumura N, Higuchi Y, Ishikawa S, Tozuka M, Ishida F, Kitano K, Katsuyama T. Fibrinogen Matsumoto III: a variant with γ275 Arg- > Cys (CGC- > TGC) - comparison of fibrin polymerization properties with those of Matsumoto I (γ364 Asp- > His) and Matsumoto II (γ308 Asn- > Lys). Thromb Haemost 1999; 81: 763-6.
11. 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.
12. 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.
13. Hogan KA, Lord ST, Okumura N, Terasawa F, Galanakis DK, Scharrer I, Gorkun OV. A functional assay suggests that heterodimers exist in two C-terminal γ-chain dysfibrinogens. Matsumoto I and Vlissingen/Frankfurt IV. Thromb Haemost 2000; 83: 592-7.
14. Okumura N, Terasawa F, Fujita K, Fujihara N, Tozuka M, Koh C-S. Evidence that heterodimers exist in the fibrinogen Matsumoto II (γ308N- > K) proband and participate in fibrin fiber formation. Thromb Res 2002; 107: 157-62.
15. Okumura N, Gorkun OV, Lord ST. Severely impaired polymerization of recombinant fibrinogen γ-364 Asp- > His, the substitution discovered in a heterozygous individual. J Biol Chem 1997; 272: 29596-601.
16. Takebe M, Soe G, Kohno I, Sugo T, Matsuda M. Calcium ion-dependent monoclonal antibody against human fibrinogen; preparation, characterization, and application to fibrinogen purification. Thromb Haemost 1995; 73: 662-7.
17. Mihalyi E. Physicochemical studies of bovine fibrinogen. IV. Ultraviolet absorption and its relation to the structure of the molecule. Biochemistry 1968; 7: 208-23.
18. Lounes KC, Lefkowitz JB, Henschen-Edman AH, Coates AI, Hantgan RR, Lord ST. The impaired polymerization of fibrinogen Longmont (Bβ166Arg- > Cys) is not improved by removal of disulfide-linked dimers from a mixture of dimers and cysteine-linked monomers. Blood 2001; 98: 661-6.
19. Furlan M, Rupp C, Beck EA. Inhibition of fibrin polymerization by fragment D is affected by calcium, Gly-Pro-Arg and Gly-His-Arg. Biochim Biophys Acta 1983; 742: 25-32.
20. Hirota-Kawadobora M, Terasawa F, Yonekawa O, Sahara N, Shimizu E, Okumura N, Katsuyama T, Shigematsu H. Fibrinogens Kosai and Ogasa: Bβ15Gly- > Cys (GGT- > TGT) substitution associated with impairment of fibrinopeptide B release and lateral aggregation. J Thromb Haemost 2003; 1: 275-83.
21. Holm B, Nilsen DWT, Kierulf P, Godal HC. Purification and characterization of 3 fibrinogens with different molecular weights obtained from normal human plasma. Thromb Res 1985; 37: 165-76.
22. Miyata T, Terukina S, Matsuda M, Kasamatsu A, Takeda Y, Murakami T, Iwanaga S. Fibrinogens Kawaguchi and Osaka: an amino acid substitution of Aα arginine-16 to cysteine which forms an extra interchain disulfide bridge between the two Aα chains. J Biochem (Tokyo) 1987; 102:93-101.
23. Pirkle H, Kaydewitz H, Henschen A, Theodor I. Substitution of Bβ14 arginine by cyst(e)ine in fibrinogen Seattle I. In: Lowe GDO, Douglas JT, Forbes CD, Henschen A, eds. Fibrinogen 2. Biochemistry, Physiology and Clinical Relevance. Amsterdam: Elsevier Science Publishers, 1987: 49-52.
24. 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.
25. Steinmann C, Bogli C, Jungo M, Lammle 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.
26. Terukina S, Matsuda M, Hirata H, Takeda Y, Miyata T, Takao T, Shimonishi Y. Substitution of γArg-275 by Cys in an abnormal fibrinogen, 'fibrinogen Osaka II'. Evidence for a unique solitary cystine structure at the mutation site. J Biol Chem 1988; 263: 13579-87.
27. Borrell M, Gari M, Coll I, Vallve C, Tirado I, Soria JM, Sala N, Munoz C, Oliver A, Garcia A, Fontcuberta J. Abnormal polymerization and normal binding of plasminogen and t-PA in three new dysfibrinogenaemias. Barcelona III and IV (γArg275- > His) and Villajoyosa (γArg275- > Cys). Blood Coagul Fibrin 1995; 6: 198-206.
28. Mimuro J, Kawata Y, Niwa K, Muramatsu S, Madoiwa S, Takano H, Sugo T, Sakata Y, Sugimoto T, Nose K, Matsuda M. A new type of substitution for γArg-275 in fibrinogen Kamogawa I characterized by impaired fibrin assembly. Thromb Haemost 1999; 81: 940-4.
29. 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.
30. Weisel JW, Nagaswami C. Computer modeling of fibrin polymerization kinetics correlated with electron microscope and turbidity observations: clot structure and assembly are kinetically controlled. Biophys J 1992; 63: 111-28.
31. 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.