1. Weisel, J.W. Fibrinogen and fibrin. Adv. Protein. Chem. 2005, 70, 247–299. [CrossRef] [PubMed]
2. Huang, S.; Cao, Z.; Chung, D.W.; Davie, E.W. The role of βγ and αγ complexes in the assembly of human fibrinogen. J. Biol. Chem. 1996, 271, 27942–27947. [CrossRef]
3. Medved, L.; Weisel, J.W. Fibrinogen and Factor XIII Subcommittee of Scientific Standardization Committee of International Society on Thrombosis and Haemostasis. Recommendations for nomenclature on fibrinogen and fibrin. J. Thromb. Haemost. 2009, 7, 355–359. [CrossRef]
4. Simurda, T.; Snahnicanova, Z.; Loderer, D.; Sokol, J.; Stasko, J.; Lasabova, Z.; Kubisz, P. Fibrinogen Martin: A Novel Mutation in FGB (Gln180Stop) Causing Congenital Afibrinogenemia. Semin. Thromb. Hemost. 2016, 42, 455–458. [CrossRef]
5. Doolittle, R.F. Fibrinogen and fibrin. Annu. Rev. Biochem. 1984, 53, 195–229. [CrossRef] [PubMed]
6. Mosesson, M.W.; Siebenlist, K.R.; DiOrio, J.P.; Matsuda, M.; Hainfeld, J.F.; Wall, J.S. The role of fibrinogen D domain intermolecular association sites in the polymerization of fibrin and fibrinogen Tokyo II (γ 275 Arg→Cys). J. Clin. Investig. 1995, 96, 1053–1058. [CrossRef]
7. Spraggon, G.; Everse, S.J.; Doolittle, R.F. Crystal structures of fragment D from human fibrinogen and its crosslinked counterpart from fibrin. Nature 1997, 389, 455–462. [CrossRef] [PubMed]
8. Yang, Z.; Mochalkin, I.; Doolittle, R.F. 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, 14156–14161. [CrossRef] [PubMed]
9. Mosesson, M.W.; DiOrio, J.P.; Siebenlist, K.R.; Wall, J.S.; Hainfeld, J.F. Evidence for a second type of fibril branch point in fibrin polymer networks, the trimolecular junction. Blood 1993, 82, 1517–1521. [CrossRef]
10. Mosesson, M.W. Fibrinogen and fibrin structure and functions. J. Thromb. Haemost. 2005, 3, 1894–1904. [CrossRef]
11. Lord, S.T. Molecular mechanisms affecting fibrin structure and stability. Arterioscler. Thromb. Vasc. Biol. 2011, 31, 494–499. [CrossRef]
12. GFHT Web Site. Available online: https://site.geht.org/base-de-donnees-fibrinogene/ (accessed on 22 March 2021).
13. Simurda, T.; Zolkova, J.; Kolkova, Z.; Loderer, D.; Dobrotova, M.; Skornova, I.; Brunclíkova, M.; Grendar, M.; Lasabova, Z.; Stasko, J.; et al. Comparison of clinical phenotype with genetic and laboratory results in 31 patients with congenital dysfibrinogenemia in northern Slovakia. Int. J. Hematol. 2020, 111, 795–802. [CrossRef]
14. de Moerloose, P.; Casini, A.; Neerman-Arbez, M. Congenital fibrinogen disorders: An update. Semin. Thromb. Hemost. 2013, 39, 585–595. [CrossRef] [PubMed]
15. Hirota-Kawadobora, M.; Terasawa, F.; Suzuki, T.; Tozuka, M.; Sano, K.; Okumura, N. Comparison of thrombin-catalyzed fibrin polymerization and factor XIIIa-catalyzed cross-linking of fibrin among three recombinant variant fibrinogens, γ 275C, γ 275H, and γ 275A. J. Thromb. Haemost. 2004, 2, 1359–1367. [CrossRef] [PubMed]
16. Ferguson, E.W.; Fretto, L.J.; McKee, P.A. A re-examination of the cleavage of fibrinogen and fibrin by plasmin. J. Biol. Chem. 1975, 250, 7210–7218. [CrossRef]
17. Kamijyo, Y.; Hirota-Kawadobora, M.; Fujihara, N.; Wakabayashi, S.; Matsuda, K.; Yamauchi, K.; Terasawa, F.; Okumura, N.; Honda, T. Functional analysis of heterozygous plasma dysfibrinogens derived from two families of γArg275Cys and three families of γArg275His, and haplotype analysis for these families. Rinsho Byori 2009, 57, 651–658.
18. Terasawa, F.; Kamijyo, Y.; Fujihara, N.; Okumura, N. Assembly and secretion of mutant fibrinogens with variant γ-chain C terminal region (γ313-γ345). Rinsho Byori 2010, 58, 772–778. [PubMed]
19. Brennan, S.O.; Wyatt, J.; Medicina, D.; Callea, F.; George, P.M. Fibrinogen brescia: Hepatic endoplasmic reticulum storage and hypofibrinogenemia because of a γ284 Gly→Arg mutation. Am. J. Pathol. 2000, 157, 189–196. [CrossRef]
20. Fellowes, A.P.; Brennan, S.O.; Ridgway, H.J.; Heaton, D.C.; George, P.M. Electrospray ionization mass spectrometry identification of fibrinogen Banks Peninsula (γ280Tyr→Cys): A new variant with defective polymerization. Br. J. Haematol. 1998, 101, 24–31. [CrossRef]
21. Asselta, R.; Robusto, M.; Platé, M.; Santoro, C.; Peyvandi, F.; Duga, S. Molecular characterization of 7 patients affected by dys- or hypo-dysfibrinogenemia: Identification of a novel mutation in the fibrinogen Bβ chain causing a gain of glycosylation. Thromb. Res. 2015, 136, 168–174. [CrossRef]
22. Zhu, L.; Wang, M.; Xie, H.; Jin, Y.; Yang, L.; Xu, P. A novel fibrinogen mutation (γ Thr277Arg) causes hereditary hypofibrinogene- mia in a Chinese family. Blood Coagul. Fibrinolysis 2013, 24, 642–644. [CrossRef]
23. Terasawa, F.; Okumura, N.; Kitano, K.; Hayashida, N.; Shimosaka, M.; Okazaki, M.; Lord, S.T. Hypofibrinogenemia associated with a heterozygous missense mutation γ153Cys to arg (Matsumoto IV): In vitro expression demonstrates defective secretion of the variant fibrinogen. Blood 1999, 94, 4122–4131. [CrossRef] [PubMed]
24. Arai, S.; Ogiwara, N.; Mukai, S.; Takezawa, Y.; Sugano, M.; Honda, T.; Okumura, N. The fibrous form of intracellular inclusion bodies in recombinant variant fibrinogen-producing cells is specific to the hepatic fibrinogen storage disease-inducible variant fibrinogen. Int. J. Hematol. 2017, 105, 758–768. [CrossRef] [PubMed]
25. Brennan, S.O.; Wyatt, J.M.; Ockelford, P.; George, P.M. Defective fibrinogen polymerization associated with a novel γ279Ala→Asp mutation. Br. J. Haematol. 2000, 108, 236–240. [CrossRef] [PubMed]
26. Kaido, T.; Yoda, M.; Kamijo, T.; Taira, C.; Higuchi, Y.; Okumura, N. Heterozygous variant fibrinogen γA289V (Kanazawa III) was confirmed as hypodysfibrinogenemia by plasma and recombinant fibrinogens. Int. J. Lab. Hematol. 2020, 42, 190–197. [CrossRef]
27. Bantia, S.; Mane, S.M.; Bell, W.R.; Dang, C.V. Fibrinogen Baltimore I: Polymerization defect associated with a γ 292Gly—-Val (GGC—-GTC) mutation. Blood 1990, 76, 2279–2283. [CrossRef]
28. Kobayashi, T.; Takezawa, Y.; Terasawa, F.; Okumura, N. Comparison of fibrinogen synthesis and secretion between novel variant fibrinogen, nagakute (γ305Thr→Ala), and other variants located in γ305-308 residues. Rinsho Byori 2012, 60, 831–838.
29. Dear, A.; Dempfle, C.E.; Brennan, S.O.; Kirschstein, W.; George, P.M. Fibrinogen Mannheim II: A novel γ307 His→Tyr substitution in the γD domain causes hypofibrinogenemia. J. Thromb. Haemost. 2004, 2, 2194–2199. [CrossRef]
30. Okumura, N.; Furihata, K.; Terasawa, F.; Nakagoshi, R.; Ueno, I.; Katsuyama, T. Fibrinogen Matsumoto I: A γ 364 Asp→His (GAT→CAT) substitution associated with defective fibrin polymerization. Thromb. Haemost. 1996, 75, 887–891. [CrossRef]
31. Okumura, N.; Terasawa, F.; Fujita, K.; Tozuka, M.; Ota, H.; Katsuyama, T. Difference in electrophoretic mobility and plasmic digestion profile between four recombinant fibrinogens, γ 308K, γ 308I, γ 308A, and wild type (γ 308N). Electrophoresis 2000, 21, 2309–2315. [CrossRef]
32. Ebert, R.F.; Bell, W.R. Fibrinogen Baltimore III: Congenital dysfibrinogenemia with a shortened gamma-subunit. Thromb. Res. 1988, 51, 251–258. [CrossRef]
33. Meyer, M.; Bergmann, F.; Brennan, S.O. Novel fibrinogen mutation (γ 313 Ser→Asn) associated with hypofibrinogenemia in two unrelated families. Blood Coagul. Fibrinolysis 2006, 17, 63–67. [CrossRef] [PubMed]
34. Brennan, S.O.; Davis, R.L.; Conard, K.; Savo, A.; Furuya, K.N. Novel fibrinogen mutation γ314Thr→Pro (fibrinogen AI duPont) associated with hepatic fibrinogen storage disease and hypofibrinogenaemia. Liver Int. 2010, 30, 1541–1547. [CrossRef]
35. Mukai, S.; Ikeda, M.; Takezawa, Y.; Sugano, M.; Honda, T.; Okumura, N. Differences in the function and secretion of congenital aberrant fibrinogenemia between heterozygous γD320G (Okayama II) and γ∆N319-∆D320 (Otsu I). Thromb. Res. 2015, 136, 1318–1324. [CrossRef]
36. Lounes, K.C.; Soria, C.; Valognes, A.; Turchini, M.F.; Soria, J.; Koopman, J. Fibrinogen Bastia (γ 318 Asp→Tyr) a novel abnormal fibrinogen characterized by defective fibrin polymerization. Thromb. Haemost. 1999, 82, 1639–1643. [CrossRef] [PubMed]
37. Brennan, S.O.; Davis, R.L.; Mosesson, M.W.; Hernandez, I.; Lowen, R.; Alexander, S.J. Congenital hypodysfibrinogenaemia (Fibrinogen Des Moines) due to a γ320Asp deletion at the Ca2+ binding site. Thromb. Haemost. 2007, 98, 467–469. [PubMed]
38. Brennan, S.O.; Laurie, A. Functionally compromised FGG variant (γ320Asp→Glu) expressed at low level in plasma fibrinogen. Thromb. Res. 2014, 134, 744–746. [CrossRef]
39. Haneishi, A.; Terasawa, F.; Fujihara, N.; Yamauchi, K.; Okumura, N.; Katsuyama, T. Recombinant variant fibrinogens substituted at residues γ326Cys and γ339Cys demonstrated markedly impaired secretion of assembled fibrinogen. Thromb. Res. 2009, 124, 368–372. [CrossRef]
40. Guglielmone, H.A.; Sanchez, M.C.; Abate Daga, D.; Bocco, J.L. A new heterozygous mutation in gamma fibrinogen gene leading to 326 Cys→Ser substitution in fibrinogen Córdoba is associated with defective polymerization and familial hypodysfibrinogenemia. J. Thromb. Haemost. 2004, 2, 352–354. [CrossRef]
41. Meyer, M.; Franke, K.; Richter, W.; Steiniger, F.; Seyfert, U.T.; Schenk, J.; Treuner, J.; Haberbosch, W.; Eisert, R.; Barthels, M. 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.
42. Song, K.S.; Park, N.J.; Choi, J.R.; Doh, H.J.; Chung, K.H. Fibrinogen Seoul (FGG Ala341Asp): A novel mutation associated with hypodysfibrinogenemia. Clin. Appl. Thromb. Hemost. 2006, 12, 338–343. [CrossRef] [PubMed]
43. Okumura, N.; Gorkun, O.V.; Lord, S.T. Severely impaired polymerization of recombinant fibrinogen gamma-364 Asp → His, the substitution discovered in a heterozygous individual. J. Biol. Chem. 1997, 272, 29596–29601. [CrossRef] [PubMed]
44. Kobayashi, T.; Arai, S.; Ogiwara, N.; Takezawa, Y.; Nanya, M.; Terasawa, F.; Okumura, N. γ375W fibrinogen-synthesizing CHO cells indicate the accumulation of variant fibrinogen within endoplasmic reticulum. Thromb. Res. 2014, 133, 101–107. [CrossRef]
45. 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 gamma-arginine 375 by glycine. The lack of high affinity calcium binding to D-domains and the lack of protective effect of calcium on fibrinolysis. J. Biol. Chem. 1992, 267, 2753–2759. [CrossRef]
46. Ikeda, M.; Kobayashi, T.; Arai, S.; Mukai, S.; Takezawa, Y.; Terasawa, F.; Okumura, N. Recombinant γT305A fibrinogen indicates severely impaired fibrin polymerization due to the aberrant function of hole ‘A’ and calcium binding sites. Thromb. Res. 2014, 134, 518–525. [CrossRef]
47. Appel, I.M.; Grimminck, B.; Geerts, J.; Stigter, R.; Cnossen, M.H.; Beishuizen, A. Age dependency of coagulation parameters during childhood and puberty. J. Thromb. Haemost. 2012, 10, 2254–2263. [CrossRef]
48. Duga, S.; Braidotti, P.; Asselta, R.; Maggioni, M.; Santagostino, E.; Pellegrini, C.; Coggi, G.; Malcovati, M.; Tenchini, M.L. Liver histology of an afibrinogenemic patient with the Bβ-L353R mutation showing no evidence of hepatic endoplasmic reticulum storage disease (ERSD); comparative study in COS-1 cells of the intracellular processing of the Bβ-L353R fibrinogen vs. the ERSD-associated γ-G284R mutant. J. Thromb. Haemost. 2005, 3, 724–732. [CrossRef]
49. Platè, M.; Asselta, R.; Spena, S.; Spreafico, M.; Fagoonee, S.; Peyvandi, F.; Tenchini, M.L.; Duga, S. Congenital hypofibrinogenemia: Characterization of two missense mutations affecting fibrinogen assembly and secretion. Blood Cells Mol. Dis. 2008, 41, 292–297. [CrossRef] [PubMed]
50. Vu, D.; Di Sanza, C.; Neerman-Arbez, M. Manipulating the quality control pathway in transfected cells: Low temperature allows rescue of secretion-defective fibrinogen mutants. Haematologica 2008, 93, 224–231. [CrossRef]
51. Rooney, M.M.; Parise, L.V.; Lord, S.T. Dissecting clot retraction and platelet aggregation. Clot retraction does not require an intact fibrinogen gamma chain C terminus. J. Biol. Chem. 1996, 271, 8553–8555. [CrossRef]
論文の公開元へ
