Fibrinogen Caracas I: A dysfibrinogenemia with a hemorrhagic diathesis associated with diminished fibrin fiber diameter and reduced fibrin gel porosity

Blood Coagulation and Fibrinolysis

Volumn 9, Issue 8, 1998, Pages 733-739

  Marchi, R ^a   Lundberg, U ^a   De Bosch, N B ^b   Arocha Piñango, Carmen Luisa ^a  

^a INSTITUTO VENEZOLANO DE INVESTIGACIONES CIENTÍFICAS   (Venezuela)

^b Banco Metropolitano de Sangre del Distrito Capital   (Venezuela)

Author keywords

Bleeding diathesis; Dysfibrinogenemia; Electron microscopy; Permeability; Turbidity

Indexed keywords

FIBRIN; FIBRINOGEN;

ARTICLE; BLEEDING TENDENCY; CASE REPORT; CONTROLLED STUDY; DYSFIBRINOGENEMIA; FEMALE; FIBRIN FORMATION; GENE MUTATION; HUMAN; PERMEABILITY; PRIORITY JOURNAL; TRANSMISSION ELECTRON MICROSCOPY; TURBIDITY;

EID: 0032447954     PISSN: 09575235     EISSN: None     Source Type: Journal    
DOI: 10.1097/00001721-199811000-00002     Document Type: Article

References (54)

1. Henschen A, Kehl M, Southan C. Genetically abnormal fibrinogens. Some current characterisation strategies. In: Haverkate F, Nieuwenhuizen W, Henschen A, Straub PW (editors): Fibrinogen structure. Functional aspects. Metabolism. Berlin, New York: Walter de Gruyter; 1983. pp. 125-144.
2. Soria J, Mirshahi MC, Collet JP, Vasse M, Caen JP, Soria C. Dysfibrinogénémies. In: Sampol J, Arnoux D, B. Boutiere B (editors): Manuel d'hemostase. Amsterdam: Elsevier; 1995. pp. 489-505.
3. Arocha-Piñango CL, Marchi R, Caires-Tronchoni D. Dysfibrinogenemias. A puzzle. A critical review. Rev Iberoamer Tromb Hemostasia 1990; 3: 75-94.
4. Koopman J, Haverkate F. Hereditary variants of human fibrinogens. In: Bloom AL, Forbes CD, Thomas DP, Tuddenham EGD (editors): Haemostasis and thrombosis. London: Churchill Livingstone; 1994. pp. 515-529.
5. Blombäck M, Blombäck B, Mammen EF, Prasad AS. Fibrinogen Detroit - a molecular defect in the N-terminal disulphide knot of human fibrinogen. Nature 1968; 218: 134-137.
6. Samama MM, Haverkate F. Hereditary dysfibrinogenemia, afibrinogenemia, hypofibrinogenemia and thrombosis. In: Segatchian MJ, Samama MM, Hecker SP (editors): Hypercoagulable states. Fundamental aspects, acquired disorders and congenital thrombopbilia. Boca Raton, Florida: CRC Press Inc.; 1996. pp. 379-383.
7. Koopman J, Haverkate F, Grimbergen J, Lord ST, Mosesson M, Diorio JP, et al. Molecular basis for fibrinogen Dusart (Aα554Arg→Cys) and its association with abnormal fibrin polymerization and thrombophilia. J Clin Invest 1993; 91: 1637-1643.
8. Collet JP, Soria J, Mirshahi M, Hirsch M, Dagonnet FB, Caen J, et al. Dusart syndrome: a new concept of the relationship between fibrin clot degradability: hypofibrinolysis related to an abnormal clot structure. Blood 1993; 82: 2462-2469.
9. Siebenlist KR, Mosesson MW, Diorio JP, Soria J, Soria C, Caen JP. The polymerization of fibrinogen Dusart (Aα554Arg→Cys after removal of carboxy terminal regions of the A-chains). Blood Coag Fibrinol 1993; 4: 61-65.
10. Collet JP, Woodhead JL, Soria J, Soria C, Mirshali M, Caen JP, et al. Fibrinogen Dusart: electron microscopy of molecules, fibres and clots, and viscoelastic properties of clots. Biophys J 1996; 70: 500-510.
11. Wada Y, Lord ST. A correlation between thrombotic disease and a specific fibrinogen abnormality (Aα554Arg→Cys) in two unrelated kindred Dusart and Chapel Hill III. Blood 1994; 84: 3709-3714.
12. Blombäck B, Banerjee D, Carlsson K, Hamsten A, Hessel B, Procyk R, et al. Native fibrin gel networks and factors influencing their formation in health and disease. In: Liu CY, Chien S (editors): Fibrinogen, thrombosis, coagulation, and fibrinolysis. New York: Plenum Press; 1990. pp. 1-23.
13. Hessel B, Silveira AMV, Carlsson K, Oksa H, Rasi V, Vahtera E, et al. Fibrinogenemia Tampere - a dysfibrinogenemia with defective gelation and thromboembolic disease. Thromb Res 1995; 78: 323-339.
14. Blombäck B. Fibrinogen and fibrin-proteins with complex roles in hemostasis and thrombosis. Thromb Res 1996; 83: 1-75.
15. Carr ME, Qureshi GD. The impact of delayed fibrinopeptide A release on fibrin structure. Studies of an abnormal fibrinogen. J Biol Chem 1987; 262: 15568-15574.
16. Bosch NB, Arocha-Pinango CL, Soria, J, Soria, C, Rodriguez A, Rodriguez S. An abnormal fibrinogen in a Venezuelan family. Thromb Res 1977; 1: 253-265.
17. Kazal LA, Amsel S, Miller OP, Tocantins LM. Preparation and some properties of fibrinogen precipirated from human plasma by glycine. Proc Soc Exp Biol Med 1963; 113: 989-944.
18. Blombäck B, Carlsson K, Hessel B, Liljeborg A, Procyk R, Aslund N. Native fibrin gel networks observed by 3D microscopy, permeation and turbidity. Biochim Biophys Acta 1989; 997: 96-110.
19. Blombäck B, Blombäck M. Purification of human and bovine fibrinogen. Arkiv för Kemi 1956; 10: 415-443.
20. Carr ME, Hermans J. Size and density of fibrin fibers from turbidity. Macromolecules 1978; 11: 46-50.
21. Carr ME Jr, Shen LE, Hermans J. Mass-length ratio of fibrin fibers from gel permeation and light scattering. Biopolymers 1977; 16: 1-15.
22. Weisel JW. The electron microscope band pattern of human fibrin: various stains, lateral order, and carbohydrate localization. J Ultrastruct Res 1986; 96: 176-188.
23. Gralnick HR. Congenital disorders of fibrinogen. In: Williams WJ, Beutler E, Erslev AJ, Rundles RW (editors): Hematology. New York: McGraw Hill; 1977. pp. 1423-1431.
24. Henschen A, Kehl M, Southan C. Genetically abnormal fibrinogens - strategies for structure elucidation including fibrinopeptide analysis. In: Beck EA, Furlan M (editors): Variants of human fibrinogen. Bern: Hans Huber; 1984. pp. 273-320.
25. Southan C. Molecular and genetic abnormalities of fibrinogen. In: Francis JE (editor). Fibrinogen, fibrin stabilization and fibrinolysis. Chichester: Ellis Horwood, 1988. pp. 65-99.
26. Meh DA, Siebenlist KR, Galanakis DK, Bergtrom G, Mosesson MW. The dimeric A chain composition of dysfibrinogenemic molecules with mutations at Aα 16. Thromb Res 1995; 78: 531-539.
27. Mosesson MW. Fibrinogen and fibrin polymerization: appraisal of the binding events that accompany fibrin generation and fibrin clot assembly. Blood Coag Fibrinol 1997; 8:257-267.
28. Ni F, Konishi V, Bullock LD, Rivetna MN, Scheraga HA. High resolution NMR studies of fibrinogen-like peptides in solution: structural basis for the bleeding disorder caused by a single mutation of Gly(12) to Val(12) in the A chain of human fibrinogen Rouen. Biochemistry 1989; 28: 3106-3119.
29. Wada Y, Niwa K, Maekawa H, Asakura S, Sugo T, Nakanishi M, et al. A new type of congenital dysfibrinogen, fibrinogen Bremen, with and A(Gly-17 to Val substitution associated with hemorrhagic diathesis and delayed wound healing. Thromb Haemost 1993; 70: 397-403.
30. Yoshida N, Okuma M, Hirata H, Matsuda M, Yamazumi K, Asakura S. Fibrinogen Kyoto II, a new congenitally abnormal molecule characterized by the replacement of Aα proline-18 by leucine. Blood 1991; 78:149-153.
31. Dempfle CEH, Henschen A. Fibrinogen Mannheim I. Identification of an Aα 19Arg(Gly substitution in dysfibrinogenemia associated with bleeding tendency. In: Matsuda M, Iwanaga S, Takada A, Henschen A (editors): Fibrinogen 4. Current basic and clinical aspects. Amsterdam: Elsevier Science Publ BV; 1990. pp. 159-166.
32. Brennan SO, Hammonds B, George PM. Aberrant hepatic processing causes removal of activation peptide and primary polymerisation site from fibrinogen Canterbury (Aα20Val→Asp). J Clin Invest 1995; 96: 2854-2858.
33. Blombäck B, Hessel B, Fields R, Procyk R. Fibrinogen Aarhus: an abnormal fibrinogen with Aα 19Arg→Gly substitution. In: Mosesson MW, Amrani DL, Siebenlist KR, DiOrio JP (editors): Fibrinogen 3. Biochemistry, biological functions, gene regulation and expression. Amsterdam: Elsevier; 1988. pp. 263-266.
34. Yamaguchi SI, Sugo T, Hashimoto Y, Kimura K, Okajima K, Matsuda M. Fibrinogen Kumamoto with an Aα Arg-19 to Gly substitution associated clinically with Thrombosis. XIVth International Fibrinogen Workshop. Fibrinolysis 1996; 10: 1-26.
35. Kaudewitz H, Henschen A, Soria C, Soria J, Bertrand O, Heaton D. The molecular defect of the genetically abnormal fibrinogen Christchurch II. In: Müller-Berghaus G, Scheefers-Borchel V, Seymlar E, Henschen A (editors): Fibrinogen and its derivatives. Amsterdam: Elsevier; 1986. pp. 31-36.
36. Yamazumi K, Terukina S, Onohara S, Matsuda M. Normal plasmic cleavage of the γ-chain variant of "fibrinogen Saga" with an Arg-275 to, Matsuda M. Normal plasmic cleavage of the (-chain variant of "fibrinogen Saga" with an Arg-275 to His substitution. Thromb Haemost 1988; 60: 476-480.
37. Okumura N, Furihata K, Terasawa F, Ishikawa S, Ueno I, Katsuyama T. Fibrinogen Matsumoto II: γ308 Asn→Lys (AAT→AAG) mutation. Br J Haematol 1996; 94: 526-528.
38. Yamazumi K, Shimura K, Maekawa H, Murumatsu S, Matsuda M. Delayed intermolecular-chain crosslinking by factor XIIIa in fibrinogen Asahi characterized by a γ-Met 310 to Thr substitution with an N-glycosylated γ-Asn 308. Blood Coag Fibrinol 1990; 1: 557-559.
39. Branson HE. "Dirty" fiber: a theory of the organization of fibrin from fibrinogen. Thromb Haemost 1979; 42: 1378-1387.
40. Budzynski AZ, Marder VJ, Ménaché D, Guillin MC. Defect in the gamma polypeptide chain of a congenital abnormal fibrinogen (Paris I). Nature 1974; 752: 66-68.
41. Mosesson MW, Feldmann G, Menache D. Electron microscopy of fibrin Paris I. Blood 1980; 56: 80-83.
42. Rosenberg JB, Newman PJ, Mosesson MW, Guillin MC, Amrani DL. Paris I dysfibrinogenemia: a point mutation in intron 8 results in the insertion of a 15 amino acid sequence in the fibrinogen γ-chain. Thromb Haemost 1993; 69: 217-220.
43. Liu CY, Walker P, Handly DA. Fibrinogen New York I: the structural, functional and genetic defects and a hypothesis of the role of fibrin in the regulation of coagulation and fibrinolysis. In: Lane DA, Henshen A, Jasani MK (editors): Fibrinogen, fibrin formation and fibrinolysis. Berlin: Walter de Gruyter; 1986. pp. 79-90.
44. Krause WH, Heene DL, Lasch HG. Congenital dysfibrinogenemia (Fibrinogen Giessen). Thromb Diath Haemost 1973; 29: 547-561.
45. Samama M, Soria J, Soria C, Bousser J. Dysfibrinogenemie congenitale et familiale sans tendance hemorrhagique. Nouv Rev Franc doHematol 1969; 9: 817-832.
46. Lane DA, Cuddigan B, Van Ross M, Kakkar VV. Dysfibrinogenemia characterized by abnormal fibrin monomer polymerization and normal fibrinopeptide A release. Br J Haematol 1980; 44: 483-494.
47. Jassen CL, Urecken J. Fibrinogen Amsterdam, another hereditary abnormality of fibrinogen. Br J Haematol 1971; 20: 287-289.
48. Crum ED, Shainoff JR, Graham RC, Ratnoff OD. Fibrinogen Cleveland II: an abnormal fibrinogen with defective fibrinopeptide A release. J Clin Invest 1974; 53: 1308-1319.
49. Beck EA, Shainoff JR, Vogel A, Jackson DP. Functional evaluation of an inherited abnormal fibrinogen: fibrinogen Baltimore. J Clin Invest 1971; 50: 1874-1884.
50. Maekawa H, Yamazumi K, Muramatsu S, Kaneko M, Hirata H, Takahashi N, et al. An A Ser-434 to N-glycosylated Asn substitution in a dysfibrinogen, fibrinogen Caracas II, characterized by impaired fibrin gel formation. J Biol Chem 1991; 266: 11575-11581.
51. Woodhead JL, Nagaswami C, Matsuda M, ArochaPiñango CL, Weisel JW. The ultrastructure of fibrinogen Caracas II molecules, fibers and clots. J Biol Chem 1996; 271: 4946-4953.
52. Webb CD. Fibrinogen Caracas II molecules, fibers and clots. J Biol Chem 1996; 271: 4946-4953.
53. Webb CD, Hantgan RR, Byeff PD, Owen J. Fibrinogen New Britain: characterization of an Aα Arg 16→His variant human fibrinogen. Blood Coag Fibrinol 1994; 5: 233-238.
54. Baradet TC, Haselgrove JC, Weisel JW. Three-dimensional reconstruction of fibrin clot networks from stereoscopic intermediate voltage electron microscope images and analysis of branching. Biophys J 1995; 68: 1551-1560.