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DOI: 10.1055/s-0038-1651123
Fibrinogen Haifa: Fibrinogen Variant with Absence of Protective Effect of Calcium on Plasmin Degradation of Gamma Chains
Publication History
Received 12 May 1986
Accepted after revision 23 February 1987
Publication Date:
06 July 2018 (online)
![](https://www.thieme-connect.de/media/10.1055-s-00035024/198703/lookinside/thumbnails/10-1055-s-0038-1651123-1.jpg)
Summary
The abnormal fibrinogen Haifa is characterized by the fact that calcium present during enzymatic digestion by plasmin does not protect the Haifa D gamma chain against further plasmin attack as it does in normal molecules.
Since calcium binding to fibrinogen, ADP - platelet aggregation cofactor activity and gamma dimerization process induced by factor XIIIa are normal for fibrinogen Haifa, the corresponding sequences in the gamma chain are not involved. It seems rather that the anomaly resides near the gamma 302 plasmin cleavage site that is protected when calcium is bound to the gamma chain and that this affects the availability of the polymerization site located in the C terminal part of the chain.
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References
- 1 Henschen A, Kehl M, Southan C, Lottspeich F, Georgopoulos D. Genetically abnormal fibrinogens, some current characterization strategies. In: Fibrinogen, Structure, Functional Aspects, Metabolism. Haverkate F, Henschen A, Nieuwenhuizen W, Straub PW. (Eds.) Walter de Gruyter; 1983: 125-144
- 2 Blombäck M, Blombäck B, Mammen EF, Prasad AJ. Fibrinogen Detroit. A molecular defect in the N terminal disulphide knot of human fibrinogen?. Nature 1968; 218: 134-137
- 3 Van Ruijven-Vermeer J AM, Nieuwenhuizen W. Purification of rat fibrinogen and its constituent chains. Biochem J 1978; 159: 653-658
- 4 Blombäck B, Blombäck M. Purification of human and bovine fibrinogen. Arkiv for Kem 1956; 10: 415-443
- 5 Caen J, Larrieu MJ, Samama M. In: Hémostase. Méthodes d’exploration et Diagnostic pratique. Masson Ed; Paris: 1975
- 6 Bouvier CA, Gruedlinger J. Etude des phénomènes de coagulation et de fibrinolyse par une méthode d’enregistrement optique. Schweiz Med Wochenschr 1960; 93: 1401-1455
- 7 Merskey C, Lalezari P, Johnson A. A rapid simple sensitive method for measuring fibrinolytic split products. Soc Exp Biol (NY) 1969; 131: 871-877
- 8 Soria J, Soria C, Samama M, Girard ML. Troubles de la fibrinoformation. Technique d’appréciation du premier stade. Pathol Biol 1972; 20: 315-321
- 9 Belitser VN, Varetsnaja JV, Malvena EV. Fibrinogen-fibrin interaction. Biochim Biophys Acta 1968; 154: 367-375
- 10 Schwarz ML, Pizzo SV, Hill AL, McKee P. The effect of fibrin stabilizing factor on the sub-units structure of human fibrin. J Clin Invest 1971; 50: 1506-1513
- 11 Patscheke H, Worner P. Platelet activation detected by turbidimetric shape-change analysis. Thromb Res 1978; 12: 485-496
- 12 Soria J, Soria C, Boulard C. Anomalie de structure du fibrinogène Metz locaüsée sur la chaine A alpha de la molécule. Biochimie 1972; 54: 415-417
- 13 Haverkate F, Timan G. Protective effect of calcium in the plasmin degradation of fibrinogen and fibrin fragment D. Thromb Res 1977; 10: 803-812
- 14 Warren L. The thiobarbituric acid assay of sialic acid. J Biol Chem 1959; 234: 1971-1975
- 15 Mester L, Szabados L. Differences constitutionnelles entre les fragments glucidiques du fibrinogène humain normal et du fibrinogène anormal. C R Acad Sc Paris 1968; 266: 34-36
- 16 Roka L, Rademacher FG. Binding of the thrombin to fibrin. VIIth International Congress on Thrombosis and Haemostasis. London: 1979. p 123 abstract 294
- 17 Marguerie G, Chagniel G, Suscillon M. The binding of calcium to bovine fibrinogen Biochim. Biophys Acta 1977; 490: 94-103
- 18 Brook JG, Tabori S, Tatarsky I, Hashmonai M, Schramek A. Fibrinogen Haifa. A new variant. A case report. Haemostasis 1983; 13: 277-281
- 19 Nieuwenhuizen W, Van Ruijven-Vermeer JA, Nodijen WJ, Vermomd A. Recalculation of calcium-binding properties of human and rat fibrin(ogen) and their degradation products. Thromb Res 1981; 22: 653-657
- 20 Henschen A. On the structure of functional sites in fibrinogen. Thromb Res 1983; supplt V: 27-39
- 21 Henschen A, Lottspeich F, Kehl M, Southan C. Covalent structure of fibrinogen. Ann NY Acad Sc 1983; 408: 521-535
- 22 Hawiger J, Kloczewiak M, Timmons S. Interaction of fibrinogen with staphylococcal clumping factor and with platelets. Molecular biology of fibrinogen and fibrin. Ann NY Acad Sc 1983; 408: 521-535
- 23 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 gamma chain. Biochemistry 1984; 23: 1767-1774
- 24 Chen R, Doolittle FR. Gamma gamma cross-linking sites in human and bovine fibrin. Biochemistry 1971; 10: 44-91
- 25 Budzynski AZ, Olexa SA, Pandya BV. Fibrin polymerization sites in fibrinogen and fibrin fragments. Ann NY Acad Sc 1983; 4085: 301-314
- 26 Horwitz BH, Varadi A, Scheraga HA. Localization of a fibrin gamma chain polymerization site within segment Thr 374 to Glu 396 of human fibrinogen. Proc Natl Acad Sc 1984; 81: 5980-5984
- 27 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: 1034-1041
- 28 Liu CY, Nossel H, Kaplan K. The binding of thrombin by fibrin. J Biol Chem 1979; 254: 1042-1045