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Thromb Haemost 1987; 57(03): 310-313
DOI: 10.1055/s-0038-1651123
Original Article
Schattauer GmbH Stuttgart

Fibrinogen Haifa: Fibrinogen Variant with Absence of Protective Effect of Calcium on Plasmin Degradation of Gamma Chains

J Soria
*   The Laboratoire Central d’Hématologie et de Biochemie, Hôtel Dieu, Paris, France
,
C Soria
**   The Département d’Hématologie, Hôpital Lariboisière, Paris, France
,
M Samama
*   The Laboratoire Central d’Hématologie et de Biochemie, Hôtel Dieu, Paris, France
,
S Tabori
•   The Department of Haematology, Rambam Medical Center and Techn. Faculty of Medicine, Haifa, Israel
,
M Kehl
***   The Max-Planck-Institut, Martinsried, West-Germany
,
A Henschen
***   The Max-Planck-Institut, Martinsried, West-Germany
,
W Nieuwenhuizen
****   The Gaubius Institute, Leiden, The Netherlands
,
A Rimon
•   The Department of Haematology, Rambam Medical Center and Techn. Faculty of Medicine, Haifa, Israel
,
I Tatarski
•   The Department of Haematology, Rambam Medical Center and Techn. Faculty of Medicine, Haifa, Israel
› Author Affiliations
Further Information

Publication History

Received 12 May 1986

Accepted after revision 23 February 1987

Publication Date:
06 July 2018 (online)

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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.

Keywords

Dysfibrinogenemia - Fibrinogen - Fibrinogen degradation products - Fibrinolysis
 

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