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Thromb Haemost 1996; 75(06): 887-891
DOI: 10.1055/s-0038-1650389
Scientific and Standardization Committee Communications
Schattauer GmbH Stuttgart

Fibrinogen Matsumoto I: A γ364 Asp → His (GAT→CAT) Substitution Associated with Defective Fibrin Polymerization

Nobuo Okumura
1   The Division of Clinical Chemistry and Medical Technology, School of Allied Medical Sciences, Shinshu University, Matsumoto, Nagano, Japan
,
Kenichi Furihata
2   The Dept. of Laboratory Medicine, Shinshu University School of Medicine, Matsumoto, Nagano, Japan
,
Fumiko Terasawa
1   The Division of Clinical Chemistry and Medical Technology, School of Allied Medical Sciences, Shinshu University, Matsumoto, Nagano, Japan
,
Ritsuko Nakagoshi
3   Central Clinical Laboratory, Shinshu University Hospital, Matsumoto, Nagano, Japan
,
Ichiro Ueno
3   Central Clinical Laboratory, Shinshu University Hospital, Matsumoto, Nagano, Japan
,
Tsutomu Katsuyama
2   The Dept. of Laboratory Medicine, Shinshu University School of Medicine, Matsumoto, Nagano, Japan
› Author Affiliations
Further Information

Publication History

Received 30 August 1995

Accepted after resubmission 21 February 1996

Publication Date:
11 July 2018 (online)

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Summary

Fibrinogen Matsumoto I is a novel hereditary dysfibrinogen identified in a 1-year-old boy with Down’s syndrome. Though he showed no apparent bleeding or thrombotic tendency, he had a congenital heart disease. Preoperative coagulation tests of his plasma revealed a prolonged thrombin time and the fibrinogen level determined by the thrombin time method was markedly decreased. Molecular weight of fibrinogen chains showed apparently normal Aα, Bβ-, and γ-chains. The rate of fibrinopeptide release was normal, whereas fibrin polymerization was delayed. Fibrinogen γ-chain gene fragments from the propositus were amplified by polymerase chain reaction then sequenced. The triplet GAT, coding for the amino acid residue γ364, was replaced by CAT, resulting in the substitution of Asp→His. This residue is adjacent to the Tyr-363 that is demonstrated to be the primary site for fibrin polymerization. Our results indicate that the residue γ364 Asp is essential for normal polymerization of fibrin monomer.

 

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