Fibrinogen Matsumoto V: a Variant with Aα19 Arg → Gly (AGG → GGG)

Hitoshi Tanaka; Fumiko Terasawa; Toshiro Ito; Shin-ichi Tokunaga; Fumihiro Ishida; Kiyoshi Kitano; Kendo Kiyosawa; Nobuo Okumura

doi:10.1055/s-0037-1612912

Thrombosis and Haemostasis, Inhaltsverzeichnis

Thromb Haemost 2001; 85(01): 108-113
DOI: 10.1055/s-0037-1612912

Review Article

Schattauer GmbH

Fibrinogen Matsumoto V: a Variant with Aα19 Arg → Gly (AGG → GGG)

Comparison between Fibrin Polymerization Stimulated by Thrombin or Reptilase and Fibrin Monomer Polymerization

Autor*innen

Hitoshi Tanaka

¹Second Department of Internal Medicine, Shinshu University School of Medicine, Nagano, Nagano, Japan
Fumiko Terasawa

²Laboratory of Clinical Chemistry, Department of Medical Technology, School of Allied Medical Sciences, Shinshu University, Matsumoto, Nagano, Japan
Toshiro Ito

³Department of Internal Medicine, Nagano Red Cross Hospital, Nagano, Nagano, Japan
Shin-ichi Tokunaga

³Department of Internal Medicine, Nagano Red Cross Hospital, Nagano, Nagano, Japan
Fumihiro Ishida

¹Second Department of Internal Medicine, Shinshu University School of Medicine, Nagano, Nagano, Japan
Kiyoshi Kitano

¹Second Department of Internal Medicine, Shinshu University School of Medicine, Nagano, Nagano, Japan
Kendo Kiyosawa

¹Second Department of Internal Medicine, Shinshu University School of Medicine, Nagano, Nagano, Japan
Nobuo Okumura

²Laboratory of Clinical Chemistry, Department of Medical Technology, School of Allied Medical Sciences, Shinshu University, Matsumoto, Nagano, Japan

Abstract

Summary

Fibrinogen Matsumoto V (M-V) is a dysfibrinogen identified in a 52-year-old woman with systemic lupus erythematous. The triplet AGG encoding the amino acid residue Aα19 was replaced by GGG, resulting in the substitution of Arg→Gly. Residue Aα19 has been shown to be one of the most important amino acids in the so-called ‘A’ site or α-chain knob. The thrombin-catalyzed release of fibrinopeptide A from M-V fibrinogen was only slightly delayed yet release of fibrinopeptide B was significantly delayed. Both thrombin-catalyzed fibrin polymerization and fibrin monomer polymerization were markedly impaired compared to normal fibrinogen. In addition, reptilase-catalyzed fibrin polymerization of M-V was much more impaired than thrombin-catalyzed fibrin polymerization. These results indicate ‘B’ and/or ‘b’ site of M-V fibrinogen play a more important role in thrombin- catalyzed fibrin polymerization than that of normal control fibrinogen.

Keywords

Fibrinogen - dysfibrinogenemia polymerizationion - thrombin - reptilase

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Referenzen

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