纤维蛋白原松本V：一种Aα19位精氨酸突变为甘氨酸（AGG→GGG）的变体。凝血酶或蛇毒凝血酶刺激的纤维蛋白聚合与纤维蛋白单体聚合的比较。

Fibrinogen Matsumoto V: a variant with Aalpha19 Arg-->Gly (AGG-->GGG). Comparison between fibrin polymerization stimulated by thrombin or reptilase and fibrin monomer polymerization.

作者信息

Tanaka H, Terasawa F, Ito T, Tokunaga S, Ishida F, Kitano K, Kiyosawa K, Okumura N

机构信息

Second Department of Internal Medicine, Shinshu University School of Medicine, Matsumoto, Nagano, Japan.

出版信息

Thromb Haemost. 2001 Jan;85(1):108-13.

PMID:11204560

Abstract

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 Aalpha19 was replaced by GGG, resulting in the substitution of Arg-->Gly. Residue Aalpha19 has been shown to be one of the most important amino acids in the so-called 'A' site or alpha-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.

摘要

纤维蛋白原松本V型（M-V）是在一名患有系统性红斑狼疮的52岁女性中发现的一种异常纤维蛋白原。编码氨基酸残基Aα19的三联体AGG被GGG取代，导致精氨酸被甘氨酸替代。已证明残基Aα19是所谓“A”位点或α链钮中最重要的氨基酸之一。凝血酶催化从M-V纤维蛋白原释放纤维蛋白肽A仅略有延迟，但纤维蛋白肽B的释放则明显延迟。与正常纤维蛋白原相比，凝血酶催化的纤维蛋白聚合和纤维蛋白单体聚合均明显受损。此外，蛇毒凝血酶催化的M-V纤维蛋白聚合比凝血酶催化的纤维蛋白聚合受损更严重。这些结果表明，M-V纤维蛋白原的“B”和/或“b”位点在凝血酶催化的纤维蛋白聚合中比正常对照纤维蛋白原发挥更重要的作用。