Antifibrinolytic Role of a Bee Venom Serine Protease Inhibitor That Acts as a Plasmin Inhibitor

被引：67

作者：

Choo, Young Moo ^{[1
]}

Lee, Kwang Sik ^{[1
]}

Yoon, Hyung Joo ^{[2
]}

Qiu, Yuling ^{[1
]}

Wan, Hu ^{[1
]}

Sohn, Mi Ri ^{[1
]}

Sohn, Hung Dae ^{[1
]}

Jin, Byung Rae ^{[1
]}

机构：

[1] Dong A Univ, Coll Nat Resources & Life Sci, Pusan, South Korea

[2] Natl Acad Agr Sci, Dept Agr Biol, Suwon, South Korea

来源：

PLOS ONE | 2012年 / 7卷 / 02期

关键词：

PSEUDONAJA-TEXTILIS; BLOOD-COAGULATION; APROTININ; EVOLUTION; PURIFICATION; HEMOSTASIS; ENZYME;

D O I：

10.1371/journal.pone.0032269

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Bee venom is a rich source of pharmacologically active substances. In this study, we identified a bumblebee (Bombus ignitus) venom Kunitz-type serine protease inhibitor (Bi-KTI) that acts as a plasmin inhibitor. Bi-KTI showed no detectable inhibitory effect on factor Xa, thrombin, or tissue plasminogen activator. In contrast, Bi-KTI strongly inhibited plasmin, indicating that it acts as an antifibrinolytic agent; however, this inhibitory ability was two-fold weaker than that of aprotinin. The fibrin(ogen)olytic activities of B. ignitus venom serine protease (Bi-VSP) and plasmin in the presence of Bi-KTI indicate that Bi-KTI targets plasmin more specifically than Bi-VSP. These findings demonstrate a novel mechanism by which bumblebee venom affects the hemostatic system through the antifibrinolytic activity of Bi-KTI and through Bi-VSP-mediated fibrin(ogen) olytic activities, raising interest in Bi-KTI and Bi-VSP as potential clinical agents.

引用

页数：5

共 25 条

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