Enhancement of fibrin binding and activation of plasminogen by staplabin through induction of a conformational change in plasminogen

FEBS Letters

Hasumi, Keiji¹  Endo, Akira¹  Takayasu, Ritsuko¹  Shinohara, Chikara¹ 

[1]Department of Applied Biological Science, Tokyo Noko University, 3-5-8 Saiwaicho, Fuchu, Tokyo 183, Japan

关键词: Plasminogen activation;    Plasminogen binding;    Conformational change;    Plg;    plasminogen;    EACA;    ϵ-aminocaproic acid;    NTP;    NH2-terminal peptide;    u-PA;    urokinase-type plasminogen activator;    t-PA;    tissue-type plasminogen activator;    pNA;    p-nitroaniline;    CNBr-Fbg;    CNBr fragment of fibrinogen;    PAGE;    polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(97)01334-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Staplabin (0.3–0.6 mM), a fungal triprenyl phenol, enhanced 3–6-fold the plasminogen activator-catalyzed activation of Glu-plasminogen and Lys-plasminogen as well as their binding to fibrin. Staplabin was not stimulatory to the amidolytic activity of plasmin and plasminogen activators. Even in the presence of ϵ-aminocaproic acid (EACA) and fibrinogen fragments, allosteric effectors for Glu-plasminogen, staplabin increased the activation of both forms of plasminogen. In size-exclusion chromatography of Glu-plasminogen and Lys-plasminogen, the molecular elution time, which varies as the conformation of a protein changes, was shortened by staplabin. These results suggest that staplabin causes plasminogens to be more susceptible to activation and fibrin binding by inducing a conformational change that is, at least in part, different from that induced by EACA and fibrinogen fragments.

【 授权许可】

Unknown