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Enhancement of fibrin binding and activation of plasminogen by staplabin through induction of a conformational change in plasminogen
Author(s) -
Takayasu Ritsuko,
Hasumi Keiji,
Shinohara Chikara,
Endo Akira
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01334-3
Subject(s) - plasmin , chemistry , fibrin , conformational change , fibrinogen , allosteric regulation , plasminogen activator , biochemistry , fibrinolysis , enzyme , biology , immunology , medicine , endocrinology
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.