Binding of Human Tissue Plasminogen Activator (t-PA) to Blood Clots and Clot-Lytic Activity of Clot-Bound t-PA

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The binding affinity ; incorporation and adsorption, of human tissue plasminogen activator (t-PA) and urokinase plasminogen activator (u-PA) for blood clots was investigated in vitro. In order to study the incorporation, the blood clot formation was performed after mixing [^<125>I] t-PA or [^<125>I] u-PA with the blood obtained from human and several animal species. The radioactivities of [^<125>I] t-PA incorporated in blood clots of human, dog, rat and rabbit were higher than those of [^<125>I] u-PA. The adsorption study was carried out by immersing the blood clot in saline containing the [^<125>I] plasminogen activators (PAs). The adsorptions of [^<125>I] t-PA to blood clots of human and animals were higher than those of [^<125>I] u-PA. The results suggest that t-PA has a much higher affinity for fibrin in blood clots than u-PA. The blood clot lysis caused by the clot-bound PAs was investigated using the [^<125>I] fibrincontaining blood clots pretreated with t-PA or u-PA. In the human blood clot, the clot-bound t-PA showed a dose-dependent clot lysis at the concentrations of t-PA ranging from 0.3 to 3 nM, while the clot-bound u-PA has little clot-lytic activity. The t-PA bound to the human blood clot showed the most effective clot lysis as compared with those bound to the animal blood clots.
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