Specific fibrinolytic properties of different molecular forms of pro-urokinase from a monkey kidney cell culture

D.C. Rijken, D.J. Binnema, P. Los

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

The specific fibrinolytic properties of both high molecular weight (55 kd) and low molecular weight (30 kd) pro-urokinase from a monkey kidney cell culture were evaluated in a plasma clot lysis system and compared with those of human urokinase. The system was composed of a radiolabelled plasma clot immersed in plasma containing the fibrinolytic agent. On unit base, 55 kd pro-urokinase was approximately 1.5 times more effective in lysing the clot than 30 kd pro-urokinase and equally effective as urokinase. In contrast to urokinase, both pro-urokinase forms induced clot lysis without degrading fibrinogen in the surrounding plasma. However, a considerable activation of the fibrinolytic system in the plasma occurred as a large amount of alpha 2-antiplasmin was consumed, indicating that pro-urokinase was not fully fibrin-specific. Quenching antibodies against tissue-type plasminogen activator (t-PA) added to the plasma clot lysis system retarded but did not prevent pro-urokinase-induced clot lysis. This indicated that not only was t-PA in plasma involved in the activation of pro-urokinase (probably via plasmin), but that an additional mechanism also existed.

Original languageEnglish
Pages (from-to)761-768
JournalThrombosis and haemostasis
Volume42
Issue number6
DOIs
Publication statusPublished - 15 Jun 1986

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Keywords

  • Animals
  • Enzyme Activation
  • Enzyme Precursors
  • Fibrinogen
  • Fibrinolysin
  • Fibrinolysis
  • In Vitro Techniques
  • Kidney
  • Macaca fascicularis
  • Molecular Weight
  • Plasminogen Activators
  • Substrate Specificity
  • Tissue Plasminogen Activator
  • Urokinase-Type Plasminogen Activator
  • alpha-2-Antiplasmin
  • Journal Article
  • Research Support, Non-U.S. Gov't

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