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Effects of Structural Modifications on the Properties of Tissue Plasminogen Activator (tPA)

  • Per Wallén
  • Xiang-Fei Cheng
  • Per-Ingvar Ohlsson
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 281)

Abstract

Physiological fibrinolysis is a proteolytic degradation of polymerized fibrin. A particular fibrinolytic enzyme system is present in blood. The central reaction in this system is the activation of a proenzyme, plasminogen, to the proteolytic enzyme plasmin. The activation is triggered by highly specialized proteases, plasminogen activators. One of these, the tissue plasminogen activator (tPA), is synthesized by endothelial cells and excreted to the blood on certain stimuli. Properties, which distinguish tPA from other types of plasminogen activators are a high affinity to fibrin and the very strong stimulation exerted by fibrin on tPA induced activation (2–3 orders of magnitude). These properties have evoked the idea of an efficient ternary activation complex between tPA, plasminogen and fibrin. The work on the isolation of tPA, the determination of its primary structure and gene structure as well as elucidation of its physicochemical properties has been performed by a large number of scientists. Several reviews have been published (e.g. Collen 1980; Rånby and Wallén 1985; Danö et al. 1985; Erickson et al. 1985; Wallén 1987). Fig. 1 shows the now well established primary structure* of wild tPA.

Keywords

Plasminogen Activator Tissue Plasminogen Activator Plasminogen Activation Plasminogen Activator Activity Type Plasminogen Activator 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Springer Science+Business Media New York 1990

Authors and Affiliations

  • Per Wallén
    • 1
  • Xiang-Fei Cheng
    • 1
  • Per-Ingvar Ohlsson
    • 1
  1. 1.Department of Medical Biochemistry and BiophysicsUniversity of UmeåUmeåSweden

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