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Related Experiment Videos

Plasma contact activation: a revised hypothesis

A H Schmaier1

  • 1Department of Internal Medicine and Pathology, University of Michigan, Ann Arbor 48109-0640, USA. aschmaie@umich.edu

Biological Research
|November 27, 1998
PubMed
Summary
This summary is machine-generated.

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A novel hypothesis explains plasma kallikrein/kinin system activation on endothelial cells, independent of factor XIIa. This process releases bradykinin, enhancing fibrinolysis and contributing to anticoagulation.

Area of Science:

  • Biochemistry
  • Physiology
  • Molecular Biology

Background:

  • The contact system of plasma proteolysis, including the plasma kallikrein/kinin system, plays a crucial role in physiological processes.
  • Endothelial cells possess a multiprotein receptor for kininogens, involving cytokeratin 1, urokinase plasminogen activator receptor, and gC1qR.

Purpose of the Study:

  • To present a new hypothesis for the activation of the plasma kallikrein/kinin system on endothelial cells.
  • To elucidate the physiological consequences of this activation pathway.

Main Methods:

  • Investigated the assembly of contact proteins (high molecular weight kininogen and prekallikrein) on endothelial cell kininogen receptors.
  • Examined the expression of endothelial cell membrane cysteine protease for prekallikrein activation.

Related Experiment Videos

  • Assessed the effects of kallikrein formation on bradykinin liberation, tissue-type plasminogen activator release, and pro-urokinase activation.

    • Main Results:

    • Prekallikrein activation on endothelial cells occurs independently of factor XIIa.
    • Activated kallikrein cleaves high molecular weight kininogen, releasing bradykinin, which stimulates tissue-type plasminogen activator release.
    • Kininogens contribute to anticoagulation by inhibiting calpain, blocking thrombin binding to platelet receptors, and preventing thrombin-mediated cleavage of protease activated receptor 1.

    Conclusions:

    • A novel biologic system for plasma kallikrein/kinin system activation on endothelial cells has been identified.
    • This activation pathway leads to enhanced cellular fibrinolysis and contributes to the anticoagulant properties of the intravascular compartment.
    • The findings provide a comprehensive understanding of the contact system's activation and its physiological implications.