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[Thrombomodulin: a new proteoglycan. Structure-function relation].

M C Bourin1

  • 1Laboratoire de Biotechnologie des Cellules Eucaryotes, Université Paris Val-de-Marne, Créteil.

Annales De Biologie Clinique
|January 1, 1991
PubMed
Summary

Thrombomodulin (TM) is a proteoglycan that regulates blood clotting. Its protein core activates protein C, while its chondroitin sulfate chain inhibits thrombin, enhancing anticoagulant functions.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Hematology

Context:

  • Endothelial cell surface receptor thrombomodulin (TM) plays a crucial role in regulating coagulation.
  • Previous studies suggested TM possesses anticoagulant functions, acting as a cofactor for protein C activation and inhibiting thrombin.
  • Understanding the specific roles of TM's structural domains is key to elucidating its mechanism of action.

Purpose:

  • To identify and characterize the functional domains of rabbit lung thrombomodulin (TM).
  • To elucidate the mechanism by which TM exerts its anticoagulant functions.
  • To determine the contribution of the polysaccharide chain to TM's biological activities.

Summary:

  • Rabbit lung TM was identified as a chondroitin sulfate proteoglycan.
  • Thrombin binding to TM's protein core is essential for all its activities.
  • The polysaccharide chain is crucial for inhibiting thrombin's procoagulant effects on fibrinogen and Factor V, and enhances thrombin inhibition by antithrombin III.

Impact:

  • Reveals that the chondroitin sulfate chain confers additional anticoagulant activities beyond protein C activation.
  • Establishes TM as a novel proteoglycan with significant regulatory functions in hemostasis.
  • Highlights the dual contribution of both the protein core and polysaccharide chain to TM's anticoagulant properties.

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