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A Liposome Membrane Permeability Assay for Investigating the Effects of Phosphatidylinositol Phosphate Groups on Membranotropic Action of Venom PLA2
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Polyphosphate binds with high affinity to exosite II of thrombin.

N J Mutch1, T Myles, L L K Leung

  • 1Department of Biochemistry, College of Medicine, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.

Journal of Thrombosis and Haemostasis : JTH
|December 17, 2009
PubMed
Summary

Polyphosphate, released by platelets, binds to thrombin's exosite II. This interaction, with a low dissociation constant, may be significant in blood coagulation.

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Area of Science:

  • Biochemistry
  • Hematology
  • Molecular Biology

Background:

  • Polyphosphate is secreted from platelet dense granules.
  • Polyphosphate accelerates factor V activation by thrombin.

Purpose of the Study:

  • To examine the interaction of polyphosphate with thrombin.

Main Methods:

  • Gel mobility assays to assess polyphosphate-thrombin interaction.
  • Mutagenesis of thrombin exosites.
  • Surface plasmon resonance (SPR) for binding kinetics.
  • Competition assays with glycosaminoglycans.

Main Results:

  • Thrombin binds polyphosphate, primarily through exosite II.
  • SPR revealed a tight interaction (K(d) ≈ 5 nM).
  • Polyphosphate binding partially overlaps with, but is distinct from, the heparin-binding site.

Conclusions:

  • Polyphosphate interacts with thrombin via exosite II.
  • This interaction is likely physiologically relevant due to achievable polyphosphate concentrations in vivo.
  • Polyphosphate does not interfere with heparin's anticoagulant function via antithrombin.