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Related Experiment Videos

Human kininogens regulate thrombin binding to platelets through the glycoprotein Ib-IX-V complex

H N Bradford1, R A Dela Cadena, S P Kunapuli

  • 1The Sol Sherry Thrombosis Research Center and Department of Medicine, Temple University School of Medicine, Philadelphia, PA 19140, USA.

Blood
|August 15, 1997
PubMed
Summary

Kininogens regulate platelet aggregation by binding to the glycoprotein Ib-IX-V complex, inhibiting thrombin

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Area of Science:

  • Biochemistry
  • Hematology
  • Molecular Biology

Background:

  • High and low molecular mass kininogens inhibit thrombin-induced platelet aggregation.
  • The inhibitory mechanism involves the heavy chain, specifically a heptapeptide sequence (L271-A277).
  • Thrombin binds to platelet receptors glycoprotein (GP) Ib-IX-V and a G protein-coupled receptor.

Purpose of the Study:

  • To elucidate the molecular mechanism by which kininogens inhibit thrombin-induced platelet aggregation.
  • To determine the specific platelet receptor involved in kininogen's inhibitory action.

Main Methods:

  • Studied thrombin-induced aggregation of Bernard-Soulier platelets (lacking GP Ib-IX-V).
  • Investigated the effect of recombinant K270-G292 polypeptide and synthetic peptide L271-A277 on thrombin binding.

Related Experiment Videos

  • Utilized monoclonal antibodies (TM-60, SZ 2) against GP Ib-IX-V to assess kininogen-receptor interactions.
  • Examined kininogen's effect on biotinylated thrombin binding to transfected cells expressing GP Ib-IX-V.

    • Main Results:

    • Kininogen failed to inhibit aggregation in Bernard-Soulier platelets, indicating interaction with the GP Ib-IX-V complex.
    • Kininogen and its derived peptides reduced thrombin binding to platelets, similar to GP Ib-IX ligands.
    • Antibodies to GP Ib-IX-V inhibited kininogen binding, and kininogen blocked antibody binding.
    • Kininogen inhibited thrombin binding to GP Ib-IX-V expressed on fibroblasts.

    Conclusions:

    • Kininogen binds to the glycoprotein Ib-IX-V complex on platelets.
    • This interaction modulates thrombin binding and subsequent platelet aggregation.
    • Kininogen acts as a regulator of early platelet stimulation by thrombin.