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Related Experiment Videos

Plasmin-platelet interaction involves cleavage of functional thrombin receptor

M Kimura1, T T Andersen, J W Fenton

  • 1Hypertension Research Center, University of Medicine and Dentistry of New Jersey, New Jersey Medical School, Newark 07103-2714, USA.

The American Journal of Physiology
|July 11, 1996
PubMed
Summary

Plasmin inhibits thrombin-induced platelet activation by cleaving the thrombin receptor. However, plasmin

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Area of Science:

  • Biochemistry
  • Hematology
  • Molecular Biology

Background:

  • Platelet activation is crucial for hemostasis and thrombosis.
  • Thrombin receptor (TR) activation initiates platelet signaling.
  • Plasmin's role in modulating TR-mediated platelet activation requires clarification.

Purpose of the Study:

  • To investigate if plasmin inhibits thrombin-induced platelet activation via enzymatic cleavage of the thrombin receptor.
  • To elucidate the mechanism of plasmin's effect on platelet activation.

Main Methods:

  • Monitoring anti-thrombin receptor antibody [anti-TR-(34-46)] binding to platelets.
  • Assessing cleavage of synthetic thrombin receptor peptides by plasmin and thrombin.
  • Measuring cytosolic Ca2+ responses induced by thrombin, TR peptides, and plasmin.

Related Experiment Videos

  • Utilizing anti-TR-(1-160) antibody to block TR signaling.

    • Main Results:

    • Plasmin inhibited anti-TR-(34-46) binding to platelets in a dose- and time-dependent manner, indicating TR cleavage.
    • Both thrombin and plasmin cleaved a synthetic TR peptide (40-55) to generate an active form (SFLLRNPNDKYEPF).
    • Plasmin-induced platelet Ca2+ responses were not abolished by an antibody blocking TR signaling, suggesting a non-TR tethered peptide mechanism.

    Conclusions:

    • Plasmin inhibits thrombin-evoked platelet activation by enzymatically cleaving the thrombin receptor.
    • The mechanism of plasmin-induced platelet Ca2+ response is independent of thrombin receptor tethered peptide generation.