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Related Experiment Videos

Heparin modulates integrin function in human platelets.

M Sobel1, W R Fish, N Toma

  • 1Department of Surgery, Section of Vascular Surgery, Syracuse Veterans Affairs Medical Center and Upstate Medical University, State University of New York, USA. Michael.Sobel@med.va.gov

Journal of Vascular Surgery
|March 10, 2001
PubMed
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Heparin directly binds to platelet integrin alpha(IIb)beta(3), increasing fibrinogen binding and causing platelet aggregation. This process involves outside-in signaling, highlighting a direct mechanism for heparin

Area of Science:

  • Hematology
  • Biochemistry
  • Molecular Biology

Background:

  • Heparin is known to interact with human platelets, potentially causing activation and aggregation.
  • The precise mechanisms underlying heparin-induced platelet alterations remain largely unknown.
  • Understanding these mechanisms is crucial for managing heparin's effects in clinical settings.

Purpose of the Study:

  • To identify the specific platelet binding sites for heparin.
  • To elucidate how heparin influences the function of the platelet integrin alpha(IIb)beta(3) (glycoprotein IIb/IIIa).
  • To investigate the signaling pathways involved in heparin-mediated platelet aggregation.

Main Methods:

  • Photoaffinity cross-linking and affinity chromatography were employed to pinpoint heparin-binding proteins on platelet membranes.

Related Experiment Videos

  • A radioligand-binding assay was used to quantify heparin's effect on fibrinogen binding to platelets.
  • Rap2 translocation to the cytoskeleton was measured to assess outside-in signaling during heparin-induced platelet aggregation.

    • Main Results:

    • The integrin alpha(IIb)beta(3) was identified as a direct heparin-binding site on human platelets.
    • Low concentrations of heparin significantly enhanced fibrinogen binding to activated platelets, a process dependent on calcium.
    • Heparin-mediated platelet aggregation was inhibited by GRGDS peptide and EDTA, confirming its dependence on integrin alpha(IIb)beta(3) function and fibrinogen binding.
    • Aggregation was accompanied by Rap2 translocation, indicating activation of outside-in signaling pathways.

    Conclusions:

    • Heparin binds directly to the integrin alpha(IIb)beta(3) on platelets, both in vitro and ex vivo.
    • Heparin enhances fibrinogen binding to this integrin, leading to platelet aggregation.
    • This aggregation process requires an intact integrin and ligand, resulting in Rap2 translocation and outside-in signaling, suggesting direct modulation of integrin function by heparin.