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Related Experiment Video

Updated: Jun 28, 2026

An In Vitro Assay to Study Platelet Migration Using RGD-Functionalized Avidin-Biotin Tethers
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Factor H binds to platelet integrin alphaIIbbeta3.

Zakar Mnjoyan1, Jun Li, Vahid Afshar-Kharghan

  • 1MD Anderson Cancer Center, Houston, TX 77030, USA.

Platelets
|November 4, 2008
PubMed
Summary
This summary is machine-generated.

Factor H directly binds to platelet integrin alpha(IIb)beta(3), providing a constant protective presence. Platelet activation increases Factor H binding through other sites, not alpha(IIb)beta(3).

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Published on: October 27, 2009

Area of Science:

  • Immunology
  • Biochemistry

Background:

  • Factor H regulates the alternative complement pathway, protecting cells from damage.
  • Factor H interacts with various cell surface molecules, including integrins.

Purpose of the Study:

  • To investigate the direct binding of Factor H to platelet integrin alpha(IIb)beta(3).
  • To determine if alpha(IIb)beta(3) provides a constitutive presence of Factor H on platelets.

Main Methods:

  • Flow cytometry to measure Factor H binding to platelets and cells expressing alpha(IIb)beta(3).
  • Surface plasmon resonance and ELISA to assess Factor H binding to alpha(IIb)beta(3) in cell-free systems.

Main Results:

  • Factor H directly binds to alpha(IIb)beta(3) with a dissociation constant (Kd) of 131 +/- 60.9 nM.
  • This binding is independent of alpha(IIb)beta(3) active conformation and cations.
  • Platelet activation increases Factor H binding, but not via alpha(IIb)beta(3).

Conclusions:

  • Platelet integrin alpha(IIb)beta(3) serves as a constitutive binding site for Factor H.
  • Factor H's presence on platelets is likely important for complement regulation.
  • Increased Factor H binding upon platelet activation involves other platelet surface molecules.