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Related Experiment Videos

The complement fragment C3d facilitates phagocytosis by monocytes.

T A Gaither1, I Vargas, S Inada

  • 1Laboratory of Clinical Investigation, National Institute of Allergy and Infectious Diseases, Nagoya, Japan.

Immunology
|November 1, 1987
PubMed
Summary

Complement receptor 3 (CR3) on human monocytes mediates the binding of C3d-coated targets, enhancing phagocytosis. This receptor, distinct from CR4, plays a key role in immune responses involving complement fragments.

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Area of Science:

  • Immunology
  • Complement system
  • Cell surface receptors

Background:

  • Human monocytes express complement receptors CR1 and CR3, binding C3b and iC3b respectively.
  • A leukocyte receptor, CR4, binds C3dg.
  • Previous studies showed IgM-sensitized sheep erythrocytes coated with C3d (EAC3d) bind to cultured monocytes.

Purpose of the Study:

  • To investigate if C3d-coated target binding leads to phagocytosis by monocytes.
  • To identify the specific monocyte receptor responsible for C3d binding.

Main Methods:

  • Utilized EAC3d to assess binding and phagocytosis with cultured and non-cultured human monocytes.
  • Employed monoclonal antibodies (anti-CR1, anti-CR2, anti-CR3/anti-Mol) and ethylenediamine tetraacetate to identify the C3d receptor.

Related Experiment Videos

  • Quantified C3d/cell required for rosette formation and phagocytosis enhancement.

    • Main Results:

    • Non-cultured monocytes showed enhanced phagocytosis of IgG-coated erythrocytes with <100 C3d/cell.
    • CR3 (anti-Mol antibody) inhibited EAC3d rosettes by approximately 42%.
    • CR3 is metal-dependent, distinguishing it from CR4, and is predominantly responsible for C3d binding to monocytes.

    Conclusions:

    • Monocytes possess a C3d-binding receptor with low affinity for C3d-only coated particles.
    • CR3 is the primary receptor mediating C3d binding and subsequent phagocytosis enhancement in human monocytes.
    • The findings clarify the role of CR3 in complement-mediated immune functions.