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Related Experiment Videos

Sublytic complement attack exposes C-reactive protein binding sites on cell membranes

Y P Li1, C Mold, T W Du Clos

  • 1Department of Microbiology, University of New Mexico School of Medicine, Albuquerque 87131.

Journal of Immunology (Baltimore, Md. : 1950)
|March 15, 1994
PubMed
Summary

C-reactive protein (CRP) binds to complement-damaged cell membranes, specifically to exposed phospholipids, which aids in clearing damaged cells during inflammation. This binding is calcium-dependent and inhibited by phosphocholine.

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Area of Science:

  • Immunology
  • Biochemistry

Background:

  • C-reactive protein (CRP) is an acute phase protein involved in inflammation.
  • CRP's binding ligands at inflammatory sites are not fully understood.
  • Complement activation causes cell membrane damage and inflammation.

Purpose of the Study:

  • To investigate the binding of CRP to complement-damaged cell membranes.
  • To identify the specific components on damaged cell membranes that CRP binds to.

Main Methods:

  • Raji cells were treated with human serum to activate the complement system.
  • CRP binding was assessed under various conditions, including calcium dependence and phosphocholine inhibition.
  • Complement components (C3, C5, C8, C9) were depleted from serum to determine their role in CRP binding.

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  • Complement-treated liposomes were used to further investigate binding sites.

    • Main Results:

    • CRP binding to complement-treated Raji cells was calcium-dependent and inhibited by phosphocholine.
    • CRP binding required complement activation, specifically deposition of C3b and MAC, and disruption of the lipid bilayer.
    • Depletion of C3, C5, or C8 eliminated CRP binding, while C9 depletion reduced it.
    • CRP binding to complement-treated liposomes indicated phosphatidylcholine as a key binding site.

    Conclusions:

    • CRP binding to damaged cell membranes is mediated by exposed phospholipids, not MAC proteins.
    • Complement-mediated disruption of the cell membrane is essential for CRP binding.
    • This mechanism supports CRP's role in clearing damaged cells at inflammatory sites.