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Related Experiment Videos

Serum amyloid P component binds to histones and activates the classical complement pathway.

P S Hicks1, L Saunero-Nava, T W Du Clos

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

Journal of Immunology (Baltimore, Md. : 1950)
|December 1, 1992
PubMed
Summary

C-reactive protein (CRP) and serum amyloid P component (SAP) bind to histones and chromatin. Both pentraxins activate the classical complement pathway after binding, revealing shared and distinct interactions.

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Area of Science:

  • Immunology
  • Biochemistry
  • Molecular Biology

Background:

  • Pentraxins like CRP and SAP bind nuclear material, potentially aiding clearance.
  • CRP interacts with chromatin via histones; SAP's histone binding was uncharacterized.
  • Both CRP and SAP can activate the complement system.

Purpose of the Study:

  • To investigate CRP and SAP binding to histones H1 and H2A.
  • To determine complement activation following pentraxin-histone binding.
  • To compare SAP and CRP interactions with chromatin and histones.

Main Methods:

  • Chromatin and histone binding assays for CRP and SAP.
  • Complement activation assays using SAP-depleted serum.
  • Analysis of complement component deposition (C4d, C3).

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Main Results:

  • SAP binds to histones H1, H2A, and chromatin, independent of H1 for chromatin binding.
  • SAP partially inhibits CRP binding to chromatin and H1, but not H2A.
  • Binding of CRP or SAP to H2A activates the classical complement pathway via C1q.

Conclusions:

  • CRP and SAP share binding sites on histones and chromatin.
  • Both pentraxins activate the classical complement pathway upon ligand binding.
  • Distinct binding mechanisms exist for CRP and SAP with chromatin components.