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Complement System01:27

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The complement system is a group of approximately 20 plasma proteins that strengthen the body's defenses against infections through opsonization, inflammation, and cell lysis. Opsonization involves coating pathogens with complement proteins, making them more recognizable and facilitating phagocyte engulfment. Certain complement proteins induce inflammation that attracts immune cells to the site of infection. Cell lysis involves the destruction of pathogens through the formation of a...
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Updated: Mar 25, 2026

High-resolution Melting PCR for Complement Receptor 1 Length Polymorphism Genotyping: An Innovative Tool for Alzheimer's Disease Gene Susceptibility Assessment
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Collectin CL-P1 utilizes C-reactive protein for complement activation.

Nitai Roy1, Katsuki Ohtani1, Yasuyuki Matsuda1

  • 1Department of Microbiology & Immunochemistry, Asahikawa Medical University, Asahikawa 078-8510, Japan.

Biochimica Et Biophysica Acta
|March 1, 2016
PubMed
Summary

Collectin placenta-1 (CL-P1) interacts with C-reactive protein (CRP) to activate complement pathways. This interaction involves complement factor H (CFH), potentially preventing self-tissue damage during immune responses.

Keywords:
Classical pathwayCollectinComplementPentraxinScavenger receptor

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Area of Science:

  • Immunology
  • Complement System
  • Molecular Interactions

Background:

  • C-reactive protein (CRP) is induced during infection and injury, activating innate immunity.
  • CRP activates complement pathways via C1q, but other lectins' roles and downstream effects are unclear.
  • LOX-1 interacts with CRP to activate complement, but involvement of other scavenger receptors (SRs) is unknown.

Purpose of the Study:

  • Investigate the role of collectin placenta-1 (CL-P1) in CRP-mediated complement activation.
  • Determine the downstream effects of CL-P1 and CRP interaction on complement pathways.
  • Explore the involvement of complement regulatory proteins in this interaction.

Main Methods:

  • Utilized CHO/ldlA7 cells expressing CL-P1 to study CRP interaction.
  • Employed ELISA to assess protein binding between CRP and CL-P1.
  • Measured C3 fragment deposition and terminal complement complex (TCC) formation on HEK293 cells expressing CL-P1.

Main Results:

  • CL-P1 binds CRP in a charge-dependent manner.
  • CRP-CL-P1 interaction activates the classical complement pathway via C1q and an amplification pathway via properdin.
  • CRP recruits complement factor H (CFH) to CL-P1 expressing cells, inhibiting TCC formation.

Conclusions:

  • CL-P1 interaction with CFH is crucial for preventing self-tissue damage.
  • This interaction regulates complement activation initiated by CL-P1 and CRP.
  • Highlights a regulatory mechanism in CRP-induced complement activation.