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Complement System

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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 membrane...

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Related Experiment Video

Updated: Jun 2, 2026

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion

Published on: June 15, 2019

Enzymatically modified low-density lipoprotein is recognized by c1q and activates the classical complement pathway.

Gérard J Arlaud¹, Adrienn Biro, Wai Li Ling

¹Laboratoire d'Enzymologie Moléculaire, Institut de Biologie Structurale Jean-Pierre Ebel, 41 rue Jules Horowitz, 38027 Grenoble Cedex 1, France.

Journal of Lipids

|April 15, 2011

Summary

This summary is machine-generated.

Modified LDL particles activate the complement system, a key factor in atherosclerosis. Cholesterol esterase-modified LDL (E-LDL) triggers complement component C1 activation via its C1q subunit sensing fatty acids.

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Measuring the 50% Haemolytic Complement (CH50) Activity of Serum

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Last Updated: Jun 2, 2026

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Measuring the 50% Haemolytic Complement (CH50) Activity of Serum

Measuring the 50% Haemolytic Complement (CH₅₀) Activity of Serum

Published on: March 29, 2010

Area of Science:

Immunology
Biochemistry
Cardiovascular Research

Background:

The complement system plays a role in the development of atherosclerosis.
Low-density lipoprotein (LDL) modifications are implicated in atherogenesis.

Purpose of the Study:

To investigate the interaction between native and modified LDL particles with complement component C1.
To determine how LDL modifications influence C1 activation.

Main Methods:

Studied binding and activation of C1 by native LDL, oxidized LDL (oxLDL), and enzymatically modified LDL (E-LDL).
Utilized lipid vesicle reconstitution, cosedimentation, and electron microscopy.
Identified the specific component of E-LDL recognized by C1q.

Main Results:

Both oxLDL and E-LDL bound to the C1q subunit of C1.
Only E-LDL activated C1, indicating a specific modification triggers the classical complement pathway.
C1q binding to E-LDL is mediated by its globular domain sensing unesterified fatty acids.

Conclusions:

Enzymatic modification of LDL, specifically generating unesterified fatty acids, is crucial for C1 activation.
These findings highlight a mechanism by which modified LDL can drive complement-mediated inflammation in atherogenesis.