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Related Concept Videos

Complement System01:27

Complement System

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...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
Antibody Actions01:26

Antibody Actions

Antibodies, or immunoglobulins, are critical players in the immune system's arsenal against invading pathogens. Produced by B cells and plasma cells, their primary role is to detect and bind to specific antigens, molecules found on the surface of pathogens like bacteria or viruses. Beyond antigen recognition, antibodies perform several vital functions that contribute to immune defense.
Neutralization
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Receptor-mediated Endocytosis01:38

Receptor-mediated Endocytosis

Overview
Lipid-derived Compounds in the Human Body01:31

Lipid-derived Compounds in the Human Body

Fats and lipids are crucial components in the human body. Some lipid-derived compounds, such as fat-soluble vitamins, eicosanoids, lipoproteins, and glycolipids, also play unique roles to support various  biological processes .
Fat-soluble Vitamins
Fat-soluble vitamins, including vitamins A, D, E, and K, are required in minimal quantities, but their deficiencies can lead to severely abnormal physiological conditions. For example, vitamin A deficiency can cause night blindness, dry skin, delayed...
Selectins01:25

Selectins

Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...

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Related Experiment Video

Updated: Jul 20, 2026

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion
06:54

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

Published on: June 15, 2019

Modified low density lipoproteins differentially bind and activate the C1 complex of complement.

Adrienn Biró1, Nicole M Thielens, László Cervenák

  • 1IIIrd Department of Medicine, Research Laboratory, Semmelweis University, Budapest, Hungary.

Molecular Immunology
|August 30, 2006
PubMed
Summary

Enzymatically modified low-density lipoprotein (E-LDL) efficiently activates complement component C1, suggesting a key role in atherosclerosis development. Oxidized LDL (oxLDL) shows limited C1 activation, even with C-reactive protein.

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

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Last Updated: Jul 20, 2026

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion
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Published on: June 15, 2019

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Measuring the 50% Haemolytic Complement (CH50) Activity of Serum
08:26

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

Published on: March 29, 2010

Area of Science:

  • Immunology
  • Cardiovascular Biology
  • Biochemistry

Background:

  • Atherosclerosis pathogenesis involves complex inflammatory processes.
  • The complement system, particularly the classical pathway, is implicated in atherogenesis.
  • Low-density lipoprotein (LDL) modifications may influence complement activation.

Purpose of the Study:

  • To investigate the binding and C1 activation capabilities of native, oxidized (oxLDL), and enzymatically modified (E-LDL) LDL particles.
  • To determine the role of LDL modifications in initiating the classical complement pathway relevant to atherosclerosis.

Main Methods:

  • Preparation of native LDL, oxLDL, and E-LDL from commercial and purified sources.
  • Assays for C1 activation in the presence of C1 inhibitor.
  • Surface plasmon resonance (SPR) spectroscopy to measure C1q and C-reactive protein (CRP) binding affinities.

Main Results:

  • E-LDL efficiently triggered C1 activation (~60%) and bound C1q with high affinity (K(D)=58-75 nM).
  • Unmodified LDL and oxLDL did not activate C1 directly.
  • OxLDL was recognized by C1q, and one oxLDL preparation showed moderate C1 activation (~30%) with CRP.

Conclusions:

  • Enzymatically modified LDL (E-LDL) is a potent activator of the classical complement pathway under near-physiological conditions.
  • E-LDL-mediated complement activation represents a significant factor in atherosclerosis pathogenesis.
  • Direct C1 activation by oxLDL, with or without CRP, appears less likely in vivo.