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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...
Protein Complex Assembly02:41

Protein Complex Assembly

Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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
Antibodies can bind to pathogens, preventing them from infecting host cells. This process...
Hypersensitivity Reactions: Immune-Complex Reactions01:19

Hypersensitivity Reactions: Immune-Complex Reactions

Type III hypersensitivity reactions occur when antigen–antibody complexes form and activate the complement system. Normally, these complexes help the clearance of antigens by phagocytes and red blood cells. However, when large numbers of immune complexes are present, they can deposit in tissues—particularly in the walls of blood vessels—leading to inflammation and tissue injury. These deposits trigger complement activation and neutrophil recruitment, resulting in serum sickness, a systemic...
Ionic Association01:28

Ionic Association

The ionic association is the association of oppositely charged ions in an electrolyte solution to form ion pairs. Bjerrum defined ion pairs as two oppositely charged ions whose electrostatic attraction exceeds the thermal energy of the system, typically expressed as 2kT. Electrostatic attraction depends on ionic charge, separation distance, and the dielectric constant of the medium. Thermal energy, represented by kT, reflects the tendency of ions to move independently due to molecular motion.
Complexation Equilibria: The Chelate Effect01:19

Complexation Equilibria: The Chelate Effect

In complexation reactions, metal atoms or cations interact with ligands to form donor-acceptor adducts called metal complexes. Ligands that bind through one donor site are monodentate, ligands with two donor sites are bidentate, and those with more than two donor sites are polydentate ligands. For example, ethylene diamine is a bidentate ligand that binds through two nitrogen donor atoms, forming a five-membered ring. EDTA is a polydentate ligand that binds through four oxygen and two nitrogen...

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Related Experiment Video

Updated: Jun 26, 2026

Methods for Quantitative Detection of Antibody-induced Complement Activation on Red Blood Cells
06:29

Methods for Quantitative Detection of Antibody-induced Complement Activation on Red Blood Cells

Published on: January 29, 2014

Polyanion-induced self-association of complement factor H.

Michael K Pangburn1, Nenoo Rawal, Claudio Cortes

  • 1Department of Biochemistry, Center for Biomedical Research, University of Texas Health Science Center, Tyler, TX 75708, USA. michael.pangburn@uthct.edu

Journal of Immunology (Baltimore, Md. : 1950)
|January 7, 2009
PubMed
Summary
This summary is machine-generated.

Factor H regulates complement activation by binding to host cells. Polyanion interaction induces Factor H self-association into dimers and tetramers, enhancing its regulatory functions.

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Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
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Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

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Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry
05:58

Detecting and Characterizing Protein Self-Assembly In Vivo by Flow Cytometry

Published on: July 17, 2019

Area of Science:

  • Immunology
  • Biochemistry
  • Complement System

Background:

  • Factor H is the main regulator of the alternative complement pathway.
  • It prevents complement activation on host cells by binding to C3b and polyanions.

Purpose of the Study:

  • To investigate the effect of polyanions on Factor H structure and function.
  • To determine the mechanism of Factor H-mediated complement regulation.

Main Methods:

  • Gel filtration chromatography to assess Factor H size.
  • Analytical ultracentrifugation to determine Factor H molecular weight and oligomeric state.
  • Assays for decay accelerating and cofactor activity.

Main Results:

  • Polyanions induce Factor H self-association, forming dimers and tetramers.
  • Factor H exhibits an apparent size of 330,000 Da monomerically and up to 1,400,000 Da in the presence of polyanions.
  • Polyanion-induced self-association enhances Factor H's decay accelerating and cofactor activity.

Conclusions:

  • Factor H self-association, mediated by its C-terminal polyanion binding site, is crucial for its regulatory function.
  • The formation of Factor H dimers and tetramers is a key mechanism for recognizing and regulating complement activation on host cells.