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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...
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...
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...
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
Two...
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...

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Related Experiment Video

Updated: Jul 8, 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

Adiponectin binds C1q and activates the classical pathway of complement.

Philip W Peake1, Yvonne Shen, Alexandra Walther

  • 1Division of Medicine, Prince of Wales Hospital, High Street, Randwick, Sydney, NSW 2031, Australia.

Biochemical and Biophysical Research Communications
|January 9, 2008
PubMed
Summary
This summary is machine-generated.

Adiponectin binds to C1q, activating the complement system. This suggests adiponectin

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Last Updated: Jul 8, 2026

Evaluation of the Interplay Between the Complement Protein C1q and Hyaluronic Acid in Promoting Cell Adhesion
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Published on: May 19, 2020

Area of Science:

  • Immunology
  • Biochemistry

Background:

  • Adiponectin, an adipose-specific protein, binds to various targets like damaged endothelium and apoptotic cells.
  • The functional significance of adiponectin binding remains largely undetermined.

Purpose of the Study:

  • To investigate the interaction between adiponectin and C1q.
  • To elucidate the role of adiponectin in innate immunity and complement activation.

Main Methods:

  • Purified C1q binding assays with recombinant and serum-derived adiponectin.
  • Complement activation studies involving C4 and C3 deposition.
  • Western blotting and periodate treatment to assess binding characteristics.

Main Results:

  • Purified C1q binds to adiponectin under physiological conditions, dependent on Ca(++) and Mg(++).
  • Binding is enhanced by modification of adiponectin's sugars and involves the globular domain of C1q.
  • C1q binding to adiponectin triggers classical complement pathway activation, leading to C4 and C3 deposition.

Conclusions:

  • Adiponectin interacts with C1q, a key component of the complement system.
  • Adiponectin may function as a pattern-recognition molecule within the innate immune system.
  • This interaction suggests a novel role for adiponectin in immune responses and autoimmune conditions.